The regions of securin and cyclin B proteins recognized by the ubiquitination machinery are natively unfolded
Open Access
- 21 August 2002
- journal article
- Published by Wiley in FEBS Letters
- Vol. 527 (1-3) , 303-308
- https://doi.org/10.1016/s0014-5793(02)03246-5
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
This publication has 44 references indexed in Scilit:
- Natively unfolded proteins: A point where biology waits for physicsProtein Science, 2002
- Statistics of local complexity in amino acid sequences and sequence databasesPublished by Elsevier ,2001
- Intrinsically unstructured proteins: re-assessing the protein structure-function paradigmJournal of Molecular Biology, 1999
- The interaction of eIF4E with 4E‐BP1 is an induced fit to a completely disordered proteinProtein Science, 1998
- Anaphase initiation in Saccharomyces cerevisiae is controlled by the APC-dependent degradation of the anaphase inhibitor Pds1p.Genes & Development, 1996
- Cut2 proteolysis required for sister-chromatid separation in fission yeastNature, 1996
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- Anaphase is initiated by proteolysis rather than by the inactivation of maturation-promoting factorCell, 1993
- Cross relaxation and spin diffusion effects on the proton NMR of biopolymers in H2OFEBS Letters, 1978
- Solvent peak saturation with single phase and quadrature fourier transformationJournal of Magnetic Resonance (1969), 1976