The NagY regulator: A member of the BglG/SacY antiterminator family conserved in Enterococcus faecalis and involved in virulence

Autor: Diane Soussan, Marine Salze, Pierre Ledormand, Nicolas Sauvageot, Amine Boukerb, Olivier Lesouhaitier, Gwennaele Fichant, Alain Rincé, Yves Quentin, Cécile Muller

Publikováno v: Frontiers in Microbiology, Vol 13 (2023)

Enterococcus faecalis is a commensal bacterium of the gastrointestinal tract but also a major nosocomial pathogen. This bacterium uses regulators like BglG/SacY family of transcriptional antiterminators to adapt its metabolism during host colonizatio

Externí odkaz: https://doaj.org/article/fa76845a6f574c2bbf209328ac01882e

Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase

Autor: Mirna Hajj, Petra Langendijk-Genevaux, Manon Batista, Yves Quentin, Sébastien Laurent, Régine Capeyrou, Ziad Abdel-Razzak, Didier Flament, Hala Chamieh, Gwennaele Fichant, Béatrice Clouet-d’Orval, Marie Bouvier

Publikováno v: Biomolecules, Vol 11, Iss 7, p 950 (2021)

Helicase proteins are known to use the energy of ATP to unwind nucleic acids and to remodel protein-nucleic acid complexes. They are involved in almost every aspect of DNA and RNA metabolisms and participate in numerous repair mechanisms that maintai

Externí odkaz: https://doaj.org/article/c1fe9aa2acf34a768b4e2a2a0cb6a1cc

The cyst-dividing bacterium Ramlibacter tataouinensis TTB310 genome reveals a well-stocked toolbox for adaptation to a desert environment.

Autor: Gilles De Luca, Mohamed Barakat, Philippe Ortet, Sylvain Fochesato, Cécile Jourlin-Castelli, Mireille Ansaldi, Béatrice Py, Gwennaele Fichant, Pedro M Coutinho, Romé Voulhoux, Olivier Bastien, Eric Maréchal, Bernard Henrissat, Yves Quentin, Philippe Noirot, Alain Filloux, Vincent Méjean, Michael S DuBow, Frédéric Barras, Valérie Barbe, Jean Weissenbach, Irina Mihalcescu, André Verméglio, Wafa Achouak, Thierry Heulin

Publikováno v: PLoS ONE, Vol 6, Iss 9, p e23784 (2011)

Ramlibacter tataouinensis TTB310(T) (strain TTB310), a betaproteobacterium isolated from a semi-arid region of South Tunisia (Tataouine), is characterized by the presence of both spherical and rod-shaped cells in pure culture. Cell division of strain

Externí odkaz: https://doaj.org/article/afd0448274e24149bb9d29b455e3013f

Phylogenetic Diversity of Lhr Proteins and Miochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase

Autor: Manon Batista, Marie Bouvier, Yves Quentin, Petra S. Langendijk-Genevaux, Ziad Abdel Razzak, Hala Chamieh, Didier Flament, Sébastien Laurent, Béatrice Clouet-d’Orval, Gwennaele Fichant, Mirna Hajj

Helicases are proteins that use the energy of ATP to unwind nucleic acids and to remodel protein-nucleic acid complexes. They are involved in almost every aspect of the DNA and RNA metabolisms and participate in numerous repair mechanisms that mainta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b4b320b8561469f4cd0b0ec87b2d9797
https://doi.org/10.20944/preprints202103.0477.v1

RNA processing machineries in Archaea: the 5'-3' exoribonuclease aRNase J of the β-CASP family is engaged specifically with the helicase ASH-Ski2 and the 3'-5' exoribonucleolytic RNA exosome machinery

Autor: Manon Batista, Violette Morales, Sébastien Laurent, Didier Flament, Yann Moalic, Mohamed Jebbar, Petra Langendijk-Genevaux, Marie Bouvier, Clarisse Etienne, Duy Khanh Phung, Béatrice Clouet-d’Orval, Sophie Liuu, Gwennaele Fichant

Publikováno v: Nucleic Acids Research
Nucleic Acids Research, Oxford University Press, 2020, 48 (7), pp.3832-3847. ⟨10.1093/nar/gkaa052⟩
Nucleic Acids Research (0305-1048) (Oxford University Press (OUP)), 2020-04, Vol. 48, N. 7, P. 3832-3847

We are indebted to L. Correia of the Paris Sud Ouest PAPPSO proteomics core facility (http://papso.inra.fr) which is supported by INRA (http://www.inra.fr), the Ile-de-France regional council (https://www.iledefrance.fr/education-recherche), IBiSA (h

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e512fc3cb52b9155d7a812e4a9ddedd3
https://pubmed.ncbi.nlm.nih.gov/32030412