Journal
STRUCTURE
Volume 12, Issue 10, Pages 1877-1879Publisher
CELL PRESS
DOI: 10.1016/j.str.2004.07.015
Keywords
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Funding
- NIGMS NIH HHS [R01 GM059414, R01 GM059414-01] Funding Source: Medline
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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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