FEBS Letters
Volume 527, Issue 1 , Pages 303-308, 11 September 2002

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

Edited by Stuart Ferguson

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

Received 27 May 2002; received in revised form 5 August 2002; accepted 6 August 2002.

Abstract 

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.

Keywords:  Natively unfolded, Mitosis, Circular dichroism, Nuclear magnetic resonance, Cyclin B, Securin

Abbreviations:  APC/C, anaphase promoting complex/cyclosome, CD, circular dichroism, NMR, nuclear magnetic resonance, NOE, nuclear Overhauser effect

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PII: S0014-5793(02)03246-5

FEBS Letters
Volume 527, Issue 1 , Pages 303-308, 11 September 2002

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