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Structure. 2004 Oct;12(10):1877-9.

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

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Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA.


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.

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