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

A signal sequence is not required for protein export in prlA mutants of Escherichia coli.

The EMBO journal - 1 Mar 1993

Derman A I, Puziss J W, Bassford P J, Beckwith J

Abstract excerpt

The prlA/secY gene, which codes for an integral membrane protein component of the Escherichia coli protein export machinery, is the locus of the strongest suppressors of signal sequence mutations. We demonstrate that two exported proteins of E.coli, maltose-binding protein and alkaline phosphatase, each lacking its entire signal sequence, are exported to the periplasm in several prlA mutants. The export...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Base Sequence
Share to Carrier Proteins

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

Share to DNA, Bacterial

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Molecular Sequence Data

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 8458344
DOI: 10.1002/j.1460-2075.1993.tb05728.x
PMCID: PMC413286

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A signal sequence is not required for protein export in prlA mutants of Escherichia coli.PMID 8458344Read ↗

Targeting of signal sequenceless proteins for export in Escherichia coli with altered protein translocase.Semantic proximity Read ↗

Recognition of secretory proteins in Escherichia coli requires signals in addition to the signal sequence and slow folding.Semantic proximity Read ↗

Escherichia coli SecB stimulates export without maintaining export competence of ribose-binding protein signal sequence mutants.Semantic proximity Read ↗

Defective translocation of a signal sequence mutant in a prlA4 suppressor strain of Escherichia coli.Semantic proximity Read ↗

The sec and prl genes of Escherichia coli.Semantic proximity Read ↗

prlA suppression of defective export of maltose-binding protein in secB mutants of Escherichia coli.Semantic proximity Read ↗

Modeling the effects of prl mutations on the Escherichia coli SecY complex.Semantic proximity Read ↗

PrlA suppressor mutations cluster in regions corresponding to three distinct topological domains.Semantic proximity Read ↗

Both transmembrane domains of SecG contribute to signal sequence recognition by the Escherichia coli protein export machinery.Semantic proximity Read ↗

The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits.Semantic proximity Read ↗

Signal peptides: exquisitely designed transport promoters.Semantic proximity Read ↗

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

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