Prediction of multiple tandem OB-fold domains in telomere end-binding proteins Pot1 and Cdc13

Structure. 2004 Oct;12(10):1877-9. doi: 10.1016/j.str.2004.07.015.


The heterodimeric Oxytricha nova telomere end binding protein, the original telomere end binding protein characterized, contains four OB-fold domains used for recognition of single-stranded telomeric DNA. In contrast, only solitary OB-fold domains have been found in the telomere end binding proteins from yeast and higher eukaryotes. Using a sliding-window algorithm coupled with sequence profile-profile analysis, we provide support for the existence of multiple OB-fold domains in two other telomeric ssDNA binding proteins, vertebrate Pot1 and budding yeast Cdc13. This common usage of multiple, tandem OB-fold domains in telomeric end binding proteins extends the known evolutionary conservation of eukaryotic end-protection mechanisms.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Algorithms
  • Animals
  • Cell Cycle Proteins / chemistry*
  • Computational Biology / methods*
  • Oxytricha / genetics
  • Profilins
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Sequence Analysis, Protein / methods*
  • Telomere-Binding Proteins / chemistry*
  • Telomere-Binding Proteins / genetics


  • CDC3 protein, S cerevisiae
  • Cell Cycle Proteins
  • Profilins
  • Saccharomyces cerevisiae Proteins
  • Telomere-Binding Proteins