期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 15, 期 6, 页码 634-640出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1420
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资金
- Howard Hughes Medical Institute Funding Source: Medline
- NIGMS NIH HHS [R01 GM028039-20, R01 GM028039-22, R01 GM028039-23, R01 GM028039-28, R01 GM028039, R01 GM028039-27, R01 GM028039-26, R01 GM028039-25, R01 GM28039, R01 GM028039-24, R01 GM028039-21] Funding Source: Medline
Telomerase is responsible for replication of the ends of linear chromosomes in most eukaryotes. Its intrinsic RNA subunit provides the template for synthesis of telomeric DNA by the reverse-transcriptase (TERT) subunit and tethers other proteins into the ribonucleoprotein (RNP) complex. We report that a phylogenetically conserved triple helix within a pseudoknot structure of this RNA contributes to telomerase activity but not by binding the TERT protein. Instead, 2'-OH groups protruding from the triple helix participate in both yeast and human telomerase catalysis; they may orient the primer-template relative to the active site in a manner analogous to group I ribozymes. The role of RNA in telomerase catalysis may have been acquired relatively recently or, alternatively, telomerase may be a molecular fossil representing an evolutionary link between RNA enzymes and RNP enzymes.
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