Related Experiment Video
Updated: Aug 9, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Prediction of multiple tandem OB-fold domains in telomere end-binding proteins Pot1 and Cdc13
Douglas L Theobald1, Deborah S Wuttke
1Department of Chemistry and Biochemistry, University of Colorado at Boulder, Boulder, CO 80309, USA.
Abstract:
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.
Related Concept Videos
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conserved Binding Sites
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Telomeres and Telomerase
Tail-anchoring of Proteins in the ER Membrane
Single-Strand DNA Binding Proteins
Telomeres and Telomerase

