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

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.
AuthorsYasuko Ono, Chikako Hayashi, Naoko Doi, Mai Tagami, Hiroyuki Sorimachi
JournalFEBS letters (FEBS Lett) Vol. 582 Issue 5 Pg. 691-8 (Mar 05 2008) ISSN: 0014-5793 [Print] England
PMID18258189 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Muscle Proteins
  • Mutant Proteins
  • Sodium
  • Peptide Hydrolases
  • CAPN3 protein, human
  • Calpain
  • Calcium
Topics
  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Calcium (pharmacology)
  • Calpain (chemistry, isolation & purification, metabolism)
  • Chlorocebus aethiops
  • Conserved Sequence
  • Models, Molecular
  • Molecular Sequence Data
  • Muscle Proteins (chemistry, isolation & purification, metabolism)
  • Mutant Proteins (chemistry, isolation & purification, metabolism)
  • Mutation (genetics)
  • Peptide Hydrolases (chemistry, metabolism)
  • Protein Processing, Post-Translational (drug effects)
  • Protein Structure, Tertiary
  • Sodium (pharmacology)
  • Structure-Activity Relationship
  • Substrate Specificity (drug effects)

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