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Nucleic Acids Research 2006 34(3):816-825; doi:10.1093/nar/gkj481
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Published online 1 February 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oxfordjournals.org


Article

Structure of the Tetrahymena thermophila telomerase RNA helix II template boundary element

Rebecca J. Richards1, Carla A. Theimer1, L. David Finger1 and Juli Feigon1,2,*

1Department of Chemistry and Biochemistry, University of California Los Angeles, CA 90095-1569, USA 2Molecular Biology Institute, University of California Los Angeles, CA 90095-1569, USA

*To whom correspondence should be addressed. Tel: +1 310 206 6922; Fax: +1 310 825 0982; Email: feigon{at}mbi.ucla.edu

Received December 12, 2005. Revised January 14, 2006. Accepted January 14, 2006.

Telomere addition by telomerase requires an internal templating sequence located in the RNA subunit of telomerase. The correct boundary definition of this template sequence is essential for the proper addition of the nucleotide repeats. Incorporation of incorrect telomeric repeats onto the ends of chromosomes has been shown to induce chromosomal instability in ciliate, yeast and human cells. A 5' template boundary defining element (TBE) has been identified in human, yeast and ciliate telomerase RNAs. Here, we report the solution structure of the TBE element (helix II) from Tetrahymena thermophila telomerase RNA. Our results indicate that helix II and its capping pentaloop form a well-defined structure including unpaired, stacked adenine nucleotides in the stem and an unusual syn adenine nucleotide in the loop. A comparison of the T.thermophila helix II pentaloop with a pentaloop of the same sequence found in the 23S rRNA of the Haloarcula marismortui ribosome suggests possible RNA and/or protein interactions for the helix II loop within the Tetrahymena telomerase holoenzyme.


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