You will find below the publication list of our pole.
For the publication list of each pole member, please see his/her personal webpage.
2020 |
Solubilization and Stabilization of Membrane Proteins by Cycloalkane-Modified Amphiphilic Polymers Article de journal Anaïs Marconnet; Baptiste Michon; Christel Le Bon; Fabrice Giusti; Christophe Tribet; Manuela Zoonens Biomacromolecules, 21 (8), p. 3459-3467, 2020, ISSN: 1525-7797. @article{Marconnet2020, title = {Solubilization and Stabilization of Membrane Proteins by Cycloalkane-Modified Amphiphilic Polymers}, author = {Ana\"{i}s Marconnet and Baptiste Michon and Christel Le Bon and Fabrice Giusti and Christophe Tribet and Manuela Zoonens }, editor = {American Chemical Society}, url = {https://doi.org/10.1021/acs.biomac.0c00929}, doi = {10.1021/acs.biomac.0c00929}, issn = {1525-7797}, year = {2020}, date = {2020-08-10}, journal = {Biomacromolecules}, volume = {21}, number = {8}, pages = {3459-3467}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
2019 |
A Fluorescent False Neurotransmitter as a Dual Electrofluorescent Probe for Secretory Cell Models Article de journal J Pandard; N Pan; D H Ebene; T Le Saux; E Ait-Yahiatène; X Liu; L Grimaud; O Buriez; E Labbé; F Lemaître; M Guille-Collignon ChemPlusChem, 84 (10), p. 1578-1586, 2019, (cited By 0). @article{Pandard20191578, title = {A Fluorescent False Neurotransmitter as a Dual Electrofluorescent Probe for Secretory Cell Models}, author = {J Pandard and N Pan and D H Ebene and T Le Saux and E Ait-Yahiat\`{e}ne and X Liu and L Grimaud and O Buriez and E Labb\'{e} and F Lema\^{i}tre and M Guille-Collignon}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85073931778&doi=10.1002%2fcplu.201900385&partnerID=40&md5=a526291d966e7dc926b44e97c73794b3}, doi = {10.1002/cplu.201900385}, year = {2019}, date = {2019-01-01}, journal = {ChemPlusChem}, volume = {84}, number = {10}, pages = {1578-1586}, note = {cited By 0}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
A Fluorescent False Neurotransmitter as a Dual Electrofluorescent Probe for Secretory Cell Models Article de journal Eric Labbe ChemPlusChem, 2019, ISSN: 2192-6506. @article{Eric_Labbe66937150, title = {A Fluorescent False Neurotransmitter as a Dual Electrofluorescent Probe for Secretory Cell Models}, author = {Eric Labbe}, url = {http://doi.org/10.1002/cplu.201900385}, doi = {10.1002/cplu.201900385}, issn = {2192-6506}, year = {2019}, date = {2019-01-01}, journal = {ChemPlusChem}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
A Fluorescent False Neurotransmitter as a Dual Electrofluorescent Probe for Secretory Cell Models Article de journal Eric Labbe ChemPlusChem, 2019, ISSN: 2192-6506. @article{Eric_Labbe66937150b, title = {A Fluorescent False Neurotransmitter as a Dual Electrofluorescent Probe for Secretory Cell Models}, author = {Eric Labbe}, url = {http://doi.org/10.1002/cplu.201900385}, doi = {10.1002/cplu.201900385}, issn = {2192-6506}, year = {2019}, date = {2019-01-01}, journal = {ChemPlusChem}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
A split fluorescent reporter with rapid and reversible complementation Article de journal Alison G Tebo; Arnaud Gautier Nature Communications, 10 (1), p. 2822, 2019, ISSN: 2041-1723. @article{Tebo2019, title = {A split fluorescent reporter with rapid and reversible complementation}, author = {Alison G Tebo and Arnaud Gautier}, url = {https://doi.org/10.1038/s41467-019-10855-0}, doi = {10.1038/s41467-019-10855-0}, issn = {2041-1723}, year = {2019}, date = {2019-01-01}, journal = {Nature Communications}, volume = {10}, number = {1}, pages = {2822}, abstract = {Interactions between proteins play an essential role in metabolic and signaling pathways, cellular processes and organismal systems. We report the development of splitFAST, a fluorescence complementation system for the visualization of transient protein-protein interactions in living cells. Engineered from the fluorogenic reporter FAST (Fluorescence-Activating and absorption-Shifting Tag), which specifically and reversibly binds fluorogenic hydroxybenzylidene rhodanine (HBR) analogs, splitFAST displays rapid and reversible complementation, allowing the real-time visualization of both the formation and the dissociation of a protein assembly.}, keywords = {}, pubstate = {published}, tppubtype = {article} } Interactions between proteins play an essential role in metabolic and signaling pathways, cellular processes and organismal systems. We report the development of splitFAST, a fluorescence complementation system for the visualization of transient protein-protein interactions in living cells. Engineered from the fluorogenic reporter FAST (Fluorescence-Activating and absorption-Shifting Tag), which specifically and reversibly binds fluorogenic hydroxybenzylidene rhodanine (HBR) analogs, splitFAST displays rapid and reversible complementation, allowing the real-time visualization of both the formation and the dissociation of a protein assembly. |
Bacteria-Based Production of Thiol-Clickable, Genetically Encoded Lipid Nanovesicles Article de journal Jorge Royes; Oana Ilioaia; Quentin Lubart; Federica Angius; Galina V Dubacheva; Marta Bally; Bruno Miroux; Christophe Tribet Angewandte Chemie International Edition, 58 , p. 7395-7399, 2019, ISSN: 1433-7851. @article{RN1x, title = {Bacteria-Based Production of Thiol-Clickable, Genetically Encoded Lipid Nanovesicles}, author = {Jorge Royes and Oana Ilioaia and Quentin Lubart and Federica Angius and Galina V Dubacheva and Marta Bally and Bruno Miroux and Christophe Tribet}, doi = {10.1002/anie.201902929}, issn = {1433-7851}, year = {2019}, date = {2019-01-01}, journal = {Angewandte Chemie International Edition}, volume = {58}, pages = {7395-7399}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Eric Labb é; Olivier Buriez ChemElectroChem, 6 (16), p. 4061–4061, 2019. @article{Labb__2019, title = {Cover Feature: Fundamental Input of Analytical Electrochemistry in the Determination of Intermediates and Reaction Mechanisms in Electrosynthetic Processes (ChemElectroChem 16/2019)}, author = {Eric Labb \'{e} and Olivier Buriez}, url = {https://doi.org/10.1002%2Fcelc.201901158}, doi = {10.1002/celc.201901158}, year = {2019}, date = {2019-07-01}, journal = {ChemElectroChem}, volume = {6}, number = {16}, pages = {4061--4061}, publisher = {Wiley}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Distinctive Low-Resolution Structural Features of Dimers of Antibody–Drug Conjugates and Parent Antibody Determined by Small-Angle X-ray Scattering Article de journal Didier Law-Hine; Sergii Rudiuk; Audrey Bonestebe; Romain Ienco; Sylvain Huille; Christophe Tribet Mol. Pharmaceutics, 16 (12), p. 4902-4912, 2019. @article{Law-Hine2019, title = {Distinctive Low-Resolution Structural Features of Dimers of Antibody\textendashDrug Conjugates and Parent Antibody Determined by Small-Angle X-ray Scattering}, author = {Didier Law-Hine and Sergii Rudiuk and Audrey Bonestebe and Romain Ienco and Sylvain Huille and Christophe Tribet}, doi = {10.1021/acs.molpharmaceut.9b00792}, year = {2019}, date = {2019-10-16}, journal = {Mol. Pharmaceutics}, volume = {16}, number = {12}, pages = {4902-4912}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Diverting photosynthetic electrons from suspensions of Chlamydomonas reinhardtii algae - New insights using an electrochemical well device Article de journal A Sayegh; G Longatte; O Buriez; F -A Wollman; M Guille-Collignon; E Labbé; J Delacotte; F Lemaître Electrochimica Acta, 304 , p. 465 - 473, 2019, ISSN: 0013-4686. @article{SAYEGH2019465, title = {Diverting photosynthetic electrons from suspensions of Chlamydomonas reinhardtii algae - New insights using an electrochemical well device}, author = {A Sayegh and G Longatte and O Buriez and F -A Wollman and M Guille-Collignon and E Labb\'{e} and J Delacotte and F Lema\^{i}tre}, url = {http://www.sciencedirect.com/science/article/pii/S0013468619303718}, doi = {https://doi.org/10.1016/j.electacta.2019.02.105}, issn = {0013-4686}, year = {2019}, date = {2019-01-01}, journal = {Electrochimica Acta}, volume = {304}, pages = {465 - 473}, abstract = {In the last years, many strategies have been developed to benefit from oxygenic photosynthesis in the present context of renewable energies. To achieve this, bioelectricity may be produced by using photosynthetic components involved in anodic or cathodic compartments. In this respect, harvesting photosynthetic electrons from living biological systems appears to be an encouraging approach. However it raises the question of the most suitable electrochemical device. In this work, we describe and analyze the performances of an electrochemical device based on a millimeter sized well involving a gold surface as a working electrode. Photocurrents were generated by suspensions of Chlamydomonas reinhardtii algae using quinones as mediators under different experimental conditions. Chronoamperometry and cyclic voltammetry measurements gave insight into the use of this device to investigate important issues (harvesting and poisoning by quinones, photoinactivation…). Furthermore, by introducing a kinetic model originally developed for homogeneous catalytic systems, the kinetics of the electron diverting from this system (Chlamydomonas reinhardtii algae + 2,6-DCBQ + miniaturized setup) can be estimated. All these results demonstrate that this experimental configuration is suitable for future works devoted to the choice of the best parameters in terms of long lasting performances.}, keywords = {}, pubstate = {published}, tppubtype = {article} } In the last years, many strategies have been developed to benefit from oxygenic photosynthesis in the present context of renewable energies. To achieve this, bioelectricity may be produced by using photosynthetic components involved in anodic or cathodic compartments. In this respect, harvesting photosynthetic electrons from living biological systems appears to be an encouraging approach. However it raises the question of the most suitable electrochemical device. In this work, we describe and analyze the performances of an electrochemical device based on a millimeter sized well involving a gold surface as a working electrode. Photocurrents were generated by suspensions of Chlamydomonas reinhardtii algae using quinones as mediators under different experimental conditions. Chronoamperometry and cyclic voltammetry measurements gave insight into the use of this device to investigate important issues (harvesting and poisoning by quinones, photoinactivation…). Furthermore, by introducing a kinetic model originally developed for homogeneous catalytic systems, the kinetics of the electron diverting from this system (Chlamydomonas reinhardtii algae + 2,6-DCBQ + miniaturized setup) can be estimated. All these results demonstrate that this experimental configuration is suitable for future works devoted to the choice of the best parameters in terms of long lasting performances. |
Electroactive fluorescent false neurotransmitter FFN102 partially replaces dopamine in PC12 cell vesicles Article de journal L Hu; A Savy; L Grimaud; M Guille-Collignon; F Lemaître; C Amatore; J Delacotte Biophysical Chemistry, 245 , p. 1–5, 2019. @article{Hu:2019, title = {Electroactive fluorescent false neurotransmitter FFN102 partially replaces dopamine in PC12 cell vesicles}, author = {L Hu and A Savy and L Grimaud and M Guille-Collignon and F Lema\^{i}tre and C Amatore and J Delacotte}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85057201704&doi=10.1016%2fj.bpc.2018.11.001&partnerID=40&md5=28655b4c152ce0fc51fc037feefcff97}, doi = {10.1016/j.bpc.2018.11.001}, year = {2019}, date = {2019-01-01}, journal = {Biophysical Chemistry}, volume = {245}, pages = {1--5}, abstract = {In the last decade, following fluorescent dyes and protein tags, pH sensitive false fluorescent neurotransmitters (FFN) were introduced and were valuable for labeling secretory vesicles and monitoring exocytosis at living cells. In particular, the synthetic analog of neurotransmitters FFN102 was shown to be an electroactive probe. Here, we show that FFN102 is suitable to be used as a bioanalytic probe at the widely used PC12 cell model. FFN102 was uptaken in the secretory vesicles of PC12 cells, partially replacing the endogenous dopamine stored in these vesicles. The different oxidation potentials of dopamine and FFN102 allowed to determine that ca. 12% of dopamine was replaced by FFN102. Moreover, the FFN102 was found to be over released through the initial fusion pore suggesting that it was mostly uptaken in fast diffusion compartment of the vesicles. © 2018 Elsevier B.V.