Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone.
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Summary
The findings suggest that the physiologically most significant function of DnaK in the metabolism of unstressed cells is its function in heat shock gene regulation.
- Type
- article
- Published
- 1990-12-01
- Cited by
- 147
- References
- 3
- Access
- Open access
- OpenAlex
- https://openalex.org/W42076805
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:12629057
Keywords
Biology, Mutant, RNA polymerase, Genetics, Protein subunit
References
Cited by
- Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB
- Biophysical Study of the Molecular Chaperone DnaK by Intramolecular FRET
- An Intracellular Probe of Hsc70:Substrate Interactions
- Enhanced heterologous gene expression in novel rpoH mutants of Escherichia coli
- Microbial molecular chaperones.
- Evaluation of the effects of gold nanoparticles (AuNPs) on protein folding in Escherichia coli
- DNA sequence analysis of the dnaK gene of Escherichia coli B and of two dnaK genes carrying the temperature-sensitive mutations dnaK7(Ts) and dnaK756(Ts)
- Components of a Protein Machine: Allosteric Domain Assembly and a Disordered C-terminus Enable the Chaperone Functions of Hsp70
- Effects of disruption of heat shock genes on susceptibility of Escherichia coli to fluoroquinolones
- The essential Escherichia coli msgB gene, a multicopy suppressor of a temperature-sensitive allele of the heat shock gene grpE, is identical to dapE
- Heat shock proteins DnaJ, DnaK, and GrpE stimulate P1 plasmid replication by promoting initiator binding to the origin
- Interaction of the targeting sequence of chloroplast precursors with Hsp70 molecular chaperones.
- Activity of mutant sigma F proteins truncated near the C terminus
- Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange
- Allosteric Regulation of Hsp70 Chaperones Involves a Conserved Interdomain Linker*
- Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor σ32
- Late steps of ribosome assembly in E. coli are sensitive to a severe heat stress but are assisted by the HSP70 chaperone machine
- Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones.
- Characterization of HscC (Hsc62), homologue of Hsp70 in Escherichia coli: over‐expression of HscC modulates the activity of house keeping sigma factor σ70
- SwoHp, a Nucleoside Diphosphate Kinase, Is Essential in Aspergillus nidulans
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