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Monoubiquitination of Human Histone H2B: The Factors Involved and Their Roles in HOX Gene Regulation

Monoubiquitination of Human Histone H2B: The Factors Involved and Their Roles in HOX Gene Regulation

Bing Zhu, Yong Zheng, Anh-Dung Pham, Subhrangsu S Mandal, Hediye Erdjument-Bromage, Paul Tempst, Danny Reinberg

Mol Cell. 2005 Nov 23;20(4):601-11.

PMID: 16307923

Abstract:

In yeast, histone H2B monoubiquitination is a cotranscriptional event regulating histone H3 methylation at lysines 4 and 79. However, mammalian H2B monoubiquitination remains poorly understood. We report that in humans, the 600 kDa RNF20/40 complex is the E3 ligase and UbcH6 is the ubiquitin E2-conjugating enzyme for H2B-Lys120 monoubiquitination. RNF20 and RNF40 are both homologs of Bre1, the E3 ligase in the yeast case. UbcH6 physically interacts with RNF20/40 and with the hPAF complex. Formation of a trimeric complex with hPAF stimulates H2B monoubiquitination activity in vitro. Accordingly, UbcH6, RNF20/40, and the hPAF complex are recruited to transcriptionally active genes in vivo. RNF20 overexpression leads to elevated H2B monoubiquitination, subsequently higher levels of methylation at H3 lysines 4 and 79, and stimulation of HOX gene expression. In contrast, RNAi against the RNF20/40 complex or hPAF complex reduces H2B monoubiquitination, lowers methylation levels at H3 lysines 4 and 79, and represses HOX gene expression.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
IAR42415052	RNF20 active human			Price

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