Roles of the Periplasmic Domain ofEscherichia coliFtsH (HflB) in Protein Interactions and Activity Modulation (Q57952178)

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3 December 2019

title

Roles of the periplasmic domain of Escherichia coli FtsH (HflB) in protein interactions and activity modulation (English)

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3 December 2019

Escherichia coli

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2

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3 December 2019

H Mori

3

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3 December 2019

author name string

Y Akiyama

1

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T Ogura

4

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K Ito

5

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3 December 2019

language of work or name

English

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publication date

1 August 1998

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Journal of Biological Chemistry

3 December 2019

published in

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volume

273

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issue

35

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page(s)

22326-22333

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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.

3 December 2019

cites work

1 reference

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Structure and function of the ftsH gene in Escherichia coli.

21 January 2018

1 reference

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Topology and subcellular localization of FtsH protein in Escherichia coli

21 January 2018

1 reference

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

21 January 2018

1 reference

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The tolZ gene of Escherichia coli is identified as the ftsH gene

21 January 2018

1 reference

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

21 January 2018

1 reference

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

21 January 2018

1 reference

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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.

21 January 2018

1 reference

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Cell growth and lambda phage development controlled by the same essential Escherichia coli gene, ftsH/hflB.

21 January 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).

21 January 2018

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

21 January 2018

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

21 January 2018

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Polypeptide binding of Escherichia coli FtsH (HflB).

21 January 2018

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

21 January 2018

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Rapid and efficient site-specific mutagenesis without phenotypic selection

21 January 2018

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A simple screen for permissive sites in proteins: analysis of Escherichia coli lac permease.

21 January 2018

1 reference

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Determinants of the quantity of the stable SecY complex in the Escherichia coli cell

21 January 2018

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TnphoA: a transposon probe for protein export signals

21 January 2018

1 reference

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Product of a new gene, syd, functionally interacts with SecY when overproduced in Escherichia coli.

21 January 2018

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Intracellular Stability of α Fragments of β-Galactosidase: Effects of Amino-Terminally Fused Polypeptides

21 January 2018

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Control of phage λ development by stability and synthesis of cll protein: Role of the viral clll and host hflA, himA and himD genes

21 January 2018

1 reference

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hflB, a new Escherichia coli locus regulating lysogeny and the level of bacteriophage lambda cII protein.

21 January 2018

1 reference

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A temperature-sensitive mutant of E. coli exhibiting slow processing of exported proteins

21 January 2018

1 reference

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Identification of the secY (prlA) gene product involved in protein export in Escherichia coli

21 January 2018

1 reference

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21 January 2018

Identifiers

DOI

10.1074/JBC.273.35.22326

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9712851%20AND%20SRC:MED&resulttype=core&format=json

3 December 2019

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