Mutation in TERT separates processivity from anchor-site function

Telomerase shows repeat-addition processivity (RAP): synthesis of multiple telomeric DNA repeats without primer dissociation. Leu14 mutants in the telomerase essential N-terminal domain of Tetrahymena thermophila telomerase reverse transcriptase retain full activity and anchor-site function but lose...

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Published inNature structural & molecular biology Vol. 15; no. 8; pp. 870 - 872
Main Authors Zaug, Arthur J, Podell, Elaine R, Cech, Thomas R
Format Journal Article
LanguageEnglish
Published New York Nature Publishing Group US 01.08.2008
Nature Publishing Group
Subjects
Animals
Binding Sites
Biochemistry
Biological Microscopy
Biomedical and Life Sciences
brief-communication
Catalytic Domain
Deoxyribonucleic acid
DNA
DNA - chemistry
DNA Primers - chemistry
Enzymes
Genetic aspects
Humans
Influence
Kinetics
Leucine - chemistry
Life Sciences
Membrane Biology
Molecular biology
Mutation
Mutation (Biology)
Physiological aspects
Protein Structure
Protein Structure, Tertiary
Proteins
Reverse transcriptase
Telomerase
Telomerase - chemistry
Telomerase - metabolism
Temperature
Tetrahymena thermophila
Tetrahymena thermophila - enzymology
Translocation
Translocation (Genetics)
United States
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Summary:Telomerase shows repeat-addition processivity (RAP): synthesis of multiple telomeric DNA repeats without primer dissociation. Leu14 mutants in the telomerase essential N-terminal domain of Tetrahymena thermophila telomerase reverse transcriptase retain full activity and anchor-site function but lose RAP, suggesting models for how this domain facilitates DNA translocation.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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AUTHOR CONTRIBUTIONS A.J.Z. made the initial discovery and designed and carried out experiments; E.R.P. contributed to data analysis and interpretation; T.R.C. contributed to experimental design and models.
ISSN:1545-9993
1545-9985
DOI:10.1038/nsmb.1462