Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Nature communications - 21 Jan 2026

Nilaweera Thushani D, Brandes Nathan T, LaCroix Ian S, Schwarz Benjamin, Bernstein Harris D

Abstract excerpt

Virtually all integral outer membrane proteins (OMPs) produced by Gram-negative bacteria contain a unique 'β barrel' structure that serves as a membrane spanning domain. The universal barrel assembly machine (BAM) catalyzes OMP assembly (folding and membrane insertion) in vivo, and purified Escherichia coli BAM that is reconstituted into proteoliposomes catalyzes OMP assembly in vitro. Here we show that BAM also...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Outer Membrane Proteins
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to OMP gene

Share to Mutation

Share to Phospholipid Transfer Proteins

Share to Phospholipids

Source

Open in PubMed Open full text

Identifiers

PMID: 41565654
DOI: 10.1038/s41467-026-68743-3
PMCID: PMC12923597

Genes

OMP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.PMID 41565654Read ↗

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

Functions of the BamBCDE Lipoproteins Revealed by Bypass Mutations in BamA.Semantic proximity Read ↗

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

Structural basis for maintenance of bacterial outer membrane lipid asymmetry.Semantic proximity Read ↗

Identification of a novel post-insertion step in the assembly of a bacterial outer membrane protein.Semantic proximity Read ↗

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

Bacterial Outer Membrane Proteins Are Targeted to the Bam Complex by Two Parallel Mechanisms.Semantic proximity Read ↗

Advances in understanding bacterial outer-membrane biogenesis.Semantic proximity Read ↗

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

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

Plasticity within the barrel domain of BamA mediates a hybrid-barrel mechanism by BAM.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.