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• W2017875807 startingPage "4305" @default.
• W2017875807 abstract "Cdc13 is an essential protein from Saccharomyces cerevisiae that caps telomeres by protecting the C‐rich telomeric DNA strand from degradation and facilitates telomeric DNA replication by telomerase. In vitro , Cdc13 binds TG‐rich single‐stranded telomeric DNA with high affinity and specificity. A previously identified domain of Cdc13 encompassing amino acids 451–694 (the 451–694 DBD) retains the single‐stranded DNA‐binding properties of the full‐length protein; however, this domain contains a large unfolded region identified in heteronuclear NMR experiments. Trypsin digestion and MALDI mass spectrometry were used to identify the minimal DNA‐binding domain (the 497–694 DBD) necessary and sufficient for full DNA‐binding activity. This domain was completely folded, and the N‐terminal unfolded region removed was shown to be dispensable for function. Using affinity photocrosslinking to site‐specifically modified telomeric single‐stranded DNA, the 497–694 DBD was shown to contact the entire 11mer required for high‐affinity binding. Intriguingly, both domains bound single‐stranded telomeric DNA with much greater affinity than the full‐length protein. The full‐length protein exhibited the same rate of dissociation as both domains, however, indicating that the full‐length protein contains a region that inhibits association with single‐stranded telomeric DNA." @default.
• W2017875807 created "2016-06-24" @default.
• W2017875807 creator A5031343617 @default.
• W2017875807 creator A5051284682 @default.
• W2017875807 creator A5068974077 @default.
• W2017875807 date "2002-10-01" @default.
• W2017875807 modified "2023-09-23" @default.
• W2017875807 title "Delineation of the high-affinity single-stranded telomeric DNA-binding domain of Saccharomyces cerevisiae Cdc13" @default.
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• W2017875807 doi "https://doi.org/10.1093/nar/gkf554" @default.
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