}, keywords = {}, pubstate = {published}, tppubtype = {article} } In the last decade, following fluorescent dyes and protein tags, pH sensitive false fluorescent neurotransmitters (FFN) were introduced and were valuable for labeling secretory vesicles and monitoring exocytosis at living cells. In particular, the synthetic analog of neurotransmitters FFN102 was shown to be an electroactive probe. Here, we show that FFN102 is suitable to be used as a bioanalytic probe at the widely used PC12 cell model. FFN102 was uptaken in the secretory vesicles of PC12 cells, partially replacing the endogenous dopamine stored in these vesicles. The different oxidation potentials of dopamine and FFN102 allowed to determine that ca. 12% of dopamine was replaced by FFN102. Moreover, the FFN102 was found to be over released through the initial fusion pore suggesting that it was mostly uptaken in fast diffusion compartment of the vesicles. © 2018 Elsevier B.V. |
Fundamental Input of Analytical Electrochemistry in the Determination of Intermediates and Reaction Mechanisms in Electrosynthetic Processes Article de journal E Labbé; O Buriez ChemElectroChem, 6 (16), p. 4118-4125, 2019, (cited By 1). @article{Labb\'{e}20194118, title = {Fundamental Input of Analytical Electrochemistry in the Determination of Intermediates and Reaction Mechanisms in Electrosynthetic Processes}, author = {E Labb\'{e} and O Buriez}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85063908009&doi=10.1002%2fcelc.201900045&partnerID=40&md5=be86c0958f347ea6b4d1d62a0526e44c}, doi = {10.1002/celc.201900045}, year = {2019}, date = {2019-01-01}, journal = {ChemElectroChem}, volume = {6}, number = {16}, pages = {4118-4125}, note = {cited By 1}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Fundamental Input of Analytical Electrochemistry in the Determination of Intermediates and Reaction Mechanisms in Electrosynthetic Processes Article de journal Eric Labbe ChemElectroChem, 2019, ISSN: 2196-0216. @article{Eric_Labbe66937107, title = {Fundamental Input of Analytical Electrochemistry in the Determination of Intermediates and Reaction Mechanisms in Electrosynthetic Processes}, author = {Eric Labbe}, url = {http://doi.org/10.1002/celc.201900045}, doi = {10.1002/celc.201900045}, issn = {2196-0216}, year = {2019}, date = {2019-01-01}, journal = {ChemElectroChem}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Fundamental Input of Analytical Electrochemistry in the Determination of Intermediates and Reaction Mechanisms in Electrosynthetic Processes Article de journal Eric Labbe ChemElectroChem, 2019, ISSN: 2196-0216. @article{Eric_Labbe66937107b, title = {Fundamental Input of Analytical Electrochemistry in the Determination of Intermediates and Reaction Mechanisms in Electrosynthetic Processes}, author = {Eric Labbe}, url = {http://doi.org/10.1002/celc.201900045}, doi = {10.1002/celc.201900045}, issn = {2196-0216}, year = {2019}, date = {2019-01-01}, journal = {ChemElectroChem}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Live Cell Super Resolution Imaging by Radial Fluctuations Using Fluorogen Binding Tags Article de journal Muthukumaran Venkatachalapathy; Vivek Belapurkar; Mini Jose; Arnaud Gautier; Deepak Nair Nanoscale, 11 (8), p. 3626-3632, 2019, ISSN: 2040-3364. @article{RN45, title = {Live Cell Super Resolution Imaging by Radial Fluctuations Using Fluorogen Binding Tags}, author = {Muthukumaran Venkatachalapathy and Vivek Belapurkar and Mini Jose and Arnaud Gautier and Deepak Nair}, doi = {10.1039/C8NR07809B}, issn = {2040-3364}, year = {2019}, date = {2019-01-01}, journal = {Nanoscale}, volume = {11}, number = {8}, pages = {3626-3632}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Nanoparticle-based local translation reveals mRNA as a translation-coupled scaffold with anchoring function Article de journal Shunnichi Kashida; Dan Ohtan Wang; Hirohide Saito; Zoher Gueroui Proceedings of the National Academy of Sciences of the United States of America, 2019, ISSN: 10916490. @article{Kashida2019, title = {Nanoparticle-based local translation reveals mRNA as a translation-coupled scaffold with anchoring function}, author = {Shunnichi Kashida and Dan Ohtan Wang and Hirohide Saito and Zoher Gueroui}, doi = {10.1073/pnas.1900310116}, issn = {10916490}, year = {2019}, date = {2019-01-01}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, abstract = {The spatial regulation of messenger RNA (mRNA) translation is central to cellular functions and relies on numerous complex processes. Biomimetic approaches could bypass these endogenous complex processes, improve our comprehension of the regulation, and allow for controlling local translation regulations and functions. However, the causality between local translation and nascent protein function remains elusive. Here, we developed a nanoparticle (NP)-based strategy to magnetically control mRNA spatial patterns in mammalian cell extracts and investigate how local translation impacts nascent protein localization and function. By monitoring the translation of the magnetically localized mRNAs, we show that mRNA\textendashNP complexes operate as a source for the continuous production of proteins from defined positions. By applying this approach to actin-binding proteins, we triggered the local formation of actin cytoskeletons and identified the minimal requirements for spatial control of the actin filament network. In addition, our bottom-up approach identified a role for mRNA as a translation-coupled scaffold for the function of nascent N-terminal protein domains. Our approach will serve as a platform for regulating mRNA localization and investigating the function of nascent protein domains during translation.}, keywords = {}, pubstate = {published}, tppubtype = {article} } The spatial regulation of messenger RNA (mRNA) translation is central to cellular functions and relies on numerous complex processes. Biomimetic approaches could bypass these endogenous complex processes, improve our comprehension of the regulation, and allow for controlling local translation regulations and functions. However, the causality between local translation and nascent protein function remains elusive. Here, we developed a nanoparticle (NP)-based strategy to magnetically control mRNA spatial patterns in mammalian cell extracts and investigate how local translation impacts nascent protein localization and function. By monitoring the translation of the magnetically localized mRNAs, we show that mRNA–NP complexes operate as a source for the continuous production of proteins from defined positions. By applying this approach to actin-binding proteins, we triggered the local formation of actin cytoskeletons and identified the minimal requirements for spatial control of the actin filament network. In addition, our bottom-up approach identified a role for mRNA as a translation-coupled scaffold for the function of nascent N-terminal protein domains. Our approach will serve as a platform for regulating mRNA localization and investigating the function of nascent protein domains during translation. |
