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

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

The Journal of biological chemistry - 18 Feb 1994

Akiyama Y, Shirai Y, Ito K

Abstract excerpt

FtsH is an Escherichia coli protein with its amino-terminal region anchored to the cytoplasmic membrane and with its cytoplasmic domain significantly homologous to the members of an ATPase family found in eukaryotic cells. We previously showed that the loss of ftsH function results in reduced cytoplasmic retention of the alkaline phosphatase moiety that was attached to cytoplasmic regions of membrane proteins...

Topics

ATP-Dependent Proteases
Adenosine Triphosphatases
Amino Acid Sequence
Bacterial Proteins
Base Sequence
Consensus Sequence
DNA Primers
Escherichia coli
Escherichia coli Proteins
Genes, Bacterial
Genes, Dominant

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Membrane Proteins

Molecular Sequence Data

Mutagenesis, Site-Directed

Phenotype

Restriction Mapping

Source

Identifiers

PMID: 8106505

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8106505-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

0

discussions

0

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Involvement of FtsH in protein assembly into and through the membrane. II. Dominant mutations affecting FtsH functions.PMID 8106505Read ↗

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

Structure and function of the ftsH gene in Escherichia coli.Semantic proximity Read ↗

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

A new Escherichia coli gene, fdrA, identified by suppression analysis of dominant negative FtsH mutations.Semantic proximity Read ↗

Suppression of ftsH mutant phenotypes by overproduction of molecular chaperones.Semantic proximity Read ↗

Construction and analyses of mutant ftsH alleles of Bacillus subtilis involving the ATPase- and Zn-binding domains.Semantic proximity Read ↗

Defective plasmid partition in ftsH mutants of Escherichia coli.Semantic proximity Read ↗

A Lactococcus lactis gene encodes a membrane protein with putative ATPase activity that is homologous to the essential Escherichia coli ftsH gene product.Semantic proximity Read ↗

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

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

Dislocation of membrane proteins in FtsH-mediated proteolysis.Semantic proximity Read ↗

FtsL, an essential cytoplasmic membrane protein involved in cell division in Escherichia coli.Semantic proximity Read ↗

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