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Molecular and Cellular Biology, December 2001, p. 8082-8094, Vol. 21, No. 23
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.23.8082-8094.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Multiple Interactions in Sir Protein Recruitment by Rap1p at Silencers and Telomeres in Yeast

Paolo Moretti1,dagger and David Shore1,2,*

Department of Microbiology, College of Physicians & Surgeons of Columbia University, New York, New York 10032,1 and Department of Molecular Biology, Sciences II, University of Geneva, 1211 Geneva 4, Switzerland2

Received 14 June 2001/Returned for modification 13 July 2001/Accepted 28 August 2001

Initiation of transcriptional silencing at mating type loci and telomeres in Saccharomyces cerevisiae requires the recruitment of a Sir2/3/4 (silent information regulator) protein complex to the chromosome, which occurs at least in part through its association with the silencer- and telomere-binding protein Rap1p. Sir3p and Sir4p are structural components of silent chromatin that can self-associate, interact with each other, and bind to the amino-terminal tails of histones H3 and H4. We have identified a small region of Sir3p between amino acids 455 and 481 that is necessary and sufficient for association with the carboxyl terminus of Rap1p but not required for Sir complex formation or histone binding. SIR3 mutations that delete this region cause a silencing defect at HMR and telomeres. However, this impairment of repression is considerably less than that displayed by Rap1p carboxy-terminal truncations that are defective in Sir3p binding. This difference may be explained by the ability of the Rap1p carboxyl terminus to interact independently with Sir4p, which we demonstrate by in vitro binding and two-hybrid assays. Significantly, the Rap1p-Sir4p two-hybrid interaction does not require Sir3p and is abolished by mutation of the carboxyl terminus of Rap1p. We propose that both Sir3p and Sir4p can directly and independently bind to Rap1p at mating type silencers and telomeres and suggest that Rap1p-mediated recruitment of Sir proteins operates through multiple cooperative interactions, at least some of which are redundant. The physical separation of the Rap1p interaction region of Sir3p from parts of the protein required for Sir complex formation and histone binding raises the possibility that Rap1p can participate directly in the maintenance of silent chromatin through the stabilization of Sir complex-nucleosome interactions.

* Corresponding author. Mailing address: Department of Molecular Biology, Sciences II, University of Geneva, 30, Quai Ernest-Ansermet, 1211 Geneva 4, Switzerland. Phone: 41 22 702 6183. E-mail: David.Shore{at}molbio.unige.ch.

dagger Present address: Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030.

Molecular and Cellular Biology, December 2001, p. 8082-8094, Vol. 21, No. 23
0270-7306/01/$04.00+0   DOI: 10.1128/MCB.21.23.8082-8094.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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