New Mechanistic Insights into Osmium-Based Tamoxifen Derivatives Article de journal H Z S Lee; F Chau; S Top; G Jaouen; A Vessieres; E Labbe; O Buriez Electrochimica Acta, 302 , p. 130-136, 2019, ISSN: 0013-4686. @article{RN52, title = {New Mechanistic Insights into Osmium-Based Tamoxifen Derivatives}, author = {H Z S Lee and F Chau and S Top and G Jaouen and A Vessieres and E Labbe and O Buriez}, doi = {10.1016/j.electacta.2019.02.019}, issn = {0013-4686}, year = {2019}, date = {2019-01-01}, journal = {Electrochimica Acta}, volume = {302}, pages = {130-136}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Photosensitized oxidative addition to gold(i) enables alkynylative cyclization of o-alkylnylphenols with iodoalkynes Article de journal Zhonghua Xia; Vincent Corcé; Fen Zhao; Cédric Przybylski; Agathe Espagne; Ludovic Jullien; Thomas Le Saux; Yves Gimbert; Héloïse Dossmann; Virginie Mouriès-Mansuy; Cyril Ollivier; Louis Fensterbank Nature Chemistry, 11 (9), p. 797-805, 2019, ISSN: 1755-4349. @article{RN1_28, title = {Photosensitized oxidative addition to gold(i) enables alkynylative cyclization of o-alkylnylphenols with iodoalkynes}, author = {Zhonghua Xia and Vincent Corc\'{e} and Fen Zhao and C\'{e}dric Przybylski and Agathe Espagne and Ludovic Jullien and Thomas Le Saux and Yves Gimbert and H\'{e}lo\"{i}se Dossmann and Virginie Mouri\`{e}s-Mansuy and Cyril Ollivier and Louis Fensterbank}, url = {https://doi.org/10.1038/s41557-019-0295-9}, doi = {10.1038/s41557-019-0295-9}, issn = {1755-4349}, year = {2019}, date = {2019-01-01}, journal = {Nature Chemistry}, volume = {11}, number = {9}, pages = {797-805}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Redox-Triggered Control of Cell Adhesion and Deadhesion on Poly(lysine)-g-poly(ethylene oxide) Adlayers. Article de journal Louise Hespel; Julien Dupré de Baubigny; Pierre Lalanne; Simon de Beco; Mathieu Coppey; Catherine Villard; Vincent Humblot; Emmanuelle Marie; Christophe Tribet ACS Applied Bio Materials, 2 (10), p. 4367-4376, 2019. @article{Hespel2019, title = {Redox-Triggered Control of Cell Adhesion and Deadhesion on Poly(lysine)-g-poly(ethylene oxide) Adlayers.}, author = {Louise Hespel and Julien Dupr\'{e} de Baubigny and Pierre Lalanne and Simon de Beco and Mathieu Coppey and Catherine Villard and Vincent Humblot and Emmanuelle Marie and Christophe Tribet}, doi = {10.1021/acsabm.9b00601}, year = {2019}, date = {2019-09-10}, journal = {ACS Applied Bio Materials}, volume = {2}, number = {10}, pages = {4367-4376}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
RNA is a critical element for the sizing and the composition of phase-separated RNA–protein condensates Article de journal Marina Garcia-Jove Navarro; Shunnichi Kashida; Racha Chouaib; Sylvie Souquere; Gérard Pierron; Dominique Weil; Zoher Gueroui Nature Communications, 2019, ISSN: 2041-1723. @article{Garcia-JoveNavarro2019, title = {RNA is a critical element for the sizing and the composition of phase-separated RNA\textendashprotein condensates}, author = {Marina {Garcia-Jove Navarro} and Shunnichi Kashida and Racha Chouaib and Sylvie Souquere and G\'{e}rard Pierron and Dominique Weil and Zoher Gueroui}, doi = {10.1038/s41467-019-11241-6}, issn = {2041-1723}, year = {2019}, date = {2019-01-01}, journal = {Nature Communications}, abstract = {Liquid-liquid phase separation is thought to be a key organizing principle in eukaryotic cells to generate highly concentrated dynamic assemblies, such as the RNP granules. Numerous in vitro approaches have validated this model, yet a missing aspect is to take into consideration the complex molecular mixture and promiscuous interactions found in vivo. Here we report the versatile scaffold "ArtiG" to generate concentration-dependent RNA-protein condensates within living cells, as a bottom-up approach to study the impact of co-segregated endogenous components on phase separation. We demonstrate that intracellular RNA seeds the nucleation of the condensates, as it provides molecular cues to locally coordinate the formation of endogenous high order RNP assemblies. Interestingly, the co-segregation of intracellular components ultimately impacts the size of the phase-separated condensates. Thus, RNA arises as an architectural element that can influence the composition and the morphological outcome of the condensate phases in an intracellular context.}, keywords = {}, pubstate = {published}, tppubtype = {article} } Liquid-liquid phase separation is thought to be a key organizing principle in eukaryotic cells to generate highly concentrated dynamic assemblies, such as the RNP granules. Numerous in vitro approaches have validated this model, yet a missing aspect is to take into consideration the complex molecular mixture and promiscuous interactions found in vivo. Here we report the versatile scaffold "ArtiG" to generate concentration-dependent RNA-protein condensates within living cells, as a bottom-up approach to study the impact of co-segregated endogenous components on phase separation. We demonstrate that intracellular RNA seeds the nucleation of the condensates, as it provides molecular cues to locally coordinate the formation of endogenous high order RNP assemblies. Interestingly, the co-segregation of intracellular components ultimately impacts the size of the phase-separated condensates. Thus, RNA arises as an architectural element that can influence the composition and the morphological outcome of the condensate phases in an intracellular context. |
