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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2015
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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. |
format | Online Article Text |
id | pubmed-4613867 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
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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