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Nucleic Acids Res. 1993 Nov 11;21(22):5092-100.

Specific cleavage of transcription factors by the thiol protease, m-calpain.

Author information

1
CSIRO Division of Biomolecular Engineering, Sydney Laboratory, North Ryde, NSW, Australia.

Abstract

The intracellular nonlysosomal calcium-dependent cysteine protease, m-calpain, is shown to specifically cleave the bHLHzip transcription factor USF leaving the binding and dimerisation domains intact. The resultant protein is capable of efficient DNA binding but is no longer able to activate transcription. A surprisingly high proportion of other transcription factors tested, AP1 (c-Fos/c-Jun), Pit-1, Oct-1, CP1a and b, c-Myc, ATF/CREB, AP2 and AP3 but not Sp1, were similarly cleaved by m-calpain to produce specific partial digestion products. These properties make m-calpain a particularly useful protease for proteolytic studies of transcription factors and also raise the possibility that m-calpain may be involved in vivo in regulation of turnover or transcriptional activity of a number of transcription factors.

PMID:
8255762
PMCID:
PMC310622
DOI:
10.1093/nar/21.22.5092
[Indexed for MEDLINE]
Free PMC Article

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