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- W3129312126 abstract "Telomerase is a ribonucleoprotein complex that counteracts the shortening of chromosome ends due to incomplete replication. Telomerase contains a catalytic core of telomerase reverse transcriptase (TERT) and telomerase RNA (TER). However, what defines TERT and separates it from other reverse transcriptases remains a subject of debate. A recent cryoEM map of Tetrahymena telomerase revealed the structure of a previously uncharacterized TERT domain (TRAP) with unanticipated interactions with TEN domain and roles in telomerase activity. Both TEN and TRAP are absent in the putative Tribolium TERT that has been used as a model for telomerase for over a decade. To investigate the conservation of TRAP and TEN across species, we performed multiple sequence alignments and statistical coupling analysis on all identified TERTs and find that TEN and TRAP have co-evolved as telomerase specific domains. Integrating the data from bioinformatic analysis and the structure of Tetrahymena telomerase, we built a new pseudoatomic model of human telomerase catalytic core that accounts for almost all of the cryoEM density in a published map, including TRAP in previously unassigned density as well as telomerase RNA domains essential for activity. This more complete model of human telomerase catalytic core illustrates how domains of TER and TERT, including the TEN-TRAP complex, can interact in a conserved manner to regulate telomere synthesis." @default.
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- W3129312126 date "2021-02-01" @default.
- W3129312126 modified "2023-10-16" @default.
- W3129312126 title "A Structurally Conserved Human and Tetrahymena Telomerase Catalytic Core" @default.
- W3129312126 doi "https://doi.org/10.1016/j.bpj.2020.11.1037" @default.
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