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Molecular and Cellular Biology, December 2009, p. 6413-6426, Vol. 29, No. 24
0270-7306/09/$08.00+0     doi:10.1128/MCB.00876-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Set2-Dependent K36 Methylation Is Regulated by Novel Intratail Interactions within H3{triangledown}

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, Pennsylvania 16802

Received 3 July 2009/ Returned for modification 8 August 2009/ Accepted 2 October 2009

Posttranslational 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 found that the residues within the N terminus of H3 are predominantly required for steps after transcription initiation and chromatin remodeling. Specifically, deleting as few 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 intratail 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.

* Corresponding author. Mailing address: Penn State University, Department of Biochemistry and Molecular Biology, 203 Althouse Lab, University Park, PA 16802. Phone: (814) 865-1976. Fax: (814) 863-7024. E-mail: Jcr8{at}psu.edu

{triangledown} Published ahead of print on 12 October 2009.

Molecular and Cellular Biology, December 2009, p. 6413-6426, Vol. 29, No. 24
0270-7306/09/$08.00+0     doi:10.1128/MCB.00876-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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