(Q34031176)

30 July 2017

title

Proton-motive force stimulates the proteolytic activity of FtsH, a membrane-bound ATP-dependent protease in Escherichia coli (English)

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30 July 2017

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1 reference

Yoshinori Akiyama

1

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30 July 2017

language of work or name

English

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publication date

28 May 2002

1 reference

Proceedings of the National Academy of Sciences of the United States of America

30 July 2017

published in

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30 July 2017

volume

99

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30 July 2017

issue

12

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30 July 2017

page(s)

8066-8071

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The Sec protein-translocation pathway.

30 July 2017

cites work

1 reference

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5 July 2018

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Bacterial protein translocase: a unique molecular machine with an army of substrates.

5 July 2018

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Regulation by proteolysis: developmental switches

5 July 2018

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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.

5 July 2018

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The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events

5 July 2018

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Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli

5 July 2018

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Proteolysis of the phage lambda CII regulatory protein by FtsH (HflB) of Escherichia coli.

5 July 2018

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Host regulation of lysogenic decision in bacteriophage lambda: transmembrane modulation of FtsH (HflB), the cII degrading protease, by HflKC (HflA).

5 July 2018

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Proteases and their targets in Escherichia coli

5 July 2018

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Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coli.

5 July 2018

1 reference

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

5 July 2018

1 reference

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FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins

5 July 2018

1 reference

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Pro-OmpA derivatives with a His6 tag in their N-terminal "translocation initiation domains" are arrested by Ni2+ at an early post-targeting stage of translocation.

5 July 2018

1 reference

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The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression.

5 July 2018

1 reference

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

5 July 2018

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FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit

5 July 2018

1 reference

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Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB.

5 July 2018

1 reference

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Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

5 July 2018

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FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli

5 July 2018

1 reference

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The requirement for energy during export of beta-lactamase in Escherichia coli is fulfilled by the total protonmotive force

5 July 2018

1 reference

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

5 July 2018

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Production of abnormal proteins in E. coli stimulates transcription of lon and other heat shock genes

5 July 2018

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Diverse effects of the MalE-LacZ hybrid protein on Escherichia coli cell physiology

5 July 2018

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The SecY membrane component of the bacterial protein export machinery: analysis by new electrophoretic methods for integral membrane proteins

5 July 2018

1 reference

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Translocation of pro-OmpA across inner membrane vesicles of Escherichia coli occurs in two consecutive energetically distinct steps.

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=123021

The proton motive force lowers the level of ATP required for the in vitro translocation of a secretory protein in Escherichia coli.

5 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=123021

ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase

5 July 2018

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Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu

5 July 2018

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Roles of homooligomerization and membrane association in ATPase and proteolytic activities of FtsH in vitro

5 July 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.122616899

Dissecting the role of a conserved motif (the second region of homology) in the AAA family of ATPases. Site-directed mutagenesis of the ATP-dependent protease FtsH.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.122616899

Dislocation of membrane proteins in FtsH-mediated proteolysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.122616899

Revisiting the lysogenization control of bacteriophage lambda. Identification and characterization of a new host component, HflD.

21 January 2018

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https://api.crossref.org/works/10.1073%2FPNAS.122616899

Self-processing of FtsH and its implication for the cleavage specificity of this protease

21 January 2018

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https://api.crossref.org/works/10.1073%2FPNAS.122616899

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

21 January 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=123021

Proton motive force-dependent and -independent protein translocation revealed by an efficient in vitro assay system of Escherichia coli.

29 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=123021

Roles of the Periplasmic Domain ofEscherichia coliFtsH (HflB) in Protein Interactions and Activity Modulation

29 October 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.122616899

Heat shock regulation in the ftsH null mutant of Escherichia coli: dissection of stability and activity control mechanisms of sigma32 in vivo

21 January 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/12034886

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.122616899

1 reference

30 July 2017

0 references

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30 July 2017

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