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Lookup NU author(s): Professor Tracy Palmer FRS FRSE FMedSciORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2015 The Authors. BAM is a conserved molecular machine, the central component of which is BamA. Orthologues of BamA are found in all Gram-negative bacteria, chloroplasts and mitochondria where it is required for the folding and insertion of β-barrel containing integral outer membrane proteins (OMPs) into the outer membrane. BamA binds unfolded β-barrel precursors via the five polypeptide transport-associated (POTRA) domains at its N-terminus. The C-terminus of BamA folds into a β-barrel domain, which tethers BamA to the outer membrane and is involved in OMP insertion. BamA orthologues are found in all Gram-negative bacteria and appear to function in a species-specific manner. Here we investigate the nature of this species-specificity by examining whether chimeric Escherichia coliBamA fusion proteins, carrying either the β-barrel or POTRA domains from various BamA orthologues, can functionally replace E.coliBamA. We demonstrate that the β-barrel domains of many BamA orthologues are functionally interchangeable. We show that defects in the orthologous POTRA domains can be rescued by compensatory mutations within the β-barrel. These data reveal that the POTRA and barrel domains must be precisely aligned to ensure efficient OMP insertion.
Author(s): Browning DF, Bavro VN, Mason JL, Sevastsyanovich YR, Rossiter AE, Jeeves M, Wells TJ, Knowles TJ, Cunningham AF, Donald JW, Palmer T, Overduin M, Henderson IR
Publication type: Article
Publication status: Published
Journal: Molecular Microbiology
Year: 2015
Volume: 97
Issue: 4
Pages: 646-659
Print publication date: 01/08/2015
Online publication date: 06/05/2015
Acceptance date: 01/01/1900
Date deposited: 14/02/2019
ISSN (print): 0950-382X
ISSN (electronic): 1365-2958
Publisher: Blackwell Publishing Ltd
URL: https://doi.org/10.1111/mmi.13052
DOI: 10.1111/mmi.13052
PubMed id: 25943387
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