Journal
BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS
Volume 1839, Issue 12, Pages 1353-1361Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagrm.2014.03.002
Keywords
Lysine methylation; Post-translational modifications; Histones; Chromatin; Gene transcription; RNA polymerase II
Categories
Funding
- National Science Foundation (NSF) [1330320]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1330320] Funding Source: National Science Foundation
Ask authors/readers for more resources
Histones and their posttranslational modifications (PTMs) play an important role in regulating DNA-templated processes. While some PTMs directly modulate chromatin architecture via charge effects, others rely on the action of reader or effector proteins that can recognize and bind the modification to fulfill distinct cellular outcomes. One VIM that has been well studied with regard to reader proteins is histone lysine methylation a VIM linked to many DNA-templated processes including transcription, DNA replication and DNA repair. In this review, we summarize the current understanding of how histone lysine methylation is read during the process of active transcription. We also describe how the interpretation of lysine methylation fits into a larger, more complex 'code' of histone PTMs to modulate chromatin structure and function. These insights take into account emerging concepts in the field in an effort to help facilitate future studies. This article is part of a Special Issue entitled: Methylation: A Multifaceted Modification looking at transcription and beyond. (C) 2014 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
Recommended
No Data Available