Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79

Ng, H. H., Xu, R. M., Zhang, Y., Struhl, K. (September 2002) Ubiquitination of histone H2B by Rad6 is required for efficient Dot1-mediated methylation of histone H3 lysine 79. Journal of Biological Chemistry, 277 (38). pp. 34655-34657. ISSN 0021-9258

URL: http://www.ncbi.nlm.nih.gov/pubmed/12167634
DOI: 10.1074/jbc.C200433200

Abstract

Dot1 is a non-SET domain protein that methylates histone H3 at lysine 79, a surface-exposed residue that lies within the globular domain. In the context of a nucleosome, H3 lysine 79 is located in close proximity with lysine 123 of histone H2B, a major site for ubiquitination by Rad6. Here we show that Rad6-mediated ubiquitination of H2B lysine 123 is important for efficient methylation of lysine 79, but not lysine 36, of histone H3. In contrast, lysine 79 methylation of H3 is not required for ubiquitination of H2B. Our study provides a new example of trans-histone regulation between modifications on different histones. In addition, it suggests that Rad6 affects telomeric silencing, at least in part, by influencing methylation of histone H3.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > histone
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein methylation > histone methylation
CSHL Authors:
Communities: CSHL labs > Xu lab
Depositing User: Matt Covey
Date: September 2002
Date Deposited: 07 Jan 2014 21:59
Last Modified: 07 Jan 2014 21:59
Related URLs:
URI: http://repository.cshl.edu/id/eprint/28756

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