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Cited by 201

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A comprehensive library of histone mutants identifies nucleosomal residues required for H3K4 methylation

Open access
Nakanishi, Shima, Sanderson, Brian W, Delventhal, Kym M, Bradford, William D, Staehling-Hampton, Karen, Shilatifard, Ali·2008·Nature Structural & Molecular Biology

Abstract

Methylation of histone 3 lysine 4 (H3K4) by yeast Set1-COMPASS requires prior monoubiquitination of histone H2B. To define whether other residues within the histones are also required for H3K4 methylation, we systematically generated a complete library of the alanine substitutions of all of the residues of the four core histones in Saccharomyces cerevisiae. From this study we discovered that 18 residues within the four histones are essential for viability on complete growth media. We also identified several cis-regulatory residues on the histone H3 N-terminal tail, including histone H3 lysine 14 (H3K14), which are required for normal levels of H3K4 trimethylation. Several previously uncharacterized trans-regulatory residues on histones H2A and H2B form a patch on nucleosomes and are required for methylation mediated by COMPASS. This library will be a valuable tool for defining the role of histone residues in processes requiring chromatin.

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Metadata

Authors
Nakanishi, S., Sanderson, B. W., Delventhal, K. M., Bradford, W. D., Staehling-Hampton, K., & Shilatifard, A.
Venue
Nature Structural & Molecular Biology
Published
2008-07-11
Volume
15
Issue
8
Pages
881-888
ISSN
  • 1545-9985 (ISSN-L)
  • 1545-9993
OpenAlex
W2088831308
Cited by
201
References
1
FWCI
6.45
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: A comprehensive library of histone mutants identifies nucleosomal residues required for H3K4 methylation. https://app.cochat.ai/papers/10.1038/nsmb.1454
The paper
Nakanishi, S., Sanderson, B. W., Delventhal, K. M., Bradford, W. D., Staehling-Hampton, K., & Shilatifard, A. (2008). A comprehensive library of histone mutants identifies nucleosomal residues required for H3K4 methylation. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1454

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