The regions of securin and cyclin B proteins recognized by the ubiquitination machinery are natively unfolded

被引：38

作者：

Cox, CJ ^{[1
]}

Dutta, K ^{[1
]}

Petri, ET ^{[1
]}

Hwang, WC ^{[1
]}

Lin, YQ ^{[1
]}

Pascal, SM ^{[1
]}

Basavappa, R ^{[1
]}

机构：

[1] Univ Rochester, Sch Med & Dent, Dept Biochem & Biophys, Rochester, NY 14618 USA

来源：

FEBS LETTERS | 2002年 / 527卷 / 1-3期

关键词：

natively unfolded; mitosis; circular dichroism; nuclear magnetic resonance; cyclin B; securin;

D O I：

10.1016/S0014-5793(02)03246-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The proteins securin and cyclin B are destroyed in mitosis by the ubiquitin/proteasome system. This destruction is important to mitotic progression. The N-terminal regions of these proteins contain the sequence features recognized by the ubiquitination system. We have demonstrated using circular dichroism and 1-D and 2-D nuclear magnetic resonance that these rather substantial regions are natively unfolded. Based on these findings, we propose a model that helps to explain previously enigmatic observations. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

引用

页码：303 / 308

页数：6

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