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Molecular and Cellular Biology, December 2002, p. 8292-8301, Vol. 22, No. 23
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.23.8292-8301.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Esc1, a Nuclear Periphery Protein Required for Sir4-Based Plasmid Anchoring and Partitioning

Erik D. Andrulis,1,{dagger} David C. Zappulla,1 Athar Ansari,2 Severine Perrod,3 Catherine V. Laiosa,2 Marc R. Gartenberg,2* and Rolf Sternglanz1*

Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, New York 11794-5215,1 Department of Pharmacology, University of Medicine and Dentistry of New Jersey-Robert Wood Johnson Medical School, Piscataway, New Jersey 08854,2 Swiss Institute for Experimental Cancer Research (ISREC), CH-1066 Epalinges/Lausanne, Switzerland3

Received 31 July 2002/ Accepted 5 September 2002

A targeted silencing screen was performed to identify yeast proteins that, when tethered to a telomere, suppress a telomeric silencing defect caused by truncation of Rap1. A previously uncharacterized protein, Esc1 (establishes silent chromatin), was recovered, in addition to well-characterized proteins Rap1, Sir1, and Rad7. Telomeric silencing was slightly decreased in {Delta}esc1 mutants, but silencing of the HM loci was unaffected. On the other hand, targeted silencing by various tethered proteins was greatly weakened in {Delta}esc1 mutants. Two-hybrid analysis revealed that Esc1 and Sir4 interact via a 34-amino-acid portion of Esc1 (residues 1440 to 1473) and a carboxyl-terminal domain of Sir4 known as PAD4 (residues 950 to 1262). When tethered to DNA, this Sir4 domain confers efficient partitioning to otherwise unstable plasmids and blocks the ability of bound DNA segments to rotate freely in vivo. Here, both phenomena were shown to require ESC1. Sir protein-mediated partitioning of a telomere-based plasmid also required ESC1. Fluorescence microscopy of cells expressing green fluorescent protein (GFP)-Esc1 showed that the protein localized to the nuclear periphery, a region of the nucleus known to be functionally important for silencing. GFP-Esc1 localization, however, was not entirely coincident with telomeres, the nucleolus, or nuclear pore complexes. Our data suggest that Esc1 is a component of a redundant pathway that functions to localize silencing complexes to the nuclear periphery.

* Corresponding authors. Mailing address for Marc R. Gartenberg: Department of Pharmacology, UMDNJ-Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854. Phone: (732) 235-5800. Fax: (732) 235-4073. E-mail: gartenbe{at}UMDNJ.EDU. Mailing address for Rolf Sternglanz: Department of Biochemistry and Cell Biology, State University of New York, Stony Brook, NY 11794-5215. Phone: (631) 632-8565. Fax: (631) 632-8575. E-mail: rolf{at}life.bio.sunysb.edu.

{dagger} Present address: Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853.

Molecular and Cellular Biology, December 2002, p. 8292-8301, Vol. 22, No. 23
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.23.8292-8301.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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