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J. Biol. Chem., Vol. 279, Issue 23, 24323-24333, June 4, 2004

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Stm1p, a G₄ Quadruplex and Purine Motif Triplex Nucleic Acid-binding Protein, Interacts with Ribosomes and Subtelomeric Y' DNA in Saccharomyces cerevisiae^*

Michael W. Van Dyke, Laura D. Nelson, Rodney G. Weilbaecher, and Dakshesh V. Mehta

From the Department of Molecular and Cellular Oncology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030

The Saccharomyces cerevisiae protein Stm1 was originally identified as a G4 quadruplex and purine motif triplex nucleic acid-binding protein. However, more recent studies have suggested a role for Stm1p in processes ranging from antiapoptosis to telomere maintenance. To better understand the biological role of Stm1p and its potential for G^*G multiplex binding, we used epitope-tagged protein and immunological methods to identify the subcellular localization and protein and nucleic acid partners of Stm1p in vivo. Indirect immunofluorescence microscopy indicated that Stm1p is primarily a cytoplasmic protein, although a small percentage is also present in the nucleus. Conventional immunoprecipitation found that Stm1p is associated with ribosomal proteins and rRNA. This association was verified by rate zonal separation through sucrose gradients, which showed that Stm1p binds exclusively to mature 80 S ribosomes and polysomes. Chromatin immunoprecipitation experiments found that Stm1p preferentially binds telomere-proximal Y' element DNA sequences. Taken together, our data suggest that Stm1p is primarily a ribosome-associated protein, but one that can also interact with DNA, especially subtelomeric sequences. We discuss the implications of our findings in relation to prior genetic, genomic, and proteomic studies that have identified STM1 and/or Stm1p as well as the possible biological role of Stm1p.

Received for publication, February 23, 2004

^* This work was supported by Robert A. Welch Foundation Grant G-1199 (to M. W. V. D.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Aurigene Discovery Technology Ltd., Electronic City Phase II, Hosur Rd., 39-40 KIABD Industrial Area, Bangalore 560 100, India.

To whom correspondence should be addressed: Dept. of Molecular and Cellular Oncology, The University of Texas M. D. Anderson Cancer Center, Unit 79, 1515 Holcombe Blvd., Houston, TX 77030-4009. Tel.: 713-792-8954; Fax: 713-794-0209; E-mail: mvandyke{at}mdanderson.org.

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