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Molecular and Cellular Biology, April 2007, p. 3226-3240, Vol. 27, No. 8
0270-7306/07/$08.00+0     doi:10.1128/MCB.02368-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Characterization of Physical and Functional Anchor Site Interactions in Human Telomerase{triangledown}

Haley D. M. Wyatt, Deirdre A. Lobb, and Tara L. Beattie*

Southern Alberta Cancer Research Institute and Department of Biochemistry and Molecular Biology, University of Calgary, 3330 Hospital Drive NW, Calgary, Alberta, Canada, T2N 4N1

Received 19 December 2006/ Returned for modification 25 January 2007/ Accepted 5 February 2007

Telomerase is a ribonucleoprotein reverse transcriptase (RT) that processively synthesizes telomeric repeats onto the ends of linear chromosomes to maintain genomic stability. It has been proposed that the N terminus of the telomerase protein subunit, telomerase RT (TERT), contains an anchor site that forms stable interactions with DNA to prevent enzyme-DNA dissociation during translocation and to promote realignment events that accompany each round of telomere synthesis. However, it is not known whether human TERT (hTERT) can directly interact with DNA in the absence of the telomerase RNA subunit. Here we use a novel primer binding assay to establish that hTERT forms stable and specific contacts with telomeric DNA in the absence of the human telomerase RNA component (hTR). We show that hTERT-mediated primer binding can be functionally uncoupled from telomerase-mediated primer extension. Our results demonstrate that the first 350 amino acids of hTERT have a critical role in regulating the strength and specificity of protein-DNA interactions, providing additional evidence that the TERT N terminus contains an anchor site. Furthermore, we establish that the RT domain of hTERT mediates important protein-DNA interactions. Collectively, these data suggest that hTERT contains distinct anchor regions that cooperate to help regulate telomerase-mediated DNA recognition and elongation.

* Corresponding author. Mailing address: Southern Alberta Cancer Research Institute, Department of Biochemistry and Molecular Biology, Room 372B HMRB, 2220 Hospital Drive NW, Calgary, AB, Canada T2N 4N1. Phone: (403) 220-8328. Fax: (403) 283-8727. E-mail: tbeattie{at}ucalgary.ca

{triangledown} Published ahead of print on 12 February 2007.

Molecular and Cellular Biology, April 2007, p. 3226-3240, Vol. 27, No. 8
0270-7306/07/$08.00+0     doi:10.1128/MCB.02368-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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  • Finger, S. N., Bryan, T. M. (2008). Multiple DNA-binding sites in Tetrahymena telomerase. Nucleic Acids Res 36: 1260-1272 [Abstract] [Full Text]  


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