Self-aggregation of oxidized procyanidins contributes to the formation of heat-reversible haze in apple-based liqueur wine Article de journal M Millet; P Poupard; S Guilois-Dubois; D Zanchi; S Guyot Food Chemistry, 276 , p. 797–805, 2019. @article{Millet:2019, title = {Self-aggregation of oxidized procyanidins contributes to the formation of heat-reversible haze in apple-based liqueur wine}, author = {M Millet and P Poupard and S Guilois-Dubois and D Zanchi and S Guyot}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85055330959&doi=10.1016%2fj.foodchem.2018.09.171&partnerID=40&md5=023402dcebfde4b3a1f3f506c5b74529}, doi = {10.1016/j.foodchem.2018.09.171}, year = {2019}, date = {2019-01-01}, journal = {Food Chemistry}, volume = {276}, pages = {797--805}, abstract = {The ability of tannins to self-associate or form complexes with other macromolecules has important nutritional implications but can also result in defects in beverages. In addition, oxidation may be involved in the aggregation properties of tannins. In order to assess the impact of tannin oxidation on their self-association, oligomeric procyanidins were oxidized in a model solution and their aggregation kinetics were studied using light scattering. Under the conditions tested, only oxidized procyanidins were involved in haze formation. An increase in the level of oxidation and the degree of polymerization of procyanidins enhanced aggregation. Procyanidin oxidation products were depolymerized and the evolution of their markers was monitored throughout the aggregation process using liquid chromatography coupled with mass spectrometry. This revealed the involvement of intramolecular coupling in reversible haze formation. The haze formed in a model solution was partially reversible at high temperature. This property was similar in pommeau, an apple-based beverage. This work highlighted the involvement of oxidized tannins in reversible haze. © 2018 Elsevier Ltd}, keywords = {}, pubstate = {published}, tppubtype = {article} } The ability of tannins to self-associate or form complexes with other macromolecules has important nutritional implications but can also result in defects in beverages. In addition, oxidation may be involved in the aggregation properties of tannins. In order to assess the impact of tannin oxidation on their self-association, oligomeric procyanidins were oxidized in a model solution and their aggregation kinetics were studied using light scattering. Under the conditions tested, only oxidized procyanidins were involved in haze formation. An increase in the level of oxidation and the degree of polymerization of procyanidins enhanced aggregation. Procyanidin oxidation products were depolymerized and the evolution of their markers was monitored throughout the aggregation process using liquid chromatography coupled with mass spectrometry. This revealed the involvement of intramolecular coupling in reversible haze formation. The haze formed in a model solution was partially reversible at high temperature. This property was similar in pommeau, an apple-based beverage. This work highlighted the involvement of oxidized tannins in reversible haze. © 2018 Elsevier Ltd |
Single-Molecule Localization Microscopy with the Fluorescence-Activating and Absorption-Shifting Tag (FAST) System Article de journal Elizabeth M Smith; Arnaud Gautier; Elias M Puchner ACS Chemical Biology, 14 (6), p. 1115-1120, 2019, ISSN: 1554-8929. @article{Smith2019, title = {Single-Molecule Localization Microscopy with the Fluorescence-Activating and Absorption-Shifting Tag (FAST) System}, author = {Elizabeth M Smith and Arnaud Gautier and Elias M Puchner}, url = {https://doi.org/10.1021/acschembio.9b00149}, doi = {10.1021/acschembio.9b00149}, issn = {1554-8929}, year = {2019}, date = {2019-06-21}, journal = {ACS Chemical Biology}, volume = {14}, number = {6}, pages = {1115-1120}, publisher = {American Chemical Society}, abstract = {We develop and employ the Fluorescence-Activating and absorption-Shifting Tag (FAST) system for super-resolution (SR) imaging and single-molecule tracking based on single-molecule localizations. The fast off rate of fluorogen binding, combined with its spatially well-separated labeling of the densely expressed FAST fusion proteins, allowed single-molecule measurements to be performed in both living and fixed cells. The well-separated fluorescence localization density was achieved by either reversibly controlling the fluorogen concentration or by irreversibly photobleaching the FAST-fluorogen complex. The experimentally determined resolution of 28 nm allowed us to resolve Ensconsin-labeled microtubules and to track single molecules in mitochondria. Our results demonstrate that FAST is well-suited for single-molecule localization microscopy (SMLM). The small size and the availability of spectrally distinct fluorogens present unique advantages of the FAST system as a potential orthogonal labeling strategy that could be applied in conjunction with existing super-resolution dyes and photoactivatable proteins in versatile imaging applications.}, keywords = {}, pubstate = {published}, tppubtype = {article} } We develop and employ the Fluorescence-Activating and absorption-Shifting Tag (FAST) system for super-resolution (SR) imaging and single-molecule tracking based on single-molecule localizations. The fast off rate of fluorogen binding, combined with its spatially well-separated labeling of the densely expressed FAST fusion proteins, allowed single-molecule measurements to be performed in both living and fixed cells. The well-separated fluorescence localization density was achieved by either reversibly controlling the fluorogen concentration or by irreversibly photobleaching the FAST-fluorogen complex. The experimentally determined resolution of 28 nm allowed us to resolve Ensconsin-labeled microtubules and to track single molecules in mitochondria. Our results demonstrate that FAST is well-suited for single-molecule localization microscopy (SMLM). The small size and the availability of spectrally distinct fluorogens present unique advantages of the FAST system as a potential orthogonal labeling strategy that could be applied in conjunction with existing super-resolution dyes and photoactivatable proteins in versatile imaging applications. |
