Journal
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY
Volume 11, Issue 12, Pages -Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1101/cshperspect.a032383
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Funding
- National Institutes of Health (NIH) [GM048123]
- National Science Foundation (NSF) [MCB1517625]
- Department of Energy (DOE) [DE-FC0202ER63421]
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Telomerase is a DNA polymerase that extends the 3' ends of chromosomes by processively synthesizing multiple telomeric repeats. It is a unique ribonucleoprotein (RNP) containing a specialized telomerase reverse transcriptase (TERT) and telomerase RNA (TER) with its own template and other elements required with TERT for activity (catalytic core), as well as species-specific TER-binding proteins important for biogenesis and assembly (core RNP); other proteins bind telomerase transiently or constitutively to allow association of telomerase and other proteins with telomere ends for regulation of DNA synthesis. Here we describe how nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography of TER and protein domains helped define the structure and function of the core RNP, laying the groundwork for interpreting negative-stain and cryo electron microscopy (cryo-EM) density maps of Tetrahymena thermophila and human telomerase holoenzymes. As the resolution has improved from similar to 30 angstrom to similar to 5 angstrom, these studies have provided increasingly detailed information on telomerase architecture and mechanism.
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