| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 2820335 | Gene | 2006 | 7 Pages |
Telomere function is mediated by a complex of proteins bound to double-stranded and single-stranded telomeric repeats. A key player in this complex is TRF1, which binds to duplex TTAGGG repeats and acts as a negative regulator of telomere length. This protein's domain structure, as defined by studies with mammalian orthologs, consists of an N-terminal acidic domain, a dimerization domain, and a C-terminal Myb DNA binding domain. TRF1 from Xenopus laevis was cloned and sequenced, and the encoded protein found to have a similar structure but with a very short acidic domain. This short acidic domain was confirmed in Xenopus tropicalis, a true diploid, by cloning of cDNA sequences by RACE and analysis of the genomic locus. The TRF1 transcript is expressed in developing and adult frogs. Compared to the mammalian orthologs, the Xenopus genes are the most distantly related vertebrate examples characterized to date. Since adult Xenopus ubiquitously express somatic telomerase activity, proteins that regulate telomerase access to the chromosome ends are important in regulating telomere length in normal somatic tissue. The structure of Xenopus TRF1 has implications for its regulation by tankyrase.
