Progress in structural studies of telomerase

被引：17

作者：

Miracco, Edward J. ^{[1
]}

Jiang, Jiansen ^{[1
,2
,3
]}

Cash, Darian D. ^{[1
]}

Feigon, Juli ^{[1
,3
]}

机构：

[1] Univ Calif Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90095 USA

[2] Univ Calif Los Angeles, Dept Microbiol Immunol & Mol Genet, Los Angeles, CA 90095 USA

[3] Univ Calif Los Angeles, Calif Nanosyst Inst, Los Angeles, CA 90095 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2014年 / 24卷

基金：

美国国家科学基金会;

关键词：

CATALYTIC SUBUNIT TERT; RNA-BINDING DOMAIN; TETRAHYMENA TELOMERASE; REVERSE-TRANSCRIPTASE; TRIPLE-HELIX; PROTEIN P65; CRYSTAL-STRUCTURE; TERMINAL DOMAIN; H/ACA RNPS; HOLOENZYME;

D O I：

10.1016/j.sbi.2014.01.008

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：115 / 124

页数：10

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