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Molecular and Cellular Biology, April 2008, p. 2154-2166, Vol. 28, No. 7
0270-7306/08/$08.00+0     doi:10.1128/MCB.01637-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Chp1-Tas3 Interaction Is Required To Recruit RITS to Fission Yeast Centromeres and for Maintenance of Centromeric Heterochromatin{triangledown} ,{dagger}

Jennifer L. DeBeauchamp,{ddagger} Arian Moses,{ddagger},§ Victoria J. P. Noffsinger, Dagny L. Ulrich,|| Godwin Job, Aaron M. Kosinski,{dagger}{dagger} and Janet F. Partridge*

Department of Biochemistry, St. Jude Children's Research Hospital, Memphis, Tennessee 38105

Received 4 September 2007/ Returned for modification 29 October 2007/ Accepted 7 January 2008

The maintenance of centromeric heterochromatin in fission yeast relies on the RNA interference-dependent complexes RITS (RNA-induced transcriptional silencing complex) and RDRC (RNA-directed RNA polymerase complex), which cooperate in a positive feedback loop to recruit high levels of histone H3 K9 methyltransferase activity to centromeres and to promote the assembly and maintenance of centromeric heterochromatin. However, it is unclear how these complexes are targeted to chromatin. RITS comprises Chp1, which binds K9-methylated histone H3; Ago1, which binds short interfering (siRNAs); the adaptor protein Tas3, which links Ago1 to Chp1; and centromeric siRNAs. We have generated mutants in RITS to determine the contribution of the two potential chromatin-targeting proteins Chp1 and Ago1 to the centromeric recruitment of RITS. Mutations in Tas3 that disrupt Ago1 binding are permissive for RITS recruitment and maintain centromeric heterochromatin, but the role of Tas3's interaction with Chp1 is unknown. Here, we define the Chp1 interaction domain of Tas3. A strain expressing a tas3 mutant that cannot bind Chp1 (Tas3{Delta}10-24) failed to maintain centromeric heterochromatin, with a loss of centromeric siRNAs, a failure to recruit RITS and RDRC to centromeres, and high levels of chromosome loss. These findings suggest a pivotal role for Chp1 and its association with Tas3 for the recruitment of RITS, RDRC, and histone H3 K9 methyltransferase activity to centromeres.

* Corresponding author. Mailing address: Mailstop 340, Department of Biochemistry, St. Jude Children's Research Hospital, 332 N. Lauderdale, Memphis, TN 38105. Phone: (901) 495-2679. Fax: (901) 525-8025. E-mail: Janet.Partridge{at}stjude.org

{triangledown} Published ahead of print on 22 January 2008.

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

{ddagger} These authors contributed equally to this work.

§ Present address: Case Western Reserve University, Cleveland, OH 44106.

Present address: University of Kentucky, Lexington, KY 40506.

|| Present address: Department of Pharmaceutical Sciences, St. Jude Children's Research Hospital, Memphis, TN 38105.

{dagger}{dagger} Present address: Department of Chemical Biology, St. Jude Children's Research Hospital, Memphis, TN 38105.

Molecular and Cellular Biology, April 2008, p. 2154-2166, Vol. 28, No. 7
0270-7306/08/$08.00+0     doi:10.1128/MCB.01637-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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