Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1993-10-26
pubmed:abstractText
The ribonucleoprotein enzyme telomerase synthesizes one strand of telomeric DNA by copying a template sequence within the RNA moiety of the enzyme. Kinetic studies of this polymerization reaction were used to analyze the mechanism and properties of the telomerase from Tetrahymena thermophila. This enzyme synthesizes TTGGGG repeats, the telomeric DNA sequence of this species, by elongating a DNA primer whose 3' end base pairs with the template-forming domain of the RNA. The enzyme was found to act nonprocessively with short (10- to 12-nucleotide) primers but to become processive as TTGGGG repeats were added. Variation of the 5' sequences of short primers with a common 3' end identified sequence-specific effects which are distinct from those involving base pairing of the 3' end of the primer with the RNA template and which can markedly induce enzyme activity by increasing the catalytic rate of the telomerase polymerization reaction. These results identify an additional mechanistic basis for telomere and DNA end recognition by telomerase in vivo.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-1497307, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-1689074, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-1689810, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-1700787, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-1708110, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-1875940, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-1896088, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-1896089, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-1934071, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-2023635, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-2271646, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-2463488, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-2474761, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-2500641, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-2694944, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-2698831, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-2927395, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-3319189, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-3907856, http://linkedlifedata.com/resource/pubmed/commentcorrection/8413255-6383193
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0270-7306
pubmed:author
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6586-99
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Sequence-specific DNA primer effects on telomerase polymerization activity.
pubmed:affiliation
Department of Microbiology and Immunology, University of California, San Francisco 94143-0414.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't