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

Investigation of the role of the BAM complex and SurA chaperone in outer-membrane protein biogenesis and type III secretion system expression in Salmonella.

Microbiology (Reading, England) - 1 May 2009

Fardini Yann, Trotereau Jérôme, Bottreau Elisabeth, Souchard Charlène, Velge Philippe, Virlogeux-Payant Isabelle

Abstract excerpt

In Escherichia coli, the assembly of outer-membrane proteins (OMP) requires the BAM complex and periplasmic chaperones, such as SurA or DegP. Previous work has suggested a potential link between OMP assembly and expression of the genes encoding type-III secretion systems. In order to test this hypothesis, we studied the role of the different lipoproteins of the BAM complex (i.e. BamB, BamC, BamD and BamE), and...

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 Gene Expression

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Heat-Shock Proteins

Share to Peptidylprolyl Isomerase

Share to Periplasmic Proteins

Share to Protein Transport

Share to Salmonella

Share to Serine Endopeptidases

Source

Identifiers

PMID: 19372159
DOI: 10.1099/mic.0.025155-0

Genes

OMP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Investigation of the role of the BAM complex and SurA chaperone in outer-membrane protein biogenesis and type III secretion system expression in Salmonella.PMID 19372159Read ↗

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

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

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

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

Role of periplasmic chaperones and BamA (YaeT/Omp85) in folding and secretion of intimin from enteropathogenic Escherichia coli strains.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 ↗

Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics.Semantic proximity Read ↗

The evolution of new lipoprotein subunits of the bacterial outer membrane BAM complex.Semantic proximity Read ↗

Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis.Semantic proximity Read ↗

Demarcating SurA activities required for outer membrane targeting of Yersinia pseudotuberculosis adhesins.Semantic proximity Read ↗

Suppression of the temperature-sensitive mutation of the bamD gene required for the assembly of outer membrane proteins by multicopy of the yiaD gene in Escherichia coli.Semantic proximity Read ↗

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