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

Insertion of the polytopic membrane protein MalF is dependent on the bacterial secretion machinery.

The Journal of biological chemistry - 24 May 1996

Traxler B, Murphy C

Abstract excerpt

We examined the dependence of protein export and membrane protein insertion on SecE and SecA, two components of the secretion (Sec) apparatus of Escherichia coli. The magnitude of the secretion defect observed for signal sequence-containing proteins in cells depleted of SecE is larger and more general than that in many temperature- or cold-sensitive Sec mutants. In addition, we show that the proper insertion of...

Read the complete abstract on PubMed

Topics

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

Share to Cytoplasm
Share to ATP-Binding Cassette Transporters
Share to Azides

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Bacterial Proteins

Share to Carrier Proteins

Share to Escherichia coli Proteins

Share to Monosaccharide Transport Proteins

Share to Mutation

Source

Identifiers

PMID: 8647843
DOI: 10.1074/jbc.271.21.12394

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

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insertion of the polytopic membrane protein MalF is dependent on the bacterial secretion machinery.PMID 8647843Read ↗

The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins.Semantic proximity Read ↗

One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery.Semantic proximity Read ↗

The functional integration of a polytopic membrane protein of Escherichia coli is dependent on the bacterial signal-recognition particle.Semantic proximity Read ↗

The protein translocation apparatus contributes to determining the topology of an integral membrane protein in Escherichia coli.Semantic proximity Read ↗

Functional integration of a polytopic membrane protein of E. coli requires the bacterial signal recognition particle.Semantic proximity Read ↗

SecD and SecF facilitate protein export in Escherichia coli.Semantic proximity Read ↗

A mutation in the Escherichia coli secY gene that produces distinct effects on inner membrane protein insertion and protein export.Semantic proximity Read ↗

Protein translocation functions of Escherichia coli SecY: in vitro characterization of cold-sensitive secY mutants.Semantic proximity Read ↗

SecA is required for the insertion of inner membrane proteins targeted by the Escherichia coli signal recognition particle.Semantic proximity Read ↗

Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region.Semantic proximity Read ↗

secG and temperature modulate expression of azide-resistant and signal sequence suppressor phenotypes of Escherichia coli secA mutants.Semantic proximity Read ↗

Translocation, folding, and stability of the HflKC complex with signal anchor topogenic sequences.Semantic proximity Read ↗

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