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Article

Evidence for an active role of the DnaK chaperone system in the degradation of sigma(32).

FEBS letters - 4 Aug 2000

Tatsuta T, Joob D M, Calendar R, Akiyama Y, Ogura T

Abstract excerpt

Under non-stressed conditions in Escherichia coli, the heat shock transcription factor sigma(32) is rapidly degraded by the AAA protease FtsH. The DnaK chaperone system is also required for the rapid turnover of sigma(32) in the cell. It has been hypothesized that the DnaK chaperone system facilitates the degradation of sigma(32) by sequestering it from RNA polymerase core. This hypothesis predicts that mutant...

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Source

Identifiers

PMID: 10930581
DOI: 10.1016/s0014-5793(00)01869-x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Research trail→

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Evidence for an active role of the DnaK chaperone system in the degradation of sigma(32).PMID 10930581Read ↗

Conserved region 2.1 of Escherichia coli heat shock transcription factor sigma32 is required for modulating both metabolic stability and transcriptional activity.Semantic proximity Read ↗

The C terminus of sigma(32) is not essential for degradation by FtsH.Semantic proximity Read ↗

Role of region C in regulation of the heat shock gene-specific sigma factor of Escherichia coli, sigma32.Semantic proximity Read ↗

A Novel SRP Recognition Sequence in the Homeostatic Control Region of Heat Shock Transcription Factor σ32.Semantic proximity Read ↗

DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32.Semantic proximity Read ↗

Identification of a turnover element in region 2.1 of Escherichia coli sigma32 by a bacterial one-hybrid approach.Semantic proximity Read ↗

Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon.Semantic proximity Read ↗

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

Analysis of sigma32 mutants defective in chaperone-mediated feedback control reveals unexpected complexity of the heat shock response.Semantic proximity Read ↗

Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response.Semantic proximity Read ↗

A bacteriophage-encoded J-domain protein interacts with the DnaK/Hsp70 chaperone and stabilizes the heat-shock factor σ32 of Escherichia coli.Semantic proximity Read ↗

Genetic and biochemical characterization of mutations affecting the carboxy-terminal domain of the Escherichia coli molecular chaperone DnaJ.Semantic proximity Read ↗

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