The Telomere Terminal Transferase of Tetrahymena Is a Ribonucleoprotein Enzyme with Two Kinds of Primer Specificity

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dc.contributor.authorBlackburn, Elizabeth H.
dc.contributor.authorGreider, Carol W.
dc.date.accessioned2009-11-30T19:08:15Z
dc.date.available2009-11-30T19:08:15Z
dc.date.issued1987-12-24
dc.description.abstractWe have analyzed the de novo telomere synthesis catalyzed by the enzyme telomere terminal transferase (telomerase) from Tetrahymena. Oligonucleotides representing the G-rich strand of telomeric sequences from five different organisms specifically primed the addition of TTGGGG repeats in vitro, suggesting that primer recognition may involve a DNA structure unique to these oligonucleotides. The sequence at the 3' end of the oligonucleotide primer specified the first nucleotide added in the reaction. Furthermore, the telomerase was shown to be a ribonucleoprotein complex whose RNA and protein components were both essential for activity. After extensive purification of the enzyme by a series of five different chromatographic steps, a few small low abundance RNAs copurified with the activity.en_US
dc.identifier.citationReprinted from Cell 51, Greider, Carol W. and Elizabeth H. Blackburn, "The Telomere Terminal Transferase of Tetrahymena Is a Ribonucleoprotein Enzyme with Two Kinds of Primer Specificity", pg. 887-898, copyright 1987 with permission from Elsevier. Original version available at http://www.cell.comen_US
dc.identifier.urihttp://jhir.library.jhu.edu/handle/1774.2/33682
dc.language.isoen_USen_US
dc.publisherCell Pressen_US
dc.subjectTetrahymena/enzymologyen_US
dc.subjectRibonucleoproteins/metabolismen_US
dc.subjectReptetitive Sequencesen_US
dc.subjectNucleic Aciden_US
dc.subjectOligodeoxyribonucleotides/metabolismen_US
dc.subjectDNA Nucleotidyltransferases/metabolismen_US
dc.subjectDNA Nucleotidylexotransferase/metabolismen_US
dc.subjectDNA/metabolismen_US
dc.titleThe Telomere Terminal Transferase of Tetrahymena Is a Ribonucleoprotein Enzyme with Two Kinds of Primer Specificityen_US
dc.typeArticleen_US
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