Journal
SCIENCE
Volume 350, Issue 6260, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aab4070
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Funding
- NIH [GM048123, GM071940, GM103479, R01GM054198, P41 RR015301, P41 GM103403]
- NSF [MCB1022379]
- American Heart Association [14POST18870059]
- NIH Ruth L. Kirschstein National Research Service Award (NRSA) [GM101874]
- NIH Ruth L. Kirschstein NRSA predoctoral training grant fellowship [GM007185]
- NSF Graduate Research Fellowship [DGE-1106400]
- DOE [DE-FC0302ER63421, DE-AC02-06CH11357]
- Electron Imaging Center for NanoMachines by NIH [S10RR23057, S10OD018111, NSF DBI-133813]
- National Center for Advancing Translational Sciences UCLA Clinical and Translational Science Institute [UL1TR000124]
- Direct For Biological Sciences [1338135, 1517625] Funding Source: National Science Foundation
- Div Of Biological Infrastructure [1338135] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience [1517625] Funding Source: National Science Foundation
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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 similar to 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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