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Molecular and Cellular Biology, October 2005, p. 8887-8903, Vol. 25, No. 20
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.20.8887-8903.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Schizosaccharomyces pombe mst2⁺ Encodes a MYST Family Histone Acetyltransferase That Negatively Regulates Telomere Silencing

Eliana B. Gómez,^1,2 Joaquín M. Espinosa,^3,4 and Susan L. Forsburg^1,2*

Molecular and Cell Biology Laboratory,¹ Regulatory Biology Laboratory, The Salk Institute, La Jolla, California 92037,³ Molecular and Computational Biology Section, University of Southern California, 1050 Childs Way, Los Angeles, California 90089-2910,² Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, Colorado 80309⁴

Received 22 February 2005/ Returned for modification 23 March 2005/ Accepted 21 July 2005

Histone acetylation and deacetylation are associated with transcriptional activity and the formation of constitutively silent heterochromatin. Increasingly, histone acetylation is also implicated in other chromosome transactions, including replication and segregation. We have cloned the only Schizosaccharomyces pombe MYST family histone acetyltransferase genes, mst1⁺ and mst2⁺. Mst1p, but not Mst2p, is essential for viability. Both proteins are localized to the nucleus and bound to chromatin throughout the cell cycle. mst2 genetically interacts with mutants that affect heterochromatin, cohesion, and telomere structure. Mst2p is a negative regulator of silencing at the telomere but does not affect silencing in the centromere or mating type region. We generated a census of proteins and histone modifications at wild-type telomeres. A histone acetylation gradient at the telomeres is lost in mst2 cells without affecting the distribution of Taz1p, Swi6p, Rad21p, or Sir2p. We propose that the increased telomeric silencing is caused by histone hypoacetylation and/or an increase in the ratio of methylated to acetylated histones. Although telomere length is normal, meiosis is aberrant in mst2 diploid homozygote mutants, suggesting that telomeric histone acetylation contributes to normal meiotic progression.

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* Corresponding author. Mailing address: Molecular & Computational Biology Section, University of Southern California, 1050 Childs Way, Los Angeles, CA 90089-2910. Phone: (213) 740-7341. Fax: (213) 740-8631. E-mail: forsburg{at}usc.edu.

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

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Molecular and Cellular Biology, October 2005, p. 8887-8903, Vol. 25, No. 20
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.20.8887-8903.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

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