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http://purl.uniprot.org/citations/16337232http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16337232http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16337232http://www.w3.org/2000/01/rdf-schema#comment"The double-stranded telomeric repeat-binding protein (TRP) AtTRP1 is isolated from Arabidopsis thaliana. Using gel retardation assays, we defined the C-terminal 97 amino acid residues, Gln464 to Val560 (AtTRP1(464-560)), as the minimal structured telomeric repeat-binding domain. This region contains a typical Myb DNA-binding motif and a C-terminal extension of 40 amino acid residues. The monomeric AtTRP1(464-560) binds to a 13-mer DNA duplex containing a single repeat of an A.thaliana telomeric DNA sequence (GGTTTAG) in a 1:1 complex, with a K(D) approximately 10(-6)-10(-7) M. Nuclear magnetic resonance (NMR) examination revealed that the solution structure of AtTRP1(464-560) is a novel four-helix tetrahedron rather than the three-helix bundle structure found in typical Myb motifs and other TRPs. Binding of the 13-mer DNA duplex to AtTRP1(464-560) induced significant chemical shift perturbations of protein amide resonances, which suggests that helix 3 (H3) and the flexible loop connecting H3 and H4 are essential for telomeric DNA sequence recognition. Furthermore, similar to that in hTRF1, the N-terminal arm likely contributes to or stabilizes DNA binding. Sequence comparisons suggested that the four-helix structure and the involvement of the loop residues in DNA binding may be features unique to plant TRPs."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2005.11.009"xsd:string
http://purl.uniprot.org/citations/16337232http://purl.org/dc/terms/identifier"doi:10.1016/j.jmb.2005.11.009"xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Ho C.H."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Ho C.H."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Chung B.C."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Chung B.C."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Hsiao H.H."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Hsiao H.H."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Chen C.M."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Chen C.M."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Sue S.C."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Sue S.C."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Huang T.H."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Huang T.H."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Cheng Y.H."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Cheng Y.H."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Hsueh K.L."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/author"Hsueh K.L."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/16337232http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string