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The importance of conserved amino acid residues in p94 protease sub‐domain IIb and the IS2 region for constitutive autolysis
Author(s) -
Ono Yasuko,
Hayashi Chikako,
Doi Naoko,
Tagami Mai,
Sorimachi Hiroyuki
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.01.044
Subject(s) - autolysis (biology) , proteolysis , calpain , protease , amino acid , biochemistry , mutant , biology , chemistry , microbiology and biotechnology , gene , enzyme
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.