Premium
CPP32/Yama/apopain cleaves the catalytic component of DNA‐dependent protein kinase in the holoenzyme
Author(s) -
Teraoka Hirobumi,
Yumoto Yoshiko,
Watanabe Fumiaki,
Tsukada Kinji,
Suwa Akira,
Enari Masato,
Nagata Shigekazu
Publication year - 1996
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 - 10.1016/0014-5793(96)00842-3
Subject(s) - jurkat cells , dna , microbiology and biotechnology , raji cell , chemistry , recombinant dna , biochemistry , in vitro , biology , gene , immunology , immune system , t cell
DNA‐dependent protein kinase (DNA‐PK) is composed of a 460‐kDa catalytic component (p460) and a DNA‐binding component Ku protein. Immunoblot analysis after treatment of Jurkat cells with anti‐Fas antibody demonstrated the cleavage of p460 concomitantly with an increase in CPP32/Yama/apopain activity. Recombinant CPP32/Yama/apopain specifically cleaved p460 in the DNA‐PK preparation that had been purified from Raji cells into 230‐ and 160‐kDa polypeptides, the latter of which was detected in anti‐Fas‐treated Jurkat cells. The regulatory component Ku protein was not significantly affected by CPP32/Yama/apopain. DNA‐PK activity was decreased with the disappearance of p460 in the incubation of DNA‐PK with CPP32/Yama/apopain. These results suggest that the catalytic component of DNA‐PK is one of the target proteins for CPP32/Yama/apopain in Fas‐mediated apoptosis.