MCB Accepts, published online ahead of print on 12 October 2009

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Google Scholar Articles by Psathas, J. N. Articles by Reese, J. C. PubMed PubMed Citation Articles by Psathas, J. N. Articles by Reese, J. C.

 Previous Article  |  Next Article 

Mol. Cell. Biol. doi:10.1128/MCB.00876-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Set2-dependent K36 methylation is regulated by novel intra-tail interactions within H3

James N. Psathas, Suting Zheng, Song Tan, and Joseph C. Reese^*

Department of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, Penn State University, University Park, PA 16802

^* To whom correspondence should be addressed. Email: Jcr8{at}psu.edu.

Post-translational modifications to histones have been studied extensively, but the requirement for the residues within the tails for different stages of transcription is less clear. Using RNR3 as a model, we find that the residues within the N-terminus of H3 are predominantly required for steps after transcription initiation and chromatin remodeling. Specifically, deleting as little as 20 amino acids, or substituting glutamines for lysines in the tail, greatly impaired K36 methylation by Set2. The mutations to the tail described here preserve the residues predicted to fill the active site of Set2 and the deletion mimics the recently described cleavage of the H3 tail that occurs during gene activation. Importantly, maintaining the charge of the unmodified tail by arginine substitutions preserves Set2 function in vivo. The H3 tail is dispensable for Set2 recruitment to genes, but is required for the catalytic activity of Set2 in vitro. We propose that Set2 activity is controlled by novel intra-tail interactions, which can be influenced by modifications and changes to the structure of the H3 tail to control the dynamics and localization of methylation during elongation.