Solution structure of the Arabidopsis thaliana telomeric repeat-binding protein DNA binding domain: A new fold with an additional C-terminal helix
Resource
J. Mol. Biol. 356, 72–85
Journal
J. Mol. Biol. 356, 72–85
Pages
-
Date Issued
2006
Date
2006
Author(s)
Sue, Shih-Che
Hsiao, Hsin-hao
Chung, Ben C.P.
Cheng, Ying-Hsien
Hsueh, Kuang-Lung
Chen, Chung Mong
Ho, Chia-Hsing
Huang, Tai-Huang
DOI
246246/2006111501275445
Abstract
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 (AtTRP1464-560), 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 AtTRP1464-560 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 KDw10K6–10K7 M. Nuclear
magnetic resonance (NMR) examination revealed that the solution
structure of AtTRP1464-560 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 AtTRP1464-560 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.
Subjects
telomere binding protein
Myb domain
NMR structure
AtTRP
Publisher
Taipei:National Taiwan University Dept Chem Engn
Type
journal article
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