The Telomere-Binding Protein Taz1p as a Target for Modification by a SUMO-1 Homologue in Fission Yeast |
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Authors: | K Spink J C Y Ho K Tanaka F Z Watts A Chambers |
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Institution: | (1) Present address: Institute of Genetics, School of Biology, University of Nottingham, Queen s Medical Centre, Nottingham, United Kingdom;(2) Pfizer Limited, Ramsgate Road, Sandwich, Kent, United Kingdom;(3) Department of Biochemistry, School of Biological Sciences, University of Sussex, Falmer, Brighton, United Kingdom;(4) Department of Applied Bioscience and Biotechnology, Faculty of Life and Environmental Science, Shimane University, Matsue, Japan |
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Abstract: | In fission yeast (Schizosaccharomyces pombe) the homologue of the mammalian SUMO-1 ubiquitin-like modifier is encoded by the pmt3 gene. A two-hybrid screen using the telomere-binding protein Taz1p as bait identified Pmt3p as an interacting factor. In vitro experiments using purified components of the fission yeast Pmt3p modification system demonstrated that Taz1p could be modified directly by Pmt3p. The amino acid sequence of Taz1p contains a close match to the consensus modification site for SUMO-1, and a PEST sequence similar to those found in established SUMO-1 targets. Although previous experiments have identified an increase in telomere length as one consequence of the pmt3– genotype, we could not detect Pmt3p modification of Taz1p in protein extracts made from exponentially growing haploid cells or any effect of Pmt3p on the localization of GFP-Taz1p at discrete foci in the haploid cell nucleus. |
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Keywords: | Schizosaccharomyces pombe telomere taz1 pmt3 SUMO-1 |
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