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• W4295934140 endingPage "1788" @default.
• W4295934140 startingPage "1777" @default.
• W4295934140 abstract "Saccharomyces telomeres consist of ∼350 bp of C 1-3 A/TG 1-3 DNA. Most of this ∼350 bp is replicated by standard, semiconservative DNA replication. After conventional replication, the C 1-3 A strand is degraded to generate a long single strand TG 1-3 tail that can serve as a substrate for telomerase. Cdc13p is a single strand TG 1-3 DNA-binding protein that localizes to telomeres in vivo. Genetic data suggest that the Cdc13p has multiple roles in telomere replication. We used two hybrid analysis to demonstrate that Cdc13p interacted with both the catalytic subunit of DNA polymerase α, Pol1p, and the telomerase RNA-associated protein, Est1p. The association of these proteins was confirmed by biochemical analysis using full-length or nearly full-length proteins. Point mutations in either CDC13 or POL1 that reduced the Cdc13p–Pol1p interaction resulted in telomerase mediated telomere lengthening. Over–expression of the carboxyl terminus of Est1p partially suppressed the temperature sensitive lethality of a cdc13-1 strain. We propose that Cdc13p's interaction with Est1p promotes TG 1-3 strand lengthening by telomerase and its interaction with Pol1p promotes C 1-3 A strand resynthesis by DNA polymerase α." @default.
• W4295934140 created "2022-09-16" @default.
• W4295934140 creator A5006524357 @default.
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• W4295934140 date "2000-07-15" @default.
• W4295934140 modified "2023-10-16" @default.
• W4295934140 title "The <i>Saccharomyces</i> telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase α and the telomerase-associated Est1 protein" @default.
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• W4295934140 doi "https://doi.org/10.1101/gad.14.14.1777" @default.
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