PMID:16714294: Difference between revisions

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<span style = 'font-size: large'> '''Li, Z, Cao, R, Wang, M, Myers, MP, Zhang, Y and Xu, RM'''  (2006) Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex.''J. Biol. Chem.'' '''281''':20643-9</span>
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|{{TableHeadingColor}} |'''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.
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'''Li, Z, Cao, R, Wang, M, Myers, MP, Zhang, Y and Xu, RM'''  (2006) Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex. ''J. Biol. Chem.'' '''281''':20643-9
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!align=left  |Abstract
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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.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16714294 PubMed]
Online version:[http://dx.doi.org/10.1074/jbc.M602461200 10.1074/jbc.M602461200]
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|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16714294 PubMed]
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Crystallography, X-Ray; DNA-Binding Proteins/chemistry; Humans; Models, Molecular; Nuclear Proteins/chemistry; Polycomb Repressive Complex 1; Protein Conformation; Protein Structure, Secondary; Proto-Oncogene Proteins/chemistry; Recombinant Proteins/chemistry; Repressor Proteins/chemistry; Ubiquitin-Protein Ligases/chemistry
 
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Latest revision as of 04:30, 15 September 2013

Citation

Li, Z, Cao, R, Wang, M, Myers, MP, Zhang, Y and Xu, RM (2006) Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex. J. Biol. Chem. 281:20643-9

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.

Links

PubMed Online version:10.1074/jbc.M602461200

Keywords

Crystallography, X-Ray; DNA-Binding Proteins/chemistry; Humans; Models, Molecular; Nuclear Proteins/chemistry; Polycomb Repressive Complex 1; Protein Conformation; Protein Structure, Secondary; Proto-Oncogene Proteins/chemistry; Recombinant Proteins/chemistry; Repressor Proteins/chemistry; Ubiquitin-Protein Ligases/chemistry

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