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Molecular and Cellular Biology, October 2000, p. 7051-7058, Vol. 20, No. 19
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Type B Histone Acetyltransferase Hat1p Participates in Telomeric Silencing

Tamara J. Kelly,1 Song Qin,2 Daniel E. Gottschling,3 and Mark R. Parthun1,2,*

The Department of Molecular and Cellular Biochemistry1 and the Molecular, Cellular and Developmental Biology Program,2 The Ohio State University, Columbus, Ohio 43210, and Fred Hutchinson Cancer Research Center, Seattle, Washington 981093

Received 5 January 2000/Returned for modification 13 March 2000/Accepted 10 July 2000

Hat1p and Hat2p are the two subunits of a type B histone acetyltransferase from Saccharomyces cerevisiae that acetylates free histone H4 on lysine 12 in vitro. However, the role for these gene products in chromatin function has been unclear, as deletions of the HAT1 and/or HAT2 gene displayed no obvious phenotype. We have now identified a role for Hat1p and Hat2p in telomeric silencing. Telomeric silencing is the transcriptional repression of telomere-proximal genes and is mediated by a special chromatin structure. While there was no change in the level of silencing on a telomeric gene when the HAT1 or HAT2 gene was deleted, a significant silencing defect was observed when hat1Delta or hat2Delta was combined with mutations of the histone H3 NH2-terminal tail. Specifically, when at least two lysine residues were changed to arginine in the histone H3 tail, a hat1Delta -dependent telomeric silencing defect was observed. The most dramatic effects were seen when one of the two changes was in lysine 14. In further analysis, we found that a single lysine out of the five in the histone H3 tail was sufficient to mediate silencing. However, K14 was the best at preserving silencing, followed by K23 and then K27; K9 and K18 alone were insufficient. Mutational analysis of the histone H4 tail indicated that the role of Hat1p in telomeric silencing was mediated solely through lysine 12. Thus, in contrast to other histone acetyltransferases, Hat1p activity was required for transcriptional repression rather than gene activation.

* Corresponding author. Mailing address: Department of Molecular and Cellular Biochemistry, The Ohio State University, Columbus, OH 43210. Phone: (614) 292-6215. Fax: (614) 292-4118. E-mail: parthun.1{at}osu.edu.

Molecular and Cellular Biology, October 2000, p. 7051-7058, Vol. 20, No. 19
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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