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PMID:24148697

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Citation

'Lenz, G and Ron, EZ (2013) Novel interaction between the major bacterial heat shock chaperone (GroESL) and an RNA chaperone (CspC). J. Mol. Biol. '

Abstract

The heat shock response is one of the main global regulatory networks in all organisms and involves an increased cellular level of chaperones and proteases to enable correct protein folding and balanced growth. One of the major heat shock chaperones in Escherichia coli is GroESL, comprised of GroES and GroEL (the bacterial Hsp60 homologue), which is essential for refolding of misfolded proteins. GroESL was previously shown to play a role in the regulation of the heat shock response by promoting the proteolysis of the regulatory protein - sigma32 (RpoH), the heat shock transcription activator. Here we show the involvement of GroESL in another proteolytic process, this of the major RNA chaperone - CspC - that specifically stabilizes the transcripts of several stress-related genes. Evidence is provided for an interaction between GroESL and CspC that results in enhanced, temperature dependent, proteolysis of the latter. This interaction is of regulatory importance, as reduction in the cellular levels of CspC leads to a decrease in stability of the major heat shock gene transcripts.

Links

PubMed Online version:10.1016/j.jmb.2013.10.018

Keywords


Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:CSPC

GO:0051087: chaperone binding

ECO:0000314:

F

Figure 5 of the paper shows that CspC levels decrease when GroEL is overexpressed.

complete
CACAO 8919

ECOLI:CSPC

enables

GO:0051087: chaperone binding

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

See also

References

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