The Glowing Panoply of Fluorogen-based Markers for Advanced Bioimaging Book Chapter A Gautier The Glowing Panoply of Fluorogen-based Markers for Advanced Bioimaging, Chapitre 3, 2019. @inbook{Gautier:2019, title = {The Glowing Panoply of Fluorogen-based Markers for Advanced Bioimaging}, author = {A Gautier}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85056600039&doi=10.1039%2f9781788013284-00041&partnerID=40&md5=5d754dc76f6a9652835200ef4214a41a}, doi = {10.1039/9781788013284-00041}, year = {2019}, date = {2019-01-01}, booktitle = {The Glowing Panoply of Fluorogen-based Markers for Advanced Bioimaging}, chapter = {3}, series = {Comprehensive Series in Photochemical and Photobiological Sciences}, abstract = {The biological sciences nowadays rely extensively on imaging tools to decipher the complexity of living organisms. Fluorescence microscopy allows the study of biological processes with unprecedented temporal and spatial resolution. The revolution in fluorescence imaging has been the development of a large toolbox of fluorescent proteins able to reveal the abundance, position and dynamics of proteins. The fluorescence toolbox has recently been expanded with innovative reporters that permit proteins, and other biomolecules such as RNA, to be visualized in new ways. These innovative reporters are bipartite systems composed of a genetically encoded tag forming a fluorescent complex with a small organic fluorogenic chromophore (also called fluorogens). This chapter is a user-oriented presentation of some of the most mature fluorogen-based markers available to biologists. © 2019 European Society for Photobiology.}, keywords = {}, pubstate = {published}, tppubtype = {inbook} } The biological sciences nowadays rely extensively on imaging tools to decipher the complexity of living organisms. Fluorescence microscopy allows the study of biological processes with unprecedented temporal and spatial resolution. The revolution in fluorescence imaging has been the development of a large toolbox of fluorescent proteins able to reveal the abundance, position and dynamics of proteins. The fluorescence toolbox has recently been expanded with innovative reporters that permit proteins, and other biomolecules such as RNA, to be visualized in new ways. These innovative reporters are bipartite systems composed of a genetically encoded tag forming a fluorescent complex with a small organic fluorogenic chromophore (also called fluorogens). This chapter is a user-oriented presentation of some of the most mature fluorogen-based markers available to biologists. © 2019 European Society for Photobiology. |
Tunable and switchable soft adsorption of polymer-coated microparticles on a flat substrate Article de journal Giuseppe Boniello; Christophe Tribet; Emmanuelle Marie; Vincent Croquette; Dražen Zanchi Colloids and Surfaces A: Physicochemical and Engineering Aspects, 575 , p. 199-204, 2019, ISSN: 0927-7757. @article{Boniello2019, title = {Tunable and switchable soft adsorption of polymer-coated microparticles on a flat substrate}, author = {Giuseppe Boniello and Christophe Tribet and Emmanuelle Marie and Vincent Croquette and Dra\v{z}en Zanchi}, editor = {Elsevier}, url = {http://www.sciencedirect.com/science/article/pii/S0927775719301797}, doi = {10.1016/j.colsurfa.2019.04.081}, issn = {0927-7757}, year = {2019}, date = {2019-08-20}, journal = {Colloids and Surfaces A: Physicochemical and Engineering Aspects}, volume = {575}, pages = {199-204}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Ultrafast Oxidation of a Tyrosine by Proton-Coupled Electron Transfer Promotes Light Activation of an Animal-like Cryptochrome Article de journal Fabien Lacombat; Agathe Espagne; Nadia Dozova; Pascal Plaza; Pavel Müller; Klaus Brettel; Sophie Franz-Badur; Lars-Oliver Essen Journal of the American Chemical Society, 141 (34), p. 13394-13409, 2019, ISSN: 0002-7863. @article{RN479, title = {Ultrafast Oxidation of a Tyrosine by Proton-Coupled Electron Transfer Promotes Light Activation of an Animal-like Cryptochrome}, author = {Fabien Lacombat and Agathe Espagne and Nadia Dozova and Pascal Plaza and Pavel M\"{u}ller and Klaus Brettel and Sophie Franz-Badur and Lars-Oliver Essen}, url = {https://doi.org/10.1021/jacs.9b03680}, doi = {10.1021/jacs.9b03680}, issn = {0002-7863}, year = {2019}, date = {2019-01-01}, journal = {Journal of the American Chemical Society}, volume = {141}, number = {34}, pages = {13394-13409}, abstract = {The animal-like cryptochrome of Chlamydomonas reinhardtii (CraCRY) is a recently discovered photoreceptor that controls the transcriptional profile and sexual life cycle of this alga by both blue and red light. CraCRY has the uncommon feature of efficient formation and longevity of the semireduced neutral form of its FAD cofactor upon blue light illumination. Tyrosine Y373 plays a crucial role by elongating , as fourth member, the electron transfer (ET) chain found in most other cryptochromes and DNA photolyases, which comprises a conserved tryptophan triad. Here, we report the full mechanism of light-induced FADH• formation in CraCRY using transient absorption spectroscopy from hundreds of femtoseconds to seconds. Electron transfer starts from ultrafast reduction of excited FAD to FAD•\textendash by the proximal tryptophan (0.4 ps) and is followed by delocalized migration of the produced WH•+ radical along the tryptophan triad (∼4 and ∼50 ps). Oxidation of Y373 by coupled ET to WH•+ and deprotonation then proceeds in ∼800 ps, without any significant kinetic isotope effect, nor a pH effect between pH 6.5 and 9.0. The FAD•\textendash/Y373• pair is formed with high quantum yield (∼60%); its intrinsic decay by recombination is slow (∼50 ms), favoring reduction of Y373• by extrinsic agents and protonation of FAD•\textendash to form the long-lived, red-light absorbing FADH• species. Possible mechanisms of tyrosine oxidation by ultrafast proton-coupled ET in CraCRY, a process about 40 times faster than the archetypal tyrosine-Z oxidation in photosystem II, are discussed in detail.