BamA forms a translocation channel for polypeptide export across the bacterial outer membrane.


Journal

Molecular cell
ISSN: 1097-4164
Titre abrégé: Mol Cell
Pays: United States
ID NLM: 9802571

Informations de publication

Date de publication:
06 05 2021
Historique:
received: 19 10 2020
revised: 05 01 2021
accepted: 18 02 2021
pubmed: 12 3 2021
medline: 16 6 2021
entrez: 11 3 2021
Statut: ppublish

Résumé

The β-barrel assembly machine (BAM) integrates β-barrel proteins into the outer membrane (OM) of Gram-negative bacteria. An essential BAM subunit (BamA) catalyzes integration by promoting the formation of a hybrid-barrel intermediate state between its own β-barrel domain and that of its client proteins. Here we show that in addition to catalyzing the integration of β-barrel proteins, BamA functions as a polypeptide export channel. In vivo structural mapping via intermolecular disulfide crosslinking showed that the extracellular "passenger" domain of a member of the "autotransporter" superfamily of virulence factors traverses the OM through the BamA β-barrel lumen. Furthermore, we demonstrate that a highly conserved residue within autotransporter β-barrels is required to position the passenger inside BamA to initiate translocation and that during translocation, the passenger stabilizes the hybrid-barrel state. Our results not only establish a new function for BamA but also unify the divergent functions of BamA and other "Omp85" superfamily transporters.

Identifiants

pubmed: 33705710
pii: S1097-2765(21)00133-7
doi: 10.1016/j.molcel.2021.02.023
pmc: PMC8106670
mid: NIHMS1683470
pii:
doi:

Substances chimiques

Bacterial Outer Membrane Proteins 0
BamA protein, E coli 0
Escherichia coli Proteins 0
Tryptophan 8DUH1N11BX

Types de publication

Journal Article Research Support, N.I.H., Intramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

2000-2012.e3

Subventions

Organisme : Intramural NIH HHS
ID : ZIA DK052037
Pays : United States

Informations de copyright

Published by Elsevier Inc.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

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Auteurs

Matthew Thomas Doyle (MT)

Genetics and Biochemistry Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Harris David Bernstein (HD)

Genetics and Biochemistry Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA. Electronic address: harris_bernstein@nih.gov.

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