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Originally published In Press as doi:10.1074/jbc.M201976200 on July 31, 2002

J. Biol. Chem., Vol. 277, Issue 39, 36174-36180, September 27, 2002
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Functional Analysis of the C-terminal Extension of Telomerase Reverse Transcriptase
A PUTATIVE "THUMB" DOMAIN*

Shabbir Hossain, Sunitha Singh, and Neal F. LueDagger

From the Department of Microbiology and Immunology, William Randolph Hearst Microbiology Research Center, Weill Medical College of Cornell University, New York, New York 10021

Telomerase is an RNA-protein complex responsible for the extension of one strand of telomere terminal repeats. The catalytic protein subunit of telomerase, known generically as telomerase reverse transcriptase (TERT), exhibits significant homology to reverse transcriptases (RTs) encoded by retroviruses and retroelements. The mechanisms of telomerase may therefore be similar to those of the conventional reverse transcriptases. In this report, we explore potential similarity between these two classes of proteins in a region with no evident sequence similarity. Previous analysis has implicated a C-terminal domain of retroviral RTs (known as the "thumb" domain) in template-primer binding and in processivity control. The equivalent region of TERTs, although similar to one another, does not exhibit significant sequence homology to retroviral RTs. However, we found that removal of this region of yeast TERT similarly resulted in a decrease in the stability of telomerase-DNA complex and in the processivity of telomerase-mediated nucleotide addition. Moreover, the C-terminal domain of TERT exhibits a nucleic acid binding activity when recombinantly expressed and purified. Finally, amino acid substitutions of conserved residues in this region of TERT were found to impair telomerase activity and processivity. We suggest that mechanistic similarity between telomerase and retroviral RTs may extend beyond the regions with apparent sequence similarity.

* This work was supported by an American Cancer Society research project grant, the Tartikoff/Perelman/EIF Fund from the Academic Medicine Development Company, and an RO1 grant from the National Institutes of Health. The Department of Microbiology and Immunology was supported by the William Randolph Hearst Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 212-746-6506; Fax: 212-746-8587; E-mail: nflue@mail.med.cornell.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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