title: Mutation in TERT separates processivity from anchor-site function.
abstract: 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.
authors.affiliation: Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80309-0215, USA. Arthur.Zaug@Colorado.edu
authors.forename: Arthur J
authors.initials: AJ
authors.lastname: Zaug
authors.forename: Elaine R
authors.initials: ER
authors.lastname: Podell
authors.forename: Thomas R
authors.initials: TR
authors.lastname: Cech
mesh_terms: D000818:Animals; D001665:Binding Sites; D020134:Catalytic Domain; D004247:DNA / Q000737:chemistry; D017931:DNA Primers / Q000737:chemistry; D006801:Humans; D007700:Kinetics; D007930:Leucine / Q000737:chemistry; D009154:Mutation; D017434:Protein Structure, Tertiary; D019098:Telomerase / Q000737:chemistry* / Q000378:metabolism; D013696:Temperature; D016808:Tetrahymena thermophila / Q000201:enzymology*
chemical_list: D017931:DNA Primers; D004247:DNA; C509186:TERT protein, human; D019098:Telomerase; D007930:Leucine