A universal telomerase RNA core structure includes structured motifs required for binding the telomerase reverse transcriptase protein
- Jue Lin*,
- Hinh Ly†,‡,
- Arif Hussain†,
- Mira Abraham§,
- Sivan Pearl§,
- Yehuda Tzfati§,
- Tristram G. Parslow†,‡, and
- Elizabeth H. Blackburn*,¶
- Departments of *Biochemistry and Biophysics and †Pathology, University of California, San Francisco, CA 94143; and §Department of Genetics, Institute of Life Sciences, Hebrew University of Jerusalem, Jerusalem 91904, Israel
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Contributed by Elizabeth H. Blackburn, August 10, 2004
Abstract
Telomerase synthesizes telomeric DNA by copying a short template sequence within its telomerase RNA component. We delineated nucleotides and base-pairings within a previously mapped central domain of the Saccharomyces cerevisiae telomerase RNA (TLC1) that are important for telomerase function and for binding to the telomerase catalytic protein Est2p. Phylogenetic comparison of telomerase RNA sequences from several budding yeasts revealed a core structure common to Saccharomyces and Kluyveromyces yeast species. We show that in this structure three conserved sequences interact to provide a binding site for Est2p positioned near the template. These results, combined with previous studies on telomerase RNAs from other budding yeasts, vertebrates, and ciliates, define a minimal universal core for telomerase RNAs.
Footnotes
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↵ ¶ To whom correspondence should be addressed at: Department of Biochemistry and Biophysics, University of California, 600 16th Street, Box 2200, San Francisco, CA 94143-2200. E-mail: telomer{at}itsa.ucsf.edu.
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↵ ‡ Present address: Department of Pathology and Laboratory Medicine, Emory University, Atlanta, GA 30322.
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Abbreviations: TER, telomerase; TERT, TER reverse transcriptase.
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Data deposition: The sequences reported in this paper have been deposited in the GenBank database [accession nos. Ay737251 (the telomerase RNA gene of Saccharomyces cariocanus) and AY737252 (the telomerase RNA gene of Saccharomyces kudriavzevii)].
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See Commentary on page 14683.
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Freely available online through the PNAS open access option.
- Copyright © 2004, The National Academy of Sciences
