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

201Citations
Citations of this article
164Readers
Mendeley users who have this article in their library.

This article is free to access.

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-Å 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. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc.

Cite

CITATION STYLE

APA

Li, Z., Cao, R., Wang, M., Myers, M. P., Zhang, Y., & Xu, R. M. (2006). Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex. Journal of Biological Chemistry, 281(29), 20643–20649. https://doi.org/10.1074/jbc.M602461200

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free