ArticleNucleic acids research2002
Delineation of the high-affinity single-stranded telomeric DNA-binding domain of Saccharomyces cerevisiae Cdc13.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Cdc13 exhibits dynamic DNA strand exchange in the presence of telomeric DNA.Nucleic acids research · 2024Article
- A comprehensive map of hotspots of de novo telomere addition in Saccharomyces cerevisiae.Genetics · 2023Article
- A comprehensive map of hotspots of de novo telomere addition inbioRxiv : the preprint server for biology · 2023Article
- Regulation of Antigenic Variation byPathogens (Basel, Switzerland) · 2021Review
- Role of folding kinetics of secondary structures in telomeric G-overhangs in the regulation of telomere maintenance inThe Journal of biological chemistry · 2020Article
- Human CST Prefers G-Rich but Not Necessarily Telomeric Sequences.Biochemistry · 2017Article
- Tying up the Ends: Plasticity in the Recognition of Single-Stranded DNA at Telomeres.Biochemistry · 2016Article
- Modulation of yeast telomerase activity by Cdc13 and Est1 in vitro.Scientific reports · 2016Article
- Endogenous Hot Spots of De Novo Telomere Addition in the Yeast Genome Contain Proximal Enhancers That Bind Cdc13.Molecular and cellular biology · 2016Article
- The Telomere Binding Protein Cdc13 and the Single-Stranded DNA Binding Protein RPA Protect Telomeric DNA from Resection by Exonucleases.Journal of molecular biology · 2015Article
- The telomeric protein Pot1 from Schizosaccharomyces pombe binds ssDNA in two modes with differing 3' end availability.Nucleic acids research · 2014Article
- The tenacious recognition of yeast telomere sequence by Cdc13 is fully exerted by a single OB-fold domain.Nucleic acids research · 2014Article
- Single-stranded DNA-binding proteins: multiple domains for multiple functions.Structure (London, England : 1993) · 2013Review
- Human single-stranded DNA binding proteins are essential for maintaining genomic stability.BMC molecular biology · 2013Review
- A yeast telomerase complex containing the Est1 recruitment protein is assembled early in the cell cycle.Biochemistry · 2013Article
- Finding the end: recruitment of telomerase to telomeres.Nature reviews. Molecular cell biology · 2013Review
- Novel phosphorylation sites in the S. cerevisiae Cdc13 protein reveal new targets for telomere length regulation.Journal of proteome research · 2013Article
- Practical strategies for the evaluation of high-affinity protein/nucleic acid interactions.Journal of nucleic acids investigation · 2013Article
- Telomerase and telomere-associated proteins: structural insights into mechanism and evolution.Structure (London, England : 1993) · 2012Review
- The telomeric Cdc13 protein interacts directly with the telomerase subunit Est1 to bring it to telomeric DNA ends in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
Corrections and comments
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3 authors.
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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.
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