Prediction of multiple tandem OB-fold domains in telomere end-binding proteins Pot1 and Cdc13.
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.
Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA.
Douglas L
DL
Theobald
Deborah S
DS
Wuttke
D000465:Algorithms; D000818:Animals; D018797:Cell Cycle Proteins / Q000737:chemistry*; D019295:Computational Biology / Q000379:methods*; D016813:Oxytricha / Q000235:genetics; D051304:Profilins; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D020539:Sequence Analysis, Protein / Q000379:methods*; D034501:Telomere-Binding Proteins / Q000737:chemistry* / Q000235:genetics
C086662:CDC3 protein, S cerevisiae; D018797:Cell Cycle Proteins; D051304:Profilins; D029701:Saccharomyces cerevisiae Proteins; D034501:Telomere-Binding Proteins