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Cancer Lett. 2003 May 15;194(2):139-54.

Biochemical aspects of telomerase function.

Author information

1
Department of Medical Biophysics, Ontario Cancer Institute, University of Toronto, 620 University Avenue, Rm. 932, Ontario M5G 2C1, Toronto, Canada. leah@uhnres.utoronto.ca <leah@uhnres.utoronto.ca>

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.

PMID:
12757972
DOI:
10.1016/s0304-3835(02)00701-2
[Indexed for MEDLINE]

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