National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM048123
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM071940
United States
National Science Foundation (NSF, United States)
MCB1517625
United States
National Institutes of Health/Office of the Director
1S10OD018111
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM007185
United States
National Science Foundation (NSF, United States)
DBI-1338135
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
1U24GM116792
United States
American Heart Association
14POST18870059
United States
National Science Foundation (NSF, United States)
DMR-1548924
United States
Citation
Journal: Cell / Year: 2018 Title: Structure of Telomerase with Telomeric DNA. Authors: Jiansen Jiang / Yaqiang Wang / Lukas Sušac / Henry Chan / Ritwika Basu / Z Hong Zhou / Juli Feigon / Abstract: Telomerase is an RNA-protein complex (RNP) that extends telomeric DNA at the 3' ends of chromosomes using its telomerase reverse transcriptase (TERT) and integral template-containing telomerase RNA ...Telomerase is an RNA-protein complex (RNP) that extends telomeric DNA at the 3' ends of chromosomes using its telomerase reverse transcriptase (TERT) and integral template-containing telomerase RNA (TER). Its activity is a critical determinant of human health, affecting aging, cancer, and stem cell renewal. Lack of atomic models of telomerase, particularly one with DNA bound, has limited our mechanistic understanding of telomeric DNA repeat synthesis. We report the 4.8 Å resolution cryoelectron microscopy structure of active Tetrahymena telomerase bound to telomeric DNA. The catalytic core is an intricately interlocked structure of TERT and TER, including a previously structurally uncharacterized TERT domain that interacts with the TEN domain to physically enclose TER and regulate activity. This complete structure of a telomerase catalytic core and its interactions with telomeric DNA from the template to telomere-interacting p50-TEB complex provides unanticipated insights into telomerase assembly and catalytic cycle and a new paradigm for a reverse transcriptase RNP.
History
Deposition
Apr 22, 2018
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Header (metadata) release
May 23, 2018
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Map release
May 30, 2018
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Update
Dec 25, 2019
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Current status
Dec 25, 2019
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average exposure time: 12.0 sec. / Average electron dose: 52.0 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron optics
Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
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