4.5 Review

Histone arginine methylation

Journal

FEBS LETTERS
Volume 585, Issue 13, Pages 2024-2031

Publisher

ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2010.11.010

Keywords

Arginine methylation; Histone code; Tudor domain; CARM1; ChIP-seq

Funding

  1. NIH [DK62248]

Ask authors/readers for more resources

Arginine methylation is a common posttranslational modification (PTM). This type of PTM occurs on both nuclear and cytoplasmic proteins, and is particularly abundant on shuttling proteins. In this review, we will focus on one aspect of this PTM: the diverse roles that arginine methylation of the core histone tails play in regulating chromatin function. A family of nine protein arginine methyltransferases (PRMTs) catalyze methylation reactions, and a subset target histones. Importantly, arginine methylation of histone tails can promote or prevent the docking of key transcriptional effector molecules, thus playing a central role in the orchestration of the histone code. (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available