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The regions of securin and cyclin B proteins recognized by the ubiquitination machinery are natively unfolded
Author(s) -
Cox Cathleen J,
Dutta Kaushik,
Petri Edward T,
Hwang William C,
Lin Yaqiong,
Pascal Steven M,
Basavappa Ravi
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03246-5
Subject(s) - securin , proteasome , mitosis , microbiology and biotechnology , anaphase promoting complex , ubiquitin , cyclin b , cyclin , biology , chemistry , biochemistry , anaphase , cell cycle , ubiquitin ligase , cell , gene
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.