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Prothymosin α fragmentation in apoptosis
Author(s) -
Evstafieva Alexandra G.,
Belov George A.,
Kalkum Markus,
Chichkova Nina V.,
Bogdanov Alexey A.,
Agol Vadim I.,
Vartapetian Andrey B.
Publication year - 2000
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/s0014-5793(00)01139-x
Subject(s) - apoptosis , fragmentation (computing) , microbiology and biotechnology , nuclear protein , cleavage (geology) , peptide , dna fragmentation , nuclear localization sequence , in vitro , nucleus , caspase 3 , cell nucleus , programmed cell death , chemistry , cell growth , biology , biochemistry , transcription factor , gene , ecology , paleontology , fracture (geology)
We observed fragmentation of an essential proliferation‐related human nuclear protein prothymosin α in the course of apoptosis induced by various stimuli. Prothymosin α cleavage occurred at the DDVD 99 motif. In vitro, prothymosin α could be cleaved at D 99 by caspase‐3 and ‐7. Caspase hydrolysis disrupted the nuclear localization signal of prothymosin α and abrogated the ability of the truncated protein to accumulate inside the nucleus. Prothymosin α fragmentation may therefore be proposed to disable intranuclear proliferation‐related function of prothymosin α in two ways: by cleaving off a short peptide containing important determinants, and by preventing active nuclear uptake of the truncated protein.