}, keywords = {}, pubstate = {published}, tppubtype = {article} } The animal-like cryptochrome of Chlamydomonas reinhardtii (CraCRY) is a recently discovered photoreceptor that controls the transcriptional profile and sexual life cycle of this alga by both blue and red light. CraCRY has the uncommon feature of efficient formation and longevity of the semireduced neutral form of its FAD cofactor upon blue light illumination. Tyrosine Y373 plays a crucial role by elongating , as fourth member, the electron transfer (ET) chain found in most other cryptochromes and DNA photolyases, which comprises a conserved tryptophan triad. Here, we report the full mechanism of light-induced FADH• formation in CraCRY using transient absorption spectroscopy from hundreds of femtoseconds to seconds. Electron transfer starts from ultrafast reduction of excited FAD to FAD•– by the proximal tryptophan (0.4 ps) and is followed by delocalized migration of the produced WH•+ radical along the tryptophan triad (∼4 and ∼50 ps). Oxidation of Y373 by coupled ET to WH•+ and deprotonation then proceeds in ∼800 ps, without any significant kinetic isotope effect, nor a pH effect between pH 6.5 and 9.0. The FAD•–/Y373• pair is formed with high quantum yield (∼60%); its intrinsic decay by recombination is slow (∼50 ms), favoring reduction of Y373• by extrinsic agents and protonation of FAD•– to form the long-lived, red-light absorbing FADH• species. Possible mechanisms of tyrosine oxidation by ultrafast proton-coupled ET in CraCRY, a process about 40 times faster than the archetypal tyrosine-Z oxidation in photosystem II, are discussed in detail. |
Ultrafast photoinduced flavin dynamics in the unusual active site of the tRNA methyltransferase TrmFO Article de journal N Dozova; F Lacombat; C Bou-Nader; D Hamdane; P Plaza Physical Chemistry Chemical Physics, 21 (17), p. 8743-8756, 2019, ISSN: 1463-9076. @article{RN115, title = {Ultrafast photoinduced flavin dynamics in the unusual active site of the tRNA methyltransferase TrmFO}, author = {N Dozova and F Lacombat and C Bou-Nader and D Hamdane and P Plaza}, doi = {10.1039/c8cp06072j}, issn = {1463-9076}, year = {2019}, date = {2019-01-01}, journal = {Physical Chemistry Chemical Physics}, volume = {21}, number = {17}, pages = {8743-8756}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
2018 |
A chemically encoded timer for dual molecular delivery at tailored ranges and concentrations Article de journal S Serra; A Alouane; T Le Saux; S Huvelle; R Plasson; F Schmidt; L Jullien; R Labruère Chemical Communications, 54 (49), p. 6396–6399, 2018. @article{Serra:2018, title = {A chemically encoded timer for dual molecular delivery at tailored ranges and concentrations}, author = {S Serra and A Alouane and T Le Saux and S Huvelle and R Plasson and F Schmidt and L Jullien and R Labru\`{e}re}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85048683206&doi=10.1039%2fc8cc03253j&partnerID=40&md5=6b7d3eaf2fac02d48f0cfa34e3b730b9}, doi = {10.1039/c8cc03253j}, year = {2018}, date = {2018-01-01}, journal = {Chemical Communications}, volume = {54}, number = {49}, pages = {6396--6399}, abstract = {Spatiotemporal control of molecular distribution is much in demand in many fields of chemistry. To address this goal, we exploit a low molecular weight branched self-immolative architecture, which acts as a triggerable chemically encoded timer for autonomous sequential release of two chemicals. Using a light-activated model liberating two distinct fluorophores, we generated a tunable spatially contrasted molecular distribution. © 2018 The Royal Society of Chemistry.}, keywords = {}, pubstate = {published}, tppubtype = {article} } Spatiotemporal control of molecular distribution is much in demand in many fields of chemistry. To address this goal, we exploit a low molecular weight branched self-immolative architecture, which acts as a triggerable chemically encoded timer for autonomous sequential release of two chemicals. Using a light-activated model liberating two distinct fluorophores, we generated a tunable spatially contrasted molecular distribution. © 2018 The Royal Society of Chemistry. |
A novel diarylethene-based photoswitchable chelator for reversible release and capture of Ca2+ in aqueous media Article de journal N Dozova; G Pousse; B Barnych; J -M Mallet; J Cossy; B Valeur; P Plaza Journal of Photochemistry and Photobiology A: Chemistry, 360 , p. 181–187, 2018. @article{Dozova:2018, title = {A novel diarylethene-based photoswitchable chelator for reversible release and capture of Ca2+ in aqueous media}, author = {N Dozova and G Pousse and B Barnych and J -M Mallet and J Cossy and B Valeur and P Plaza}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85046375200&doi=10.1016%2fj.jphotochem.2018.04.029&partnerID=40&md5=acfff9bc55e2d0bb41580e84374018fc}, doi = {10.1016/j.jphotochem.2018.04.029}, year = {2018}, date = {2018-01-01}, journal = {Journal of Photochemistry and Photobiology A: Chemistry}, volume = {360}, pages = {181--187}, abstract = {The synthesis and characterisation of a novel Reversibly Photoswitchable Chelator (RPC) of calcium ions, designed as a stepping stone towards producing pulses of calcium concentration in an aqueous environment, is reported. This RPC is constituted of a photochromic diarylethene core connected on one side to a BAPTA (1,2-bis(2-aminophenoxy)ethane-N,N,N’,N’-tetraacetic acid) calcium chelator and, on the other side, to an electron-withdrawing group. The operation principle consists in photoswitching on and off an intramolecular charge transfer between one nitrogen atom of the BAPTA moiety and the electron-withdrawing group, thereby modulating the chelating affinity of BAPTA for calcium ions. Solubility of the compound in a partially aqueous solvent was achieved by grafting a short PEG (polyethylene glycol) tail to the electron-withdrawing group. A reduction of the affinity for calcium ions upon photoswitching by a factor of 3\textendash4, in the hundred nM range of dissociation constant, is reported and constitutes a proof of concept of this type of RPC. © 2018 Elsevier B.V.}, keywords = {}, pubstate = {published}, tppubtype = {article} } The synthesis and characterisation of a novel Reversibly Photoswitchable Chelator (RPC) of calcium ions, designed as a stepping stone towards producing pulses of calcium concentration in an aqueous environment, is reported. This RPC is constituted of a photochromic diarylethene core connected on one side to a BAPTA (1,2-bis(2-aminophenoxy)ethane-N,N,N’,N’-tetraacetic acid) calcium chelator and, on the other side, to an electron-withdrawing group. The operation principle consists in photoswitching on and off an intramolecular charge transfer between one nitrogen atom of the BAPTA moiety and the electron-withdrawing group, thereby modulating the chelating affinity of BAPTA for calcium ions. Solubility of the compound in a partially aqueous solvent was achieved by grafting a short PEG (polyethylene glycol) tail to the electron-withdrawing group. A reduction of the affinity for calcium ions upon photoswitching by a factor of 3–4, in the hundred nM range of dissociation constant, is reported and constitutes a proof of concept of this type of RPC. © 2018 Elsevier B.V. |
