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ID 20660
本文ファイル
著者
キーワード
caspase
nuclear localization
prodomain
apoptosis
cytotoxic activity
NDC
生物科学・一般生物学
抄録(英)
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.
掲載誌名
Biochemical and Biophysical Research Communications
291巻
1号
開始ページ
79
終了ページ
84
出版年月日
2002-02-15
出版者
Elsevier
ISSN
0006-291X
NCID
出版者DOI
言語
英語
NII資源タイプ
学術雑誌論文
広大資料タイプ
学術雑誌論文
DCMIタイプ
text
フォーマット
application/pdf
著者版フラグ
author
権利情報
Copyright (c) 2002 Elsevier Science (USA).
関連情報URL
部局名
理学研究科