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Volume 194, Issue 2, Pages 139-154 (15 May 2003)


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Biochemical aspects of telomerase function

Lea HarringtonCorresponding Author Informationemail address

Received 15 September 2002; received in revised form 5 November 2002; accepted 8 November 2002.

Abstract 

Arthur Kornberg “never met a dull enzyme” (For the Love of Enzymes: The Odyssey of a Biochemist, Harvard University Press, 1989) and telomerase is no exception. Telomerase is a remarkable polymerase that uses an internal RNA template to reverse-transcribe telomere DNA, one nucleotide at a time, onto telomeric, G-rich single-stranded DNA. In the 17 years since its discovery, the characterization of telomerase enzyme components has uncovered a highly conserved family of telomerase reverse transcriptases that, together with the telomerase RNA, appear to comprise the enzymatic core of telomerase. While not as comprehensively understood as yet, some telomerase-associated proteins also serve crucial roles in telomerase function in vivo, such as telomerase ribonudeoprotein (RNP) assembly, recruitment to the telomere, and the coordination of DNA replication at the telomere. A selected overview of the biochemical properties of this unique enzyme, in vitro and in vivo, will be presented.

Department of Medical Biophysics, Ontario Cancer Institute, University of Toronto, 620 University Avenue, Rm. 932 Toronto, Ontario Canada M5G 2C1

Corresponding Author InformationTel.: +1-416-204-2231; fax: +1-416-204-2277

PII: S0304-3835(02)00701-2

doi:10.1016/S0304-3835(02)00701-2


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