Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel

The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). The central BAM subunit (BamA) itself contains a β-barrel domain that is essential for OM protein biogenesis, but its mechanism of action is unknown. To elucidate its fu...

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Published inNature communications Vol. 10; no. 1; pp. 3358 - 13
Main Authors Doyle, Matthew T., Bernstein, Harris D.
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 26.07.2019
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Abstract The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). The central BAM subunit (BamA) itself contains a β-barrel domain that is essential for OM protein biogenesis, but its mechanism of action is unknown. To elucidate its function, here we develop a method to trap a native Escherichia coli β-barrel protein bound stably to BamA at a late stage of assembly in vivo. Using disulfide-bond crosslinking, we find that the first β-strand of a laterally ‘open’ form of the BamA β-barrel forms a rigid interface with the C-terminal β-strand of the substrate. In contrast, the lipid-facing surface of the last two BamA β-strands forms weaker, conformationally heterogeneous interactions with the first β-strand of the substrate that likely represent intermediate assembly states. Based on our results, we propose that BamA promotes the membrane integration of partially folded β-barrels by a ‘swing’ mechanism. The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). Here authors develop a method to trap an E. coli β-barrel protein bound stably to BamA at a late stage of assembly in vivo which provides insights BamA mediated membrane integration.
AbstractList The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). The central BAM subunit (BamA) itself contains a β-barrel domain that is essential for OM protein biogenesis, but its mechanism of action is unknown. To elucidate its function, here we develop a method to trap a native Escherichia coli β-barrel protein bound stably to BamA at a late stage of assembly in vivo. Using disulfide-bond crosslinking, we find that the first β-strand of a laterally 'open' form of the BamA β-barrel forms a rigid interface with the C-terminal β-strand of the substrate. In contrast, the lipid-facing surface of the last two BamA β-strands forms weaker, conformationally heterogeneous interactions with the first β-strand of the substrate that likely represent intermediate assembly states. Based on our results, we propose that BamA promotes the membrane integration of partially folded β-barrels by a 'swing' mechanism.
The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). Here authors develop a method to trap an E. coli β-barrel protein bound stably to BamA at a late stage of assembly in vivo which provides insights BamA mediated membrane integration.
The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). The central BAM subunit (BamA) itself contains a β-barrel domain that is essential for OM protein biogenesis, but its mechanism of action is unknown. To elucidate its function, here we develop a method to trap a native Escherichia coli β-barrel protein bound stably to BamA at a late stage of assembly in vivo. Using disulfide-bond crosslinking, we find that the first β-strand of a laterally ‘open’ form of the BamA β-barrel forms a rigid interface with the C-terminal β-strand of the substrate. In contrast, the lipid-facing surface of the last two BamA β-strands forms weaker, conformationally heterogeneous interactions with the first β-strand of the substrate that likely represent intermediate assembly states. Based on our results, we propose that BamA promotes the membrane integration of partially folded β-barrels by a ‘swing’ mechanism. The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). Here authors develop a method to trap an E. coli β-barrel protein bound stably to BamA at a late stage of assembly in vivo which provides insights BamA mediated membrane integration.
The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). The central BAM subunit (BamA) itself contains a β-barrel domain that is essential for OM protein biogenesis, but its mechanism of action is unknown. To elucidate its function, here we develop a method to trap a native Escherichia coli β-barrel protein bound stably to BamA at a late stage of assembly in vivo. Using disulfide-bond crosslinking, we find that the first β-strand of a laterally ‘open’ form of the BamA β-barrel forms a rigid interface with the C-terminal β-strand of the substrate. In contrast, the lipid-facing surface of the last two BamA β-strands forms weaker, conformationally heterogeneous interactions with the first β-strand of the substrate that likely represent intermediate assembly states. Based on our results, we propose that BamA promotes the membrane integration of partially folded β-barrels by a ‘swing’ mechanism.
ArticleNumber 3358
Author Bernstein, Harris D.
Doyle, Matthew T.
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  organization: Genetics and Biochemistry Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
BackLink https://www.ncbi.nlm.nih.gov/pubmed/31350400$$D View this record in MEDLINE/PubMed
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Snippet The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). The central BAM subunit...
The integration of β-barrel proteins into the bacterial outer membrane (OM) is catalysed by the β-barrel assembly machinery (BAM). Here authors develop a...
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StartPage 3358
SubjectTerms 631/326
631/45
631/57
82/1
82/29
82/80
Assembly
Bacterial Outer Membrane Proteins - chemistry
Bacterial Outer Membrane Proteins - genetics
Bacterial Outer Membrane Proteins - metabolism
Cell Membrane - chemistry
Cell Membrane - genetics
Cell Membrane - metabolism
Crosslinking
E coli
Escherichia coli - chemistry
Escherichia coli - genetics
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Escherichia coli Proteins - metabolism
Humanities and Social Sciences
Integration
Lipids
Membrane proteins
multidisciplinary
Outer membrane proteins
Polypeptides
Protein Binding
Protein Domains
Proteins
Science
Science (multidisciplinary)
Substrates
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Title Bacterial outer membrane proteins assemble via asymmetric interactions with the BamA β-barrel
URI https://link.springer.com/article/10.1038/s41467-019-11230-9
https://www.ncbi.nlm.nih.gov/pubmed/31350400
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https://search.proquest.com/docview/2265794946
https://pubmed.ncbi.nlm.nih.gov/PMC6659671
https://doaj.org/article/7ee3ebed676f43cab7020c8070468411
Volume 10
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