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Molecular and Cellular Biology, May 2006, p. 3842-3852, Vol. 26, No. 10
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.10.3842-3852.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Deciphering the Roles of the Histone H2B N-Terminal Domain in Genome-Wide Transcription{dagger}

Michael A. Parra, David Kerr, Deirdre Fahy, Derek J. Pouchnik, and John J. Wyrick*

School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-4660

Received 15 December 2005/ Returned for modification 8 February 2006/ Accepted 6 March 2006

Histone N-terminal domains are frequent targets of posttranslational modifications. Multiple acetylated lysine residues have been identified in the N-terminal domain of H2B (K6, K11, K16, K17, K21, and K22), but little is known about how these modifications regulate transcription. We systematically mutated the N-terminal domain of histone H2B, both at known sites of lysine acetylation and elsewhere, and characterized the resulting changes in genome-wide expression in each mutant strain. Our results indicate that known sites of lysine acetylation in this domain are required for gene-specific transcriptional activation. However, the entire H2B N-terminal domain is principally required for the transcriptional repression of a large subset of the yeast genome. We find that the histone H2B repression (HBR) domain, comprised of residues 30 to 37, is necessary and sufficient for this repression. Many of the genes repressed by the HBR domain are located adjacent to telomeres or function in vitamin and carbohydrate metabolism. Deletion of the HBR domain also confers an increased sensitivity to DNA damage by UV irradiation. We mapped the critical residues in the HBR domain required for its repression function. Finally, comparisons of these data with previous studies reveal that a surprising number of genes are coregulated by the N-terminal domains of histone H2B, H3, and H4.

* Corresponding author. Mailing address: School of Molecular Biosciences, Washington State University, Fulmer Hall 675, Pullman, WA 99164-4660. Phone: (509) 335-8785. Fax: (509) 335-9688. E-mail: jwyrick{at}wsu.edu.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

Molecular and Cellular Biology, May 2006, p. 3842-3852, Vol. 26, No. 10
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.10.3842-3852.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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