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FEBS Lett. 2008 Mar 5;582(5):691-8. doi: 10.1016/j.febslet.2008.01.044. Epub 2008 Feb 5.

The importance of conserved amino acid residues in p94 protease sub-domain IIb and the IS2 region for constitutive autolysis.

Author information

  • 1Department of Enzymatic Regulation for Cell Functions (Calpain Project), The Tokyo Metropolitan Institute of Medical Science (Rinshoken), Tokyo, Japan. yakoono@rinshoken.or.jp

Abstract

p94/calpain 3, a skeletal muscle-specific member of calpain protease family, is characterized by apparent Ca(2+)-independence during exhaustive autolysis and concomitant proteolysis of non-self substrates. The purpose of our study was to comprehensively profile the structural basis of p94 enabling activation in the cytosol without an extra Ca(2+). Ca(2+)-dependent p94 mutants were screened using "p94-trapping", which is an application of yeast genetic reporter system called "proteinase-trapping". Several amino acids were revealed as critical for apparent Ca(2+)-independent p94 activity. These results highlight the importance of conserved amino acids in domain IIb as well as in the p94-specific IS2 region.

PMID:
18258189
[PubMed - indexed for MEDLINE]
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