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

FEBS Letters

Pascal, Steven M¹  Hwang, William C¹  Dutta, Kaushik¹  Basavappa, Ravi¹  Cox, Cathleen J¹  Petri, Edward T¹  Lin, Yaqiong¹ 

[1] Department of Biochemistry and Biophysics, University of Rochester School of Medicine and Dentistry, 601 Elmwood Ave., Rochester, NY 14618, USA

关键词: Natively unfolded;    Mitosis;    Circular dichroism;    Nuclear magnetic resonance;    Cyclin B;    Securin;    APC/C;    anaphase promoting complex/cyclosome;    CD;    circular dichroism;    NMR;    nuclear magnetic resonance;    NOE;    nuclear Overhauser effect;   

DOI  :  10.1016/S0014-5793(02)03246-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown