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Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions.


ABSTRACT: Telomerase helps maintain telomeres by processive synthesis of telomere repeat DNA at their 3'-ends, using an integral telomerase RNA (TER) and telomerase reverse transcriptase (TERT). We report the cryo-electron microscopy structure of Tetrahymena telomerase at ~9 angstrom resolution. In addition to seven known holoenzyme proteins, we identify two additional proteins that form a complex (TEB) with single-stranded telomere DNA-binding protein Teb1, paralogous to heterotrimeric replication protein A (RPA). The p75-p45-p19 subcomplex is identified as another RPA-related complex, CST (CTC1-STN1-TEN1). This study reveals the paths of TER in the TERT-TER-p65 catalytic core and single-stranded DNA exit; extensive subunit interactions of the TERT essential N-terminal domain, p50, and TEB; and other subunit identities and structures, including p19 and p45C crystal structures. Our findings provide structural and mechanistic insights into telomerase holoenzyme function.

SUBMITTER: Jiang J 

PROVIDER: S-EPMC4687456 | biostudies-literature | 2015 Oct

REPOSITORIES: biostudies-literature

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Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions.

Jiang Jiansen J   Chan Henry H   Cash Darian D DD   Miracco Edward J EJ   Ogorzalek Loo Rachel R RR   Upton Heather E HE   Cascio Duilio D   O'Brien Johnson Reid R   Collins Kathleen K   Loo Joseph A JA   Zhou Z Hong ZH   Feigon Juli J  

Science (New York, N.Y.) 20151015 6260


Telomerase helps maintain telomeres by processive synthesis of telomere repeat DNA at their 3'-ends, using an integral telomerase RNA (TER) and telomerase reverse transcriptase (TERT). We report the cryo-electron microscopy structure of Tetrahymena telomerase at ~9 angstrom resolution. In addition to seven known holoenzyme proteins, we identify two additional proteins that form a complex (TEB) with single-stranded telomere DNA-binding protein Teb1, paralogous to heterotrimeric replication protei  ...[more]

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