Crystal structure of the endonuclease domain encoded by the telomere-specific long interspersed nuclear element, TRAS1.

The Journal of Biological Chemistry
Nobuo MaitaHaruhiko Fujiwara

Abstract

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.

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Citations

Sep 1, 2005·Chromosome Research : an International Journal on the Molecular, Supramolecular and Evolutionary Aspects of Chromosome Biology·Haruhiko FujiwaraKenji K Kojima
Feb 9, 2006·Chemical Reviews·Patrick J O'Brien
Jun 7, 2011·Molecular Biology and Evolution·Mizuko Osanai-Futahashi, Haruhiko Fujiwara
Jul 13, 2007·Nucleic Acids Research·Kostas RepanasOliver Weichenrieder
Oct 17, 2009·Journal of Theoretical Biology·Luis P Villarreal, Guenther Witzany
Mar 14, 2017·Nature Reviews. Genetics·Tania SultanaPascale Lesage
Jun 1, 2018·Genome Biology and Evolution·Eri Nishiyama, Kazuhiko Ohshima
Jun 25, 2015·Microbiology Spectrum·Haruhiko Fujiwara

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