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POTRA domains of the TamA insertase interact with the outer membrane and modulate membrane properties.
Mellouk, Abdelkader; Jaouen, Paul; Ruel, Louis-Jacques; Lê, Michel; Martini, Cyrielle; Moraes, Trevor F; El Bakkouri, Majida; Lagüe, Patrick; Boisselier, Elodie; Calmettes, Charles.
Afiliação
  • Mellouk A; Institut National de la Rechyuerche Scientifique (INRS), Centre Armand-Frappier Santé Biotechnologie, Laval, QC H7V 1B7, Canada.
  • Jaouen P; Regroupement Québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Université du Québec à Montréal, Montréal, QC H2X 3Y7, Canada.
  • Ruel LJ; Regroupement Québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Université du Québec à Montréal, Montréal, QC H2X 3Y7, Canada.
  • Lê M; Faculty of Medicine, Department of Ophthalmology and Otolaryngology-Head and Neck Surgery, centre hospitalier universitaire de Québec, Université Laval, Québec City, QC G1S 4L8, Canada.
  • Martini C; Regroupement Québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Université du Québec à Montréal, Montréal, QC H2X 3Y7, Canada.
  • Moraes TF; Département de Biochimie, de Microbiologie et de Bio-informatique, Université Laval, Québec City, QC G1V 0A6, Canada.
  • El Bakkouri M; Institut de Biologie Intégrative et des Systèmes, Université Laval, Québec City, QC G1V 0A6, Canada.
  • Lagüe P; Institut National de la Rechyuerche Scientifique (INRS), Centre Armand-Frappier Santé Biotechnologie, Laval, QC H7V 1B7, Canada.
  • Boisselier E; Regroupement Québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Université du Québec à Montréal, Montréal, QC H2X 3Y7, Canada.
  • Calmettes C; Institut National de la Rechyuerche Scientifique (INRS), Centre Armand-Frappier Santé Biotechnologie, Laval, QC H7V 1B7, Canada.
Proc Natl Acad Sci U S A ; 121(28): e2402543121, 2024 Jul 09.
Article em En | MEDLINE | ID: mdl-38959031
ABSTRACT
The outer membrane (OM) of gram-negative bacteria serves as a vital organelle that is densely populated with OM proteins (OMPs) and plays pivotal roles in cellular functions and virulence. The assembly and insertion of these OMPs into the OM represent a fundamental process requiring specialized molecular chaperones. One example is the translocation and assembly module (TAM), which functions as a transenvelope chaperone promoting the folding of specific autotransporters, adhesins, and secretion systems. The catalytic unit of TAM, TamA, comprises a catalytic ß-barrel domain anchored within the OM and three periplasmic polypeptide-transport-associated (POTRA) domains that recruit the TamB subunit. The latter acts as a periplasmic ladder that facilitates the transport of unfolded OMPs across the periplasm. In addition to their role in recruiting the auxiliary protein TamB, our data demonstrate that the POTRA domains mediate interactions with the inner surface of the OM, ultimately modulating the membrane properties. Through the integration of X-ray crystallography, molecular dynamic simulations, and biomolecular interaction methodologies, we located the membrane-binding site on the first and second POTRA domains. Our data highlight a binding preference for phosphatidylglycerol, a minor lipid constituent present in the OM, which has been previously reported to facilitate OMP assembly. In the context of the densely OMP-populated membrane, this association may serve as a mechanism to secure lipid accessibility for nascent OMPs through steric interactions with existing OMPs, in addition to creating favorable conditions for OMP biogenesis.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas da Membrana Bacteriana Externa / Proteínas de Escherichia coli Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas da Membrana Bacteriana Externa / Proteínas de Escherichia coli Idioma: En Revista: Proc Natl Acad Sci U S A Ano de publicação: 2024 Tipo de documento: Article