Actin-Network Architecture Regulates Microtubule Dynamics Article de journal A Colin; P Singaravelu; M Thery; L Blanchoin; Z Gueroui Current Biology, 28 (16), p. 2647-+, 2018, ISSN: 0960-9822. @article{RN18c, title = {Actin-Network Architecture Regulates Microtubule Dynamics}, author = {A Colin and P Singaravelu and M Thery and L Blanchoin and Z Gueroui}, url = {<Go to ISI>://WOS:000442111300035}, doi = {10.1016/j.cub.2018.06.028}, issn = {0960-9822}, year = {2018}, date = {2018-01-01}, journal = {Current Biology}, volume = {28}, number = {16}, pages = {2647-+}, keywords = {}, pubstate = {published}, tppubtype = {article} } |
Circularly Permuted Fluorogenic Proteins for the Design of Modular Biosensors Article de journal A G Tebo; F M Pimenta; M Zoumpoulaki; C Kikuti; H Sirkia; M -A Plamont; A Houdusse; A Gautier ACS Chemical Biology, 13 (9), p. 2392–2397, 2018. @article{Tebo:2018, title = {Circularly Permuted Fluorogenic Proteins for the Design of Modular Biosensors}, author = {A G Tebo and F M Pimenta and M Zoumpoulaki and C Kikuti and H Sirkia and M -A Plamont and A Houdusse and A Gautier}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85052286419&doi=10.1021%2facschembio.8b00417&partnerID=40&md5=f7f8a46015d14cb7450f3d6d2b70a529}, doi = {10.1021/acschembio.8b00417}, year = {2018}, date = {2018-01-01}, journal = {ACS Chemical Biology}, volume = {13}, number = {9}, pages = {2392--2397}, abstract = {Fluorescent reporters are essential components for the design of optical biosensors that are able to image intracellular analytes in living cells. Herein, we describe the development of circularly permuted variants of Fluorescence-Activating and absorption-Shifting Tag (FAST) and demonstrate their potential as reporting module in biosensors. Circularly permutated FAST (cpFAST) variants allow one to condition the binding and activation of a fluorogenic ligand (and thus fluorescence) to analyte recognition by coupling them with analyte-binding domains. We demonstrated their use for biosensor design by generating multicolor plug-and-play fluorogenic biosensors for imaging the intracellular levels of Ca2+ in living mammalian cells in real time. © 2018 American Chemical Society.}, keywords = {}, pubstate = {published}, tppubtype = {article} } Fluorescent reporters are essential components for the design of optical biosensors that are able to image intracellular analytes in living cells. Herein, we describe the development of circularly permuted variants of Fluorescence-Activating and absorption-Shifting Tag (FAST) and demonstrate their potential as reporting module in biosensors. Circularly permutated FAST (cpFAST) variants allow one to condition the binding and activation of a fluorogenic ligand (and thus fluorescence) to analyte recognition by coupling them with analyte-binding domains. We demonstrated their use for biosensor design by generating multicolor plug-and-play fluorogenic biosensors for imaging the intracellular levels of Ca2+ in living mammalian cells in real time. © 2018 American Chemical Society. |
Control of Protein Activity and Gene Expression by Cyclofen-OH Uncaging Article de journal W Zhang; F Hamouri; Z Feng; I Aujard; B Ducos; S Ye; S Weiss; M Volovitch; S Vriz; L Jullien; D Bensimon ChemBioChem, 19 (12), p. 1232–1238, 2018. @article{Zhang:2018, title = {Control of Protein Activity and Gene Expression by Cyclofen-OH Uncaging}, author = {W Zhang and F Hamouri and Z Feng and I Aujard and B Ducos and S Ye and S Weiss and M Volovitch and S Vriz and L Jullien and D Bensimon}, url = {https://www.scopus.com/inward/record.uri?eid=2-s2.0-85042596408&doi=10.1002%2fcbic.201700630&partnerID=40&md5=e4da60b83f338aba093989913695947b}, doi = {10.1002/cbic.201700630}, year = {2018}, date = {2018-01-01}, journal = {ChemBioChem}, volume = {19}, number = {12}, pages = {1232--1238}, abstract = {The use of light to control the expression of genes and the activity of proteins is a rapidly expanding field. Whereas many of these approaches use fusion between a light-activable protein and the protein of interest to control the activity of the latter, it is also possible to control the activity of a protein by uncaging a specific ligand. In that context, controlling the activation of a protein fused to the modified estrogen receptor (ERT) by uncaging its ligand cyclofen-OH has emerged as a generic and versatile method to control the activation of proteins quantitatively, quickly, and locally in a live organism. We present that approach and its uses in a variety of physiological contexts. © 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim}, keywords = {}, pubstate = {published}, tppubtype = {article} } The use of light to control the expression of genes and the activity of proteins is a rapidly expanding field. Whereas many of these approaches use fusion between a light-activable protein and the protein of interest to control the activity of the latter, it is also possible to control the activity of a protein by uncaging a specific ligand. In that context, controlling the activation of a protein fused to the modified estrogen receptor (ERT) by uncaging its ligand cyclofen-OH has emerged as a generic and versatile method to control the activation of proteins quantitatively, quickly, and locally in a live organism. We present that approach and its uses in a variety of physiological contexts. © 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim |