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ID 20660
file
creator
subject
caspase
nuclear localization
prodomain
apoptosis
cytotoxic activity
NDC
Biology
abstract
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.
journal title
Biochemical and Biophysical Research Communications
volume
Volume 291
issue
Issue 1
start page
79
end page
84
date of issued
2002-02-15
publisher
Elsevier
issn
0006-291X
ncid
publisher doi
language
eng
nii type
Journal Article
HU type
Journal Articles
DCMI type
text
format
application/pdf
text version
author
rights
Copyright (c) 2002 Elsevier Science (USA).
relation url
department
Graduate School of Science