2b2a
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/TERT_TETTS TERT_TETTS] Catalytic component of telomerase, an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER (PubMed:10944124, PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:16462747). TERT is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme (PubMed:10944124, PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:16462747).<ref>PMID:10944124</ref> <ref>PMID:15696174</ref> <ref>PMID:16462747</ref> <ref>PMID:17322903</ref> <ref>PMID:20713447</ref> | [https://www.uniprot.org/uniprot/TERT_TETTS TERT_TETTS] Catalytic component of telomerase, an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER (PubMed:10944124, PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:16462747). TERT is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme (PubMed:10944124, PubMed:15696174, PubMed:17322903, PubMed:20713447, PubMed:16462747).<ref>PMID:10944124</ref> <ref>PMID:15696174</ref> <ref>PMID:16462747</ref> <ref>PMID:17322903</ref> <ref>PMID:20713447</ref> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | Telomerase, a ribonucleoprotein enzyme, adds telomeric DNA repeats to the ends of linear chromosomes. Here we report the first high-resolution structure of any portion of the telomerase reverse transcriptase, the telomerase essential N-terminal (TEN) domain from Tetrahymena thermophila. The structure, which seems to represent a novel protein fold, shows phylogenetically conserved amino acid residues in a groove on its surface. These residues are crucial for telomerase catalytic activity, and several of them are required for sequence-specific binding of a single-stranded telomeric DNA primer. The positively charged C terminus, which becomes ordered upon interaction with other macromolecules, is involved in binding RNA in a non-sequence-specific manner. The TEN domain's ability to bind both RNA and telomeric DNA, coupled with the notably strong effects on activity upon mutagenesis of single surface residues, suggest how this domain contributes to telomerase catalysis. | ||
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| - | Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase.,Jacobs SA, Podell ER, Cech TR Nat Struct Mol Biol. 2006 Mar;13(3):218-25. Epub 2006 Feb 5. PMID:16462747<ref>PMID:16462747</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2b2a" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
Crystal Structure of the TEN domain of the Telomerase Reverse Transcriptase
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