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Synergistic Binding of DnaJ and DnaK Chaperones to Heat Shock Transcription Factor σ(32) Ensures Its Characteristic High Metabolic Instability: IMPLICATIONS FOR HEAT SHOCK PROTEIN 70 (Hsp70)-Hsp40 MODE OF FUNCTION
Escherichia coli heat shock transcription factor σ(32) is rapidly degraded by ATP-dependent proteases, such as FtsH and ClpYQ. Although the DnaK chaperone system (DnaK, DnaJ, and GrpE) promotes σ(32) degradation in vivo, the precise mechanism that is involved remains unknown. Our previous results in...
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| Main Authors: | , , , , , , |
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| Formáid: | Artigo |
| Teanga: | Inglês |
| Foilsithe: |
American Society for Biochemistry and Molecular Biology
2012
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| Ábhair: | |
| Rochtain Ar Líne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3365959/ https://ncbi.nlm.nih.gov/pubmed/22496372 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.331470 |
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