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Ubiquitination of Histone H2B by Rad6 Is Required for Efficient Dot1-mediated Methylation of Histone H3 Lysine 79

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Ng, Huck Hui, Xu, Rui-Ming, Zhang, Yi, Struhl, Kevin·2002·Journal of Biological Chemistry

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.

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Metadata

Authors
Ng, H. H., Xu, R.-M., Zhang, Y., & Struhl, K.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2002-09
Volume
277
Issue
38
Pages
34655-34657
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1989092936
Cited by
432
References
0
FWCI
7.67
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Ubiquitination of Histone H2B by Rad6 Is Required for Efficient Dot1-mediated Methylation of Histone H3 Lysine 79. https://app.cochat.ai/papers/10.1074/jbc.c200433200
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Ng, H. H., Xu, R.-M., Zhang, Y., & Struhl, K. (2002). Ubiquitination of Histone H2B by Rad6 Is Required for Efficient Dot1-mediated Methylation of Histone H3 Lysine 79. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.c200433200

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