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Papers In Press, published online ahead of print April 17, 2001
J. Biol. Chem, 10.1074/jbc.M101642200
Submitted on February 21, 2001
Revised on April 13, 2001
Accepted on April 17, 2001
Institute of Biopharmaceutical Science, Taipei, Taiwan 112
Corresponding Author: jjlin{at}ym.edu.tw
Cdc13p is a single-strand telomere-binding protein of Saccharomyces cerevisiae; its telomere-binding region is within amino acids 451-693, Cdc13(451-693)p. In this study, we used purified Cdc13p and Cdc13(451-693)p to characterize their telomere-binding activity. We found that the binding specificity of single-stranded TG1-3 DNA by these two proteins are similar. However, the affinity of Cdc13(451-693)p to DNA was slightly lower than that of Cdc13p. The binding of telomeric DNA by these two proteins was disrupted at NaCl concentrations higher than 0.3 N indicating that electrostatic interaction contributed significantly to the binding process. Because both proteins bound to strand TG1-3 DNA positioned at the 3' end, the 5' end, or in the middle of the oligonucleotide substrates, our result indicated that the location of TG1-3 in single-stranded DNA does not appear important for Cdc13p binding. Moreover, using DNase I footprint analysis, the structure of the telomeric DNA complexes of Cdc13p and Cdc13(451-693)p were analyzed. The DNase I footprints of these two proteins to three different telomeric DNA substrates were virtually identical indicating that the telomere contact region of Cdc13p is within Cdc13(451-693)p. Together, the binding properties of Cdc13p and its binding domain support that specific binding of Cdc13p to telomeres is an important feature of telomeres that regulate telomerase access and/or differentiate natural telomeres from broken ends.
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