The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease (Q34616752)

3 August 2017

title

The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease (English)

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3 August 2017

Sarah A Bissonnette

1

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3 August 2017

Izarys Rivera-Rivera

series ordinal

2

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3 August 2017

Robert T Sauer

series ordinal

3

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3 August 2017

Tania A Baker

series ordinal

4

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3 August 2017

language of work or name

English

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publication date

10 February 2010

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3 August 2017

published in

Molecular Microbiology

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3 August 2017

volume

75

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3 August 2017

issue

6

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3 August 2017

page(s)

1539-1549

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describes a project that uses

3 August 2017

ImageQuant

1 reference

11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3934651/fullTextXML

inferred from PubMed Central ID database lookup

cites work

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Distinct activities of Escherichia coli small heat shock proteins IbpA and IbpB promote efficient protein disaggregation.

7 July 2018

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7 July 2018

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7 July 2018

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Substrate sequestration by a proteolytically inactive Lon mutant

7 July 2018

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7 July 2018

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The mammalian small heat-shock protein Hsp20 forms dimers and is a poor chaperone.

7 July 2018

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Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor

7 July 2018

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Lon-mediated proteolysis of the Escherichia coli UmuD mutagenesis protein: in vitro degradation and identification of residues required for proteolysis

7 July 2018

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Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivo

7 July 2018

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The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system

7 July 2018

1 reference

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A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state

7 July 2018

1 reference

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Role of the major heat shock proteins as molecular chaperones

7 July 2018

1 reference

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The function of heat-shock proteins in stress tolerance: degradation and reactivation of damaged proteins

7 July 2018

1 reference

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Repair, refold, recycle: how bacteria can deal with spontaneous and environmental damage to proteins

7 July 2018

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Protein degradation in Escherichia coli: the lon gene controls the stability of sulA protein

7 July 2018

1 reference

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The N-end rule in bacteria.

7 July 2018

1 reference

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Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3934651

Intermediate steps in the degradation of a specific abnormal protein in Escherichia coli

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3934651

Escherichia coli heat-shock proteins IbpA/B are involved in resistance to oxidative stress induced by copper.

7 July 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3934651

Small heat-shock proteins function in the insoluble protein complex.

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3934651

The small heat shock protein IbpA of Escherichia coli cooperates with IbpB in stabilization of thermally aggregated proteins in a disaggregation competent state.

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3934651

Refolding of substrates bound to small Hsps relies on a disaggregation reaction mediated most efficiently by ClpB/DnaK.

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3934651

Proteomic discovery of cellular substrates of the ClpXP protease reveals five classes of ClpX-recognition signals

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3934651

Protein aggregation in Escherichia coli: role of proteases

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3934651

Small heat shock proteins, IbpA and IbpB, are involved in resistances to heat and superoxide stresses in Escherichia coli.

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3934651

Proteomic Profiling of ClpXP Substrates after DNA Damage Reveals Extensive Instability within SOS Regulon

26 October 2018

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3934651

Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol

9 December 2018

1 reference

12 December 2020

The small heat-shock protein alpha B-crystallin promotes FBX4-dependent ubiquitination

1 reference

12 December 2020

Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation

1 reference

12 December 2020

IbpA and IbpB, the new heat-shock proteins, bind to endogenous Escherichia coli proteins aggregated intracellularly by heat shock

1 reference

12 December 2020

Structure-function studies on small heat shock protein oligomeric assembly and interaction with unfolded polypeptides

1 reference

12 December 2020

10.1111/J.1365-2958.2010.07070.X

Identifiers

DOI

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3 August 2017

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3 August 2017

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