Crystal structure of human Mediator subunit MED23

Autor: Didier Monté, Bernard Clantin, Frédérique Dewitte, Zoé Lens, Prakash Rucktooa, Els Pardon, Jan Steyaert, Alexis Verger, Vincent Villeret

Publikováno v: Nature Communications, Vol 9, Iss 1, Pp 1-7 (2018)

Mediator is a large multi-subunits complex essential to the regulation of transcription by RNA pol II. Here the authors report the crystal structure of MED23—one of the largest subunits of the complex together with MED1 and MED14—revealing a comp

Externí odkaz: https://doaj.org/article/128fb504de7f40d08b3482fbcb664f49

Structural insight into the role of the PAS domainfor signal transduction in sensor-kinase BvgS

Autor: Youhua Yuan, Elian Dupré, Elodie Lesne, Françoise Jacob-Dubuisson, Rudy Antoine, Bernard Clantin, Vincent Villeret, Sophie Lecher

Publikováno v: Journal of Bacteriology
Journal of Bacteriology, American Society for Microbiology, 2021, ⟨10.1128/JB.00614-20⟩
Journal of Bacteriology, 2021, 203 (9), pp.e00614-20. ⟨10.1128/jb.00614-20⟩
J Bacteriol
Journal of Bacteriology, 2021, ⟨10.1128/JB.00614-20⟩

The two-component system BvgAS controls the virulence regulon in Bordetella pertussis. BvgS is the prototype of a family of sensor histidine kinases harboring periplasmic Venus flytrap (VFT) domains. The VFT domains are connected to the cytoplasmic k

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66751b3e15ec12d80d13e62bfb7fe979
https://hal.archives-ouvertes.fr/hal-03176410

Substrate recognition by the POTRA domains of TpsB transporter FhaC

Autor: Bernard Clantin, Anne-Sophie Delattre, Nathalie Saint, Vincent Villeret, Eve Willery, Françoise Jacob-Dubuisson, Guy Lippens, Camille Locht

Publikováno v: Molecular Microbiology. 81:99-112

Widespread in Gram-negative bacteria, the two-partner secretion (TPS) pathway mediates the secretion of large, β-helical 'TpsA' proteins with various functions. TpsA proteins harbour a conserved, N-proximal TPS domain essential for secretion. TpsB t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f3db3320f481badbd8aabe9ad67f34f6
https://doi.org/10.1111/j.1365-2958.2011.07680.x

Conserved Omp85 lid-lock structure and substrate recognition in FhaC

Autor: Françoise Jacob-Dubuisson, Sebastian Hiller, Vincent Villeret, Frédérique Dewitte, Fabian Gruss, Timm Maier, Anne-Sophie Delattre, Bernard Clantin

Publikováno v: Nature Communications
Nature Communications, Nature Publishing Group, 2015, 6, pp.7452. ⟨10.1038/ncomms8452⟩
Nature Communications, 2015, 6, pp.7452. ⟨10.1038/ncomms8452⟩
'Nature Communications ', vol: 6, pages: 7452-1-7452-99 (2015)
Nature communications

Omp85 proteins mediate translocation of polypeptide substrates across and into cellular membranes. They share a common architecture comprising substrate-interacting POTRA domains, a C-terminal 16-stranded β-barrel pore and two signature motifs locat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05c2978f3be02de8c6dfd3774100c524
https://hal.univ-lille.fr/hal-03182009

The crystal structure of filamentous hemagglutinin secretion domain and its implications for the two-partner secretion pathway

Autor: Eve Willery, Hélène Hodak, Vincent Villeret, Camille Locht, Bernard Clantin, Françoise Jacob-Dubuisson

Publikováno v: Proceedings of the National Academy of Sciences. 101:6194-6199

Filamentous hemagglutinin (FHA), the major 230-kDa adhesin of the whooping cough agent Bordetella pertussis , is one of the most efficiently secreted proteins in Gram-negative bacteria. FHA is secreted by means of the two-partner secretion (TPS) path

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9b7c3b3a5a4f581465e119d50e9c6ca
https://doi.org/10.1073/pnas.0400291101