Biochemical aspects of telomerase function.
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.
Harrington
Lea
L
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>
D000818:Animals; D002352:Carrier Proteins / Q000235:genetics; D004268:DNA-Binding Proteins; D006801:Humans; D009369:Neoplasms / Q000201:enzymology* / Q000235:genetics; D012334:RNA, Neoplasm; D016601:RNA-Binding Proteins; D019098:Telomerase / Q000235:genetics*; D020394:Vault Ribonucleoprotein Particles / Q000235:genetics
D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D012334:RNA, Neoplasm; D016601:RNA-Binding Proteins; C104342:TEP1 protein, human; D020394:Vault Ribonucleoprotein Particles; D019098:Telomerase