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Article

Functions of the BamBCDE Lipoproteins Revealed by Bypass Mutations in BamA.

Journal of bacteriology - 8 Oct 2020

Hart Elizabeth M, Silhavy Thomas J

Abstract excerpt

The heteropentomeric β-barrel assembly machine (BAM complex) is responsible for folding and inserting a diverse array of β-barrel outer membrane proteins (OMPs) into the outer membrane (OM) of Gram-negative bacteria. The BAM complex contains two essential proteins, the β-barrel OMP BamA and a lipoprotein BamD, whereas the auxiliary lipoproteins BamBCE are individually nonessential. Here, we identify and...

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Source

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Identifiers

PMID: 32817097
DOI: 10.1128/JB.00401-20
PMCID: PMC7549358

Genes

OMP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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Functions of the BamBCDE Lipoproteins Revealed by Bypass Mutations in BamA.PMID 32817097Read ↗

Classifying β-Barrel Assembly Substrates by Manipulating Essential Bam Complex Members.Semantic proximity Read ↗

Bypassing BamD essentiality by mutations in a non-essential substrate.Semantic proximity Read ↗

Substitutions in the BamA β-barrel domain overcome the conditional lethal phenotype of a ΔbamB ΔbamE strain of Escherichia coli.Semantic proximity Read ↗

The Structure of a BamA-BamD Fusion Illuminates the Architecture of the β-Barrel Assembly Machine Core.Semantic proximity Read ↗

The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane {beta}-barrel proteins in Caulobacter crescentus.Semantic proximity Read ↗

BamA β16C strand and periplasmic turns are critical for outer membrane protein insertion and assembly.Semantic proximity Read ↗

The BaeSR two-component system activates bamK, a paralog of the essential β-barrel foldase bamA, in Klebsiella pneumoniae.Semantic proximity Read ↗

High-throughput suppressor screen demonstrates that RcsF monitors outer membrane integrity and not Bam complex function.Semantic proximity Read ↗

Lateral opening and exit pore formation are required for BamA function.Semantic proximity Read ↗

Conserved residues of the putative L6 loop of Escherichia coli BamA play a critical role in the assembly of β-barrel outer membrane proteins, including that of BamA itself.Semantic proximity Read ↗

Conformation-specific labeling of BamA and suppressor analysis suggest a cyclic mechanism for β-barrel assembly in Escherichia coli.Semantic proximity Read ↗

Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.Semantic proximity Read ↗

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