Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2005-6-28
pubmed:abstractText
Telomerase-mediated telomeric DNA synthesis is important for eukaryotic cell immortality. Telomerase adds tracts of short telomeric repeats to DNA substrates using a unique repeat addition form of processivity. It has been proposed that repeat addition processivity is partly regulated by a telomerase reverse transcriptase (TERT)-dependent anchor site; however, anchor site-mediating residues have not been identified in any TERT. We report the characterization of an N-terminal human TERT (hTERT) RNA interaction domain 1 (RID1) mutation that caused telomerase activity defects consistent with disruption of a template-proximal anchor site, including reduced processivity on short telomeric primers and reduced activity on substrates with nontelomeric 5' sequences, but not on primers with nontelomeric G-rich 5' sequences. This mutation was located within a subregion of RID1 previously implicated in biological telomerase functions unrelated to catalytic activity (N-DAT domain). Other N-DAT and C-terminal DAT (C-DAT) mutants and a C-terminally tagged hTERT-HA variant were defective in elongating short telomeric primers, and catalytic phenotypes of DAT variants were partially or completely rescued by increasing concentrations of DNA primers. These observations imply that RID1 and the hTERT C terminus contribute to telomerase's affinity for its substrate, and that RID1 may form part of the human telomerase anchor site.
pubmed:commentsCorrections
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pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1059-1524
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3152-61
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:15857955-Amino Acid Motifs, pubmed-meshheading:15857955-Catalysis, pubmed-meshheading:15857955-Catalytic Domain, pubmed-meshheading:15857955-Cell Line, pubmed-meshheading:15857955-DNA, pubmed-meshheading:15857955-DNA Primers, pubmed-meshheading:15857955-Dose-Response Relationship, Drug, pubmed-meshheading:15857955-Humans, pubmed-meshheading:15857955-Immunoblotting, pubmed-meshheading:15857955-Mutation, pubmed-meshheading:15857955-Phenotype, pubmed-meshheading:15857955-Promoter Regions, Genetic, pubmed-meshheading:15857955-Protein Structure, Tertiary, pubmed-meshheading:15857955-Retroviridae, pubmed-meshheading:15857955-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:15857955-Telomerase, pubmed-meshheading:15857955-Telomere, pubmed-meshheading:15857955-Time Factors
pubmed:year
2005
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