Li, Z., Cao, R., Wang, M., Myers, M. P., Zhang, Y., Xu, R. M. (July 2006) Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex. J Biol Chem, 281 (29). pp. 20643-9. ISSN 0021-9258 (Print)
Abstract
Polycomb group proteins Bmi-1 and Ring1B are core subunits of the PRC1 complex, which plays important roles in the regulation of Hox gene expression, X-chromosome inactivation, tumorigenesis, and stem cell self-renewal. The RING finger protein Ring1B is an E3 ligase that participates in the ubiquitination of lysine 119 of histone H2A, and the binding of Bmi-1 stimulates the E3 ligase activity. We have mapped the regions of Bmi-1 and Ring1B required for efficient ubiquitin transfer and determined a 2.5-A structure of the Bmi-1-Ring1B core domain complex. The structure reveals that Ring1B "hugs" Bmi-1 through extensive RING domain contacts and its N-terminal tail wraps around Bmi-1. The two regions of interaction have a synergistic effect on the E3 ligase activity. Our analyses suggest a model where the Bmi-1-Ring1B complex stabilizes the interaction between the E2 enzyme and the nucleosomal substrate to allow efficient ubiquitin transfer.
Item Type: | Paper |
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Uncontrolled Keywords: | X-Ray Crystallography DNA-Binding Proteins chemistry Humans Models Molecular Nuclear Proteins chemistry Protein Conformation Protein Structure Secondary Proto-Oncogene Proteins chemistry Recombinant Proteins chemistry Repressor Proteins chemistry Ubiquitin-Protein Ligases chemistry |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > ubiquitin ligase Investigative techniques and equipment > x ray crystallography |
CSHL Authors: | |
Communities: | CSHL labs > Xu lab |
Depositing User: | CSHL Librarian |
Date: | 21 July 2006 |
Date Deposited: | 12 Dec 2011 16:45 |
Last Modified: | 19 Apr 2018 16:11 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/22852 |
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