Single-molecule analysis of telomerase structure and function.
Author: Hengesbach M, Akiyama BM, Stone MD.
Affiliation:
Department of Chemistry and Biochemistry, University of California, Santa Cruz, 1156 High St., Santa Cruz, CA 95064, United States.
Conference/Journal: Curr Opin Chem Biol.
Date published: 2011 Nov 4
Other:
Word Count: 118
The telomerase ribonucleoprotein is a specialized reverse transcriptase required to maintain protective chromosome end-capping structures called telomeres. In most cells, telomerase is not active and the natural shortening of telomeres with each round of DNA replication ultimately triggers cell growth arrest. In contrast, the presence of telomerase confers a high level of renewal capacity upon rapidly dividing cells. Telomerase is aberrantly activated in 90% of human cancers and thus represents an important target for anticancer therapeutics. However, the naturally low abundance of telomerase has hampered efforts to obtain high-resolution models for telomerase structure and function. To circumvent these challenges, single-molecule techniques have recently been employed to investigate telomerase assembly, structure, and catalysis.
Copyright © 2011 Elsevier Ltd. All rights reserved.
PMID: 22057212
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