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Publication Abstract from PubMed

The telomere-specific long interspersed nuclear element, TRAS1, encodes an endonuclease domain, TRAS1-EN, which specifically cleaves the telomeric repeat targets (TTAGG)n of insects and (TTAGGG)n of vertebrates. To elucidate the sequence-specific recognition properties of TRAS1-EN, we determined the crystal structure at 2.4-A resolution. TRAS1-EN has a four-layered alpha/beta sandwich structure; its topology is similar to apurinic/apyrimidinic endonucleases, but the beta-hairpin (beta10-beta11) at the edge of the DNA-binding surface makes an extra loop that distinguishes TRAS1-EN from cellular apurinic/apyrimidinic endonucleases. A protein-DNA complex model suggests that the beta10-beta11 hairpin fits into the minor groove, enabling interaction with the telomeric repeats. Mutational studies of TRAS1-EN also indicated that the Asp-130 and beta10-beta11 hairpin structure are involved in specific recognition of telomeric repeats.

Crystal structure of the endonuclease domain encoded by the telomere-specific long interspersed nuclear element, TRAS1.,Maita N, Anzai T, Aoyagi H, Mizuno H, Fujiwara H J Biol Chem. 2004 Sep 24;279(39):41067-76. Epub 2004 Jul 9. PMID:15247245^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.