Abstract
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 DDVD99 motif. In vitro, prothymosin α could be cleaved at D99 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.
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