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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.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
dc.identifier.urihttp://jhir.library.jhu.edu/handle/1774.2/33682
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
dc.language.isoen_USen
dc.publisherCell Pressen
dc.subjectTetrahymena/enzymologyen
dc.subjectRibonucleoproteins/metabolismen
dc.subjectReptetitive Sequences, Nucleic Aciden
dc.subjectOligodeoxyribonucleotides/metabolismen
dc.subjectDNA Nucleotidyltransferases/metabolismen
dc.subjectDNA Nucleotidylexotransferase/metabolismen
dc.subjectDNA/metabolismen
dc.titleThe Telomere Terminal Transferase of Tetrahymena Is a Ribonucleoprotein Enzyme with Two Kinds of Primer Specificityen
dc.typeArticleen


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