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Triple-helix structure in telomerase RNA contributes to catalysis
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 th...
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Formato: | Texto |
Lenguaje: | English |
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2008
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2562722/ https://www.ncbi.nlm.nih.gov/pubmed/18500353 http://dx.doi.org/10.1038/nsmb.1420 |
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author | Qiao, Feng Cech, Thomas R |
author_facet | Qiao, Feng Cech, Thomas R |
author_sort | Qiao, Feng |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-2562722 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
record_format | MEDLINE/PubMed |
spelling | pubmed-25627222008-12-01 Triple-helix structure in telomerase RNA contributes to catalysis Qiao, Feng Cech, Thomas R Nat Struct Mol Biol Article 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. 2008-05-25 2008-06 /pmc/articles/PMC2562722/ /pubmed/18500353 http://dx.doi.org/10.1038/nsmb.1420 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms |
spellingShingle | Article Qiao, Feng Cech, Thomas R Triple-helix structure in telomerase RNA contributes to catalysis |
title | Triple-helix structure in telomerase RNA contributes to catalysis |
title_full | Triple-helix structure in telomerase RNA contributes to catalysis |
title_fullStr | Triple-helix structure in telomerase RNA contributes to catalysis |
title_full_unstemmed | Triple-helix structure in telomerase RNA contributes to catalysis |
title_short | Triple-helix structure in telomerase RNA contributes to catalysis |
title_sort | triple-helix structure in telomerase rna contributes to catalysis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2562722/ https://www.ncbi.nlm.nih.gov/pubmed/18500353 http://dx.doi.org/10.1038/nsmb.1420 |
work_keys_str_mv | AT qiaofeng triplehelixstructureintelomerasernacontributestocatalysis AT cechthomasr triplehelixstructureintelomerasernacontributestocatalysis |