期刊
CURRENT OPINION IN STRUCTURAL BIOLOGY
卷 24, 期 -, 页码 115-124出版社
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2014.01.008
关键词
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资金
- NIH [GM48123]
- NSF [MCB1022379]
- Ruth L Kirschstein NRSA postdoctoral fellowship [GM101874]
- Direct For Biological Sciences [1022379] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience [1022379] Funding Source: National Science Foundation
Telomerase is the ribonucleoprotein (RNP) reverse transcriptase responsible for synthesizing the 3' ends of linear chromosomes. It plays critical roles in tumorigenesis, cellular aging, and stem cell renewal. The past two years have seen exciting progress in determining telomerase holoenzyme architecture and the structural basis of telomerase activity. Notably, the first electron microscopy structures of telomerase were reported, of the Tetrahymena thermophila telomerase holoenzyme and a human telomerase dimer. In addition to new structures of TERT and TER domains, the first structures of telomerase protein domains beyond TERT, and their complexes with TER or telomeric single-stranded DNA, were reported. Together these studies provide the first glimpse into the organization of the proteins and RNA in the telomerase RNP.
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