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• W2134568462 abstract "Telomerase is a ribonucleoprotein reverse transcriptase responsible for extending one strand of the telomere terminal repeats. Unique among reverse transcriptases, telomerase is thought to possess a DNA-binding domain (known as anchor site) that allows the enzyme to add telomere repeats processively. Previous crosslinking and mutagenesis studies have mapped the anchor site to an N-terminal region of TERT, and the structure of this region of Tetrahymena TERT was recently determined at atomic resolutions. Here we use a combination of homology modeling, electrostatic calculation and site-specific mutagenesis analysis to identify a positively charged, functionally important surface patch on yeast TERT. This patch is lined by both conserved and non-conserved residues, which when mutated, caused loss of telomerase processivity in vitro and telomere shortening in vivo. In addition, we demonstrate that a point mutation in this domain of yeast TERT simultaneously enhanced the repeat addition processivity of telomerase and caused telomere elongation. Our data argue that telomerase anchor site has evolved species-specific residues to interact with species-specific telomere repeats. The data also reinforce the importance of telomerase processivity in regulating telomere length." @default.
• W2134568462 created "2016-06-24" @default.
• W2134568462 creator A5036291399 @default.
• W2134568462 creator A5065552028 @default.
• W2134568462 date "2007-08-01" @default.
• W2134568462 modified "2023-09-26" @default.
• W2134568462 title "Modeling and structure function analysis of the putative anchor site of yeast telomerase" @default.
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• W2134568462 doi "https://doi.org/10.1093/nar/gkm531" @default.
• W2134568462 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1976438" @default.
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• W2134568462 hasPublicationYear "2007" @default.
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