Peptidase activity of the Escherichia coli Hsp31 chaperone (Q45154612)

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title

Peptidase activity of the Escherichia coli Hsp31 chaperone (English)

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Hirotada Mori

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Abderrahim Malki

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Thérèse Caldas

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Renée Kern

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Viola Eckey

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So Jung Kim

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Sun-Shin Cha

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Gilbert Richarme

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language of work or name

English

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publication date

18 November 2004

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Journal of Biological Chemistry

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published in

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volume

280

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issue

15

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page(s)

14420-14426

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10 December 2017

cites work

The heat-shock proteins

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Characterization of the Escherichia coli YedU protein as a molecular chaperone

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Hsp31, the Escherichia coli yedU gene product, is a molecular chaperone whose activity is inhibited by ATP at high temperatures.

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The 1.6-A crystal structure of the class of chaperones represented by Escherichia coli Hsp31 reveals a putative catalytic triad

21 January 2018

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The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites

21 January 2018

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Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share an evolutionarily conserved domain

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A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function

21 January 2018

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One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products

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Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20 S proteasomes. Evidence for peptide-induced channel opening in the alpha-rings

21 January 2018

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The role of Tyr248 probed by mutant bovine carboxypeptidase A: insight into the catalytic mechanism of carboxypeptidase A.

21 January 2018

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Characterization and regulation of lens-specific calpain Lp82

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Degradation of intracellular protein in Salmonella typhimurium peptidase mutants

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PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress

21 January 2018

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PepN, the major Suc-LLVY-AMC-hydrolyzing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and eukarya. Implications in cytosolic protein degradation.

21 January 2018

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A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.

21 January 2018

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Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease

21 January 2018

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Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing

21 January 2018

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Interaction of the eukaryotic elongation factor 1A with newly synthesized polypeptides.

21 January 2018

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Posttranslational quality control: folding, refolding, and degrading proteins.

21 January 2018

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Escherichia coli Hsp31 functions as a holding chaperone that cooperates with the DnaK-DnaJ-GrpE system in the management of protein misfolding under severe stress conditions

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Identifiers

DOI

10.1074/JBC.M408296200

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10 December 2017

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