Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2-Reference-Cited by-同舟云学术

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Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2

Published:2006-05-21 Issue:7098 Volume:442 Page:100-103
ISSN:0028-0836
Container-title:Nature
language:en
Short-container-title:Nature

Author:

Peña Pedro V.,Davrazou Foteini,Shi Xiaobing,Walter Kay L.,Verkhusha Vladislav V.,Gozani Or,Zhao Rui,Kutateladze Tatiana G.

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/nature04814.pdf

Reference27 articles.

1. Santos-Rosa, H. et al. Active genes are tri-methylated at K4 of histone H3. Nature 419, 407–411 (2002)

2. Schneider, R. et al. Histone H3 lysine 4 methylation patterns in higher eukaryotic genes. Nature Cell Biol. 6, 73–77 (2004)

3. Briggs, S. D. et al. Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiae. Genes Dev. 15, 3286–3295 (2001)

4. Sims, R. J. III, Nishioka, K. & Reinberg, D. Histone lysine methylation: a signature for chromatin function. Trends Genet. 19, 629–639 (2003)

5. Shi, X. et al. ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature doi:10.1038/nature04835 (2006).

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