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

Dislocation of membrane proteins in FtsH-mediated proteolysis.

The EMBO journal - 1 Jun 1999

Kihara A, Akiyama Y, Ito K

Abstract excerpt

Escherichia coli FtsH degrades several integral membrane proteins, including YccA, having seven transmembrane segments, a cytosolic N-terminus and a periplasmic C-terminus. Evidence indicates that FtsH initiates proteolysis at the N-terminal cytosolic domain. SecY, having 10 transmembrane segments, is also a substrate of FtsH. We studied whether and how the FtsH-catalyzed proteolysis on the cytosolic side...

Read the complete abstract on PubMed

Topics

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

Share to Alkaline Phosphatase
Share to ATP-Dependent Proteases
Share to Disulfides

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

Share to Endopeptidase K

Share to Periplasm

Share to Protein Disulfide-Isomerases

Share to SEC Translocation Channels

Share to Trypsin

Source

Open in PubMed Open full text

Identifiers

PMID: 10357810
DOI: 10.1093/emboj/18.11.2970
PMCID: PMC1171379

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

Dislocation of membrane proteins in FtsH-mediated proteolysis.PMID 10357810Read ↗

Involvement of FtsH in protein assembly into and through the membrane. I. Mutations that reduce retention efficiency of a cytoplasmic reporter.Semantic proximity Read ↗

Different pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex: an implication from the interference by a mutant form of a new substrate protein, YccA.Semantic proximity Read ↗

FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins.Semantic proximity Read ↗

Roles of the periplasmic domain of Escherichia coli FtsH (HflB) in protein interactions and activity modulation.Semantic proximity Read ↗

An AAA protease FtsH can initiate proteolysis from internal sites of a model substrate, apo-flavodoxin.Semantic proximity Read ↗

Roles of multimerization and membrane association in the proteolytic functions of FtsH (HflB).Semantic proximity Read ↗

A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli.Semantic proximity Read ↗

Involvement of FtsH in protein assembly into and through the membrane. II. Dominant mutations affecting FtsH functions.Semantic proximity Read ↗

A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY.Semantic proximity Read ↗

Sequence and length recognition of the C-terminal turnover element of LpxC, a soluble substrate of the membrane-bound FtsH protease.Semantic proximity Read ↗

Evidence for coupling of membrane targeting and function of the signal recognition particle (SRP) receptor FtsY.Semantic proximity Read ↗

FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli.Semantic proximity Read ↗

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