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

Dual role of the metalloprotease FtsH in biogenesis of the DrrAB drug transporter.

The Journal of biological chemistry - 26 Apr 2013

Li Wen, Rao Divya K, Kaur Parjit

Abstract excerpt

This study provides the first direct evidence for the dual role of the metalloprotease FtsH in membrane protein biogenesis. Using the physiological substrate DrrAB, it is shown that FtsH is not only responsible for proteolysis of unassembled DrrB protein but also plays a much broader role in biogenesis of the DrrAB complex. Previous studies showed that the stable expression of DrrB in the membrane depends on...

Read the complete abstract on PubMed

Topics

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

Share to Antibiotics, Antineoplastic
Share to ATP-Dependent Proteases
Share to Biological Transport, Active

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Doxorubicin

Share to Metalloproteases

Share to Molecular Chaperones

Share to Multiprotein Complexes

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 23504316
DOI: 10.1074/jbc.M112.441915
PMCID: PMC3636873

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Dual role of the metalloprotease FtsH in biogenesis of the DrrAB drug transporter.PMID 23504316Read ↗

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

Overexpression and functional characterization of an ABC (ATP-binding cassette) transporter encoded by the genes drrA and drrB of Mycobacterium tuberculosisSemantic proximity Read ↗

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

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

Escherichia coli FtsH is a membrane-bound, ATP-dependent protease which degrades the heat-shock transcription factor sigma 32.Semantic proximity Read ↗

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

Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli.Semantic proximity Read ↗

Conserved pore residues in the AAA protease FtsH are important for proteolysis and its coupling to ATP hydrolysis.Semantic proximity Read ↗

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

Characterization of the ftsH gene of Bacillus subtilis.Semantic proximity Read ↗

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

Characterization of mutants of the Escherichia coli AAA protease, FtsH, carrying a mutation in the central pore region.Semantic proximity Read ↗

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