Stabilization of FtsH-unfolded protein complex by binding of ATP and blocking of protease (Q38363928)

2 September 2017

title

Stabilization of FtsH-unfolded protein complex by binding of ATP and blocking of protease (English)

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2 September 2017

Hisayoshi Makyio

1

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2 September 2017

Hajime Niwa

2

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2 September 2017

Ken Motohashi

3

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2 September 2017

Hideki Taguchi

4

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2 September 2017

Masasuke Yoshida

5

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2 September 2017

language of work or name

English

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publication date

1 August 2002

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Biochemical and Biophysical Research Communications

2 September 2017

published in

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2 September 2017

volume

296

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2 September 2017

issue

1

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2 September 2017

page(s)

8-12

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AAA proteases: cellular machines for degrading membrane proteins

2 September 2017

cites work

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

7 January 2021

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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

7 January 2021

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

7 January 2021

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

7 January 2021

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

7 January 2021

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The HflB protease of Escherichia coli degrades its inhibitor lambda cIII

7 January 2021

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Degradation of carboxy-terminal-tagged cytoplasmic proteins by the Escherichia coli protease HflB (FtsH)

7 January 2021

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

7 January 2021

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

7 January 2021

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

7 January 2021

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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.

7 January 2021

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FtsH recognizes proteins with unfolded structure and hydrolyzes the carboxyl side of hydrophobic residues

7 January 2021

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

7 January 2021

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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.

7 January 2021

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

7 January 2021

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

7 January 2021

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A malachite green colorimetric assay for protein phosphatase activity

7 January 2021

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Quenched BODIPY dye-labeled casein substrates for the assay of protease activity by direct fluorescence measurement

7 January 2021

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

7 January 2021

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Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease

7 January 2021

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10.1016/S0006-291X(02)00830-6

7 January 2021

Identifiers

DOI

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2 September 2017

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