RRC ID 3349
Author Maita N, Anzai T, Aoyagi H, Mizuno H, Fujiwara H.
Title Crystal structure of the endonuclease domain encoded by the telomere-specific long interspersed nuclear element, TRAS1.
Journal J. Biol. Chem.
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.
Volume 279(39)
Pages 41067-76
Published 2004-9-24
DOI 10.1074/jbc.M406556200
PII M406556200
PMID 15247245
MeSH Amino Acid Sequence Aspartic Acid / chemistry Base Sequence Catalytic Domain Crystallography, X-Ray / methods DNA / chemistry DNA Mutational Analysis Electrons Endonucleases / chemistry* Humans Long Interspersed Nucleotide Elements* Magnesium / chemistry Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Nucleic Acid Conformation* Oligonucleotides / chemistry Plasmids / metabolism Protein Binding Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Telomere / chemistry Telomere / ultrastructure
IF 4.011
Times Cited 15
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