Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling (Q35002522)

5 August 2017

title

Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling (English)

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5 August 2017

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5

Sue Wickner

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5 August 2017

Olivier Genest

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5 August 2017

Joel R Hoskins

series ordinal

2

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5 August 2017

Jodi L Camberg

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3

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5 August 2017

Shannon M Doyle

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4

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5 August 2017

language of work or name

English

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publication date

27 April 2011

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

5 August 2017

published in

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5 August 2017

volume

108

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5 August 2017

issue

20

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5 August 2017

page(s)

8206-8211

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Conformational dynamics of the molecular chaperone Hsp90

5 August 2017

cites work

1 reference

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8 July 2018

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ClpXP protease degrades the cytoskeletal protein, FtsZ, and modulates FtsZ polymer dynamics

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Species-dependent ensembles of conserved conformational states define the Hsp90 chaperone ATPase cycle

8 July 2018

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Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements

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8 July 2018

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Large-scale identification of protein-protein interaction of Escherichia coli K-12

8 July 2018

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ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release

8 July 2018

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The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

8 July 2018

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Stepwise assembly of a glucocorticoid receptor.hsp90 heterocomplex resolves two sequential ATP-dependent events involving first hsp70 and then hsp90 in opening of the steroid binding pocket

8 July 2018

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HtpG is essential for the thermal stress management in cyanobacteria

8 July 2018

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Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones

8 July 2018

1 reference

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Mutations in the substrate binding domain of the Escherichia coli 70 kDa molecular chaperone, DnaK, which alter substrate affinity or interdomain coupling

8 July 2018

1 reference

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In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis

8 July 2018

1 reference

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The role of the ClpA chaperone in proteolysis by ClpAP

8 July 2018

1 reference

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ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo

8 July 2018

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A bacterial two-hybrid system based on a reconstituted signal transduction pathway

8 July 2018

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Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence

8 July 2018

1 reference

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Hop modulates Hsp70/Hsp90 interactions in protein folding

8 July 2018

1 reference

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The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation

8 July 2018

1 reference

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Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone

8 July 2018

1 reference

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Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent

8 July 2018

1 reference

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An analogue of the DnaJ molecular chaperone in Escherichia coli

8 July 2018

1 reference

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DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage.

8 July 2018

1 reference

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Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase

8 July 2018

1 reference

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Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo

8 July 2018

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A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli

8 July 2018

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Ancient heat shock gene is dispensable

8 July 2018

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Hsp90 chaperones protein folding in vitro.

8 July 2018

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Ribosomal protein L2 associates with E. coli HtpG and activates its ATPase activity

8 July 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1104703108

Multiple conformations of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1104703108

Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1104703108

Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1104703108

Substrate transfer from the chaperone Hsp70 to Hsp90.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1104703108

CbpA, a DnaJ homolog, is a DnaK co-chaperone, and its activity is modulated by CbpM.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1104703108

Analysis of three DnaK mutant proteins suggests that progression through the ATPase cycle requires conformational changes

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1104703108

Functional analysis of CbpA, a DnaJ homolog and nucleoid-associated DNA-binding protein.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1104703108

The amino-terminal domain of ClpB supports binding to strongly aggregated proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1104703108

Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery.

21 January 2018

1 reference

https://api.crossref.org/works/10.1073%2FPNAS.1104703108

The interplay of the GrpE heat shock protein and Mg2+ in RepA monomerization by DnaJ and DnaK.

21 January 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3100916

The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes

26 October 2018

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21525416

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

HtpG, the prokaryotic homologue of Hsp90, stabilizes a phycobilisome protein in the cyanobacterium Synechococcus elongatus PCC 7942

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21525416

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/21525416

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1073/PNAS.1104703108

1 reference

5 August 2017

0 references

1 reference

5 August 2017

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