| Literature DB >> 26918633 |
Juli Feigon1, Henry Chan1, Jiansen Jiang1,2.
Abstract
Telomerase is a ribonucleoprotein complex that helps maintain telomeres, the physical ends of linear chromosomes. The low cellular levels of telomerase, propensity for telomerase reverse transcriptase and other telomerase proteins to aggregate, and cell cycle regulation of telomerase assembly in most organisms has made it a challenging complex for structural biology. Here we review recent progress in determining the structural basis of Tetrahymena telomerase holoenzyme function and interaction at telomeres from solution NMR, X-ray crystallography and electron microscopy studies, including the first cryoelectron microscopy structure of a telomerase holoenzyme (Science, 350, 2015, aab4070).Entities:
Keywords: CST; NMR; OB-fold domain; TPP1; X-ray crystallography; cryoelectron microscopy; p50; replication protein A; telomerase RNA; telomerase reverse transcriptase
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Year: 2016 PMID: 26918633 PMCID: PMC4899323 DOI: 10.1111/febs.13691
Source DB: PubMed Journal: FEBS J ISSN: 1742-464X Impact factor: 5.542