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

YaeL (EcfE) activates the sigma(E) pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA.

Genes & development - 15 Aug 2002

Kanehara Kazue, Ito Koreaki, Akiyama Yoshinori

Abstract excerpt

Escherichia coli YaeL (EcfE) is a homolog of human site-2 protease (S2P), a membrane-bound zinc metalloprotease involved in regulated intramembrane proteolysis. We have shown previously that YaeL, having essential metalloprotease active site motifs in the cytoplasmic domain, is indispensable for viability. Here, we obtained rpoE, encoding an extracytoplasmic stress response sigma factor (sigma(E)), as a multicopy...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to beta-Galactosidase
Share to Cell Survival

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endopeptidases

Share to Immunoblotting

Share to Precipitin Tests

Share to Sigma Factor

Source

Open in PubMed Open full text

Identifiers

PMID: 12183368
DOI: 10.1101/gad.1002302
PMCID: PMC186437

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

YaeL (EcfE) activates the sigma(E) pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA.PMID 12183368Read ↗

Dispensable PDZ domain of Escherichia coli YaeL essential protease.Semantic proximity Read ↗

DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma(E)-dependent extracytoplasmic stress response.Semantic proximity Read ↗

Characterization of the yaeL gene product and its S2P-protease motifs in Escherichia coli.Semantic proximity Read ↗

RseP (YaeL), an Escherichia coli RIP protease, cleaves transmembrane sequences.Semantic proximity Read ↗

EcfE, a new essential inner membrane protease: its role in the regulation of heat shock response in Escherichia coli.Semantic proximity Read ↗

YpdC determines site-1 degradation in regulated intramembrane proteolysis of the RsiW anti-sigma factor of Bacillus subtilis.Semantic proximity Read ↗

PDZ domains of RseP are not essential for sequential cleavage of RseA or stress-induced σ(E) activation in vivo.Semantic proximity Read ↗

Function of site-2 proteases in bacteria and bacterial pathogens.Semantic proximity Read ↗

Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis.Semantic proximity Read ↗

A structure-based model of substrate discrimination by a noncanonical PDZ tandem in the intramembrane-cleaving protease RseP.Semantic proximity Read ↗

A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli.Semantic proximity Read ↗

Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage.Semantic proximity Read ↗

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