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BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism

[Image: see text] β-Barrel assembly machinery protein A (BamA) plays a critical role in the biogenesis of outer membrane proteins (OMPs); however, a mechanistic understanding of its function is lacking. Here, we report an in vitro assay that investigates whether the mechanism of BamA-catalyzed OMP f...

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Autores principales: Plummer, Ashlee M., Fleming, Karen G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2015
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4613867/
https://www.ncbi.nlm.nih.gov/pubmed/26394056
http://dx.doi.org/10.1021/acs.biochem.5b00950
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author Plummer, Ashlee M.
Fleming, Karen G.
author_facet Plummer, Ashlee M.
Fleming, Karen G.
author_sort Plummer, Ashlee M.
collection PubMed
description [Image: see text] β-Barrel assembly machinery protein A (BamA) plays a critical role in the biogenesis of outer membrane proteins (OMPs); however, a mechanistic understanding of its function is lacking. Here, we report an in vitro assay that investigates whether the mechanism of BamA-catalyzed OMP folding is stoichiometric or catalytic. We found that BamA accelerates the folding of OMPs in vitro via a catalytic mechanism, similar to the activity of the full multiprotein β-barrel assembly machinery (BAM) complex in vivo. As BamA alone can repeatedly facilitate the folding of OMPs, we suggest the additional BAM components accelerate this basal activity to biologically relevant time scales.
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spelling pubmed-46138672016-09-22 BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism Plummer, Ashlee M. Fleming, Karen G. Biochemistry [Image: see text] β-Barrel assembly machinery protein A (BamA) plays a critical role in the biogenesis of outer membrane proteins (OMPs); however, a mechanistic understanding of its function is lacking. Here, we report an in vitro assay that investigates whether the mechanism of BamA-catalyzed OMP folding is stoichiometric or catalytic. We found that BamA accelerates the folding of OMPs in vitro via a catalytic mechanism, similar to the activity of the full multiprotein β-barrel assembly machinery (BAM) complex in vivo. As BamA alone can repeatedly facilitate the folding of OMPs, we suggest the additional BAM components accelerate this basal activity to biologically relevant time scales. American Chemical Society 2015-09-22 2015-10-06 /pmc/articles/PMC4613867/ /pubmed/26394056 http://dx.doi.org/10.1021/acs.biochem.5b00950 Text en Copyright © 2015 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Plummer, Ashlee M.
Fleming, Karen G.
BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism
title BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism
title_full BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism
title_fullStr BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism
title_full_unstemmed BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism
title_short BamA Alone Accelerates Outer Membrane Protein Folding In Vitro through a Catalytic Mechanism
title_sort bama alone accelerates outer membrane protein folding in vitro through a catalytic mechanism
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4613867/
https://www.ncbi.nlm.nih.gov/pubmed/26394056
http://dx.doi.org/10.1021/acs.biochem.5b00950
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