Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex

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)

URL: https://www.ncbi.nlm.nih.gov/pubmed/16714294
DOI: 10.1074/jbc.M602461200

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
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: http://repository.cshl.edu/id/eprint/22852

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