The inhibition of the nuclear transport of caspase-7 by its prodomain
BBRC_291-1_79.pdf 1.1 MB
Apoptosis is a major form of cell death, characterized by a series of the morphological changes induced by cleaving cytoplasmic and nuclear proteins via active caspases. The data presented here show, by the fluorescence microscopic and the immunoblotting analyses, that a prodomain of caspase-7 inhibits its nuclear translocation and apoptosis-inducing activity. This nuclear localization is dependent on the presence of a basic tetrapeptide that is conserved in mammalian and Xenopus caspase-7 and that is located downstream of a cleavage site between a prodomain and a catalytic protease domain. Furthermore, an attachment of caspase-7 prodomain (31 amino acids) represses the nuclear transport of a fusion protein of a heterologous protein and the caspase-7 nuclear localization signal (19 amino acids), suggesting that the inhibition of the nuclear localization by the prodomain is mediated by the interaction of these short peptides.
Biochemical and Biophysical Research Communications
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Copyright (c) 2002 Elsevier Science (USA).
Graduate School of Science
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