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Molecular and Cellular Biology, May 2003, p. 3237-3246, Vol. 23, No. 9
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.9.3237-3246.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Putative Telomere-Recruiting Domain in the Catalytic Subunit of Human Telomerase

Blaine N. Armbruster,1 Katherine T. Etheridge,1 Dominique Broccoli,2 and Christopher M. Counter1*

Departments of Pharmacology and Cancer Biology, Radiation Oncology, Duke University Medical Center, Durham, North Carolina 27710,1 Fox Chase Cancer Center, Philadelphia, Pennsylvania 191112

Received 24 May 2002/ Returned for modification 5 July 2002/ Accepted 16 January 2003

Telomerase, the enzyme that elongates telomeres, is essential to maintain telomere length and to immortalize most cancer cells. However, little is known about the regulation of this enzyme in higher eukaryotes. We previously described a domain in the hTERT telomerase catalytic subunit that is essential for telomere elongation and cell immortalization in vivo but dispensable for catalytic activity in vitro. Here, we show that fusions of hTERT containing different mutations in this domain to the telomere binding protein hTRF2 redirected the mutated hTERT to telomeres and rescued its in vivo functions. We suggest that this domain posttranscriptionally regulates telomerase function by targeting the enzyme to telomeres.

* Corresponding author. Mailing address: Departments of Pharmacology and Cancer Biology, Radiation Oncology, Duke University Medical Center, Durham, NC 27710. Phone: (919) 684-9890. Fax: (919) 684-8958. E-mail: count004{at}mc.duke.edu.

Molecular and Cellular Biology, May 2003, p. 3237-3246, Vol. 23, No. 9
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.9.3237-3246.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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