Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions
In: Science, Jg. 350 (2015-10-30), Heft 6260
Online
academicJournal
- aab4070
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.
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Structure of Tetrahymena telomerase reveals previously unknown subunits, functions, and interactions
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Autor/in / Beteiligte Person: | Jiang, Jiansen ; Chan, Henry ; Cash, Darian D ; Miracco, Edward J ; Ogorzalek Loo, Rachel R ; Upton, Heather E ; Cascio, Duilio ; O'Brien Johnson, Reid ; Collins, Kathleen ; Loo, Joseph A ; Zhou, Z Hong ; Feigon, Juli |
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Zeitschrift: | Science, Jg. 350 (2015-10-30), Heft 6260 |
Veröffentlichung: | eScholarship, University of California, 2015 |
Medientyp: | academicJournal |
Umfang: | aab4070 |
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