2aje: Difference between revisions

Revision as of 17:28, 21 February 2008

Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain

OverviewOverview

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.

About this StructureAbout this Structure

2AJE is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain: a new fold with an additional C-terminal helix., Sue SC, Hsiao HH, Chung BC, Cheng YH, Hsueh KL, Chen CM, Ho CH, Huang TH, J Mol Biol. 2006 Feb 10;356(1):72-85. Epub 2005 Nov 22. PMID:16337232

Page seeded by OCA on Thu Feb 21 16:28:04 2008

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OCA

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 ==Overview==
-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.
+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.
 ==About this Structure==
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 [[Category: Arabidopsis thaliana]]
 [[Category: Single protein]]
-[[Category: Cheng, Y.H.]]
+[[Category: Cheng, Y H.]]
-[[Category: Chung, B.C.]]
+[[Category: Chung, B C.]]
-[[Category: Hsiao, H.H.]]
+[[Category: Hsiao, H H.]]
-[[Category: Huang, T.H.]]
+[[Category: Huang, T H.]]
-[[Category: Sue, S.C.]]
+[[Category: Sue, S C.]]
 [[Category: dna-binding]]
 [[Category: myb motif]]
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 [[Category: trp]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 18:03:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:28:04 2008''