ArticleNucleic acids research2008
Structure of the DNA-binding domain of NgTRF1 reveals unique features of plant telomere-binding proteins.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 32 citations in OpenAlex.
- TRB proteins in moss reveal their evolutionarily conserved roles in plant development and telomere maintenance.The Plant journal : for cell and molecular biology · 2025Article
- Telomeres: an organized string linking plants and mammals.Biology direct · 2024Review
- Completing the TRB family: newly characterized members show ancient evolutionary origins and distinct localization, yet similar interactions.Plant molecular biology · 2023Article
- Telomere association of Oryza sativa telomere repeat-binding factor like 1 and its roles in telomere maintenance and development in rice, Oryza sativa L.BMB reports · 2018Article
- Structure of the replication regulator Sap1 reveals functionally important interfaces.Scientific reports · 2018Article
- Interaction studies of carbon nanomaterials and plasma activated carbon nanomaterials solution with telomere binding protein.Scientific reports · 2017Article
- Telomere- and Telomerase-Associated Proteins and Their Functions in the Plant Cell.Frontiers in plant science · 2016Review
- Using Centromere Mediated Genome Elimination to Elucidate the Functional Redundancy of Candidate Telomere Binding Proteins in Arabidopsis thaliana.Frontiers in genetics · 2015Article
- Cell growth defect factor1/chaperone-like protein of POR1 plays a role in stabilization of light-dependent protochlorophyllide oxidoreductase in Nicotiana benthamiana and Arabidopsis.The Plant cell · 2013Article
- SVM based model generation for binding site prediction on helix turn helix motif type of transcription factors in eukaryotes.Bioinformation · 2013Article
- One identity or more for telomeres?Frontiers in oncology · 2013Article
- Structure of the Trichomonas vaginalis Myb3 DNA-binding domain bound to a promoter sequence reveals a unique C-terminal β-hairpin conformation.Nucleic acids research · 2012Article
- Comparative biology of telomeres: where plants stand.FEBS letters · 2010Review
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Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Telomeres are protein-DNA elements that are located at the ends of linear eukaryotic chromosomes. In concert with various telomere-binding proteins, they play an essential role in genome stability. We determined the structure of the DNA-binding domain of NgTRF1, a double-stranded telomere-binding protein of tobacco, using multidimensional NMR spectroscopy and X-ray crystallography. The DNA-binding domain of NgTRF1 contained the Myb-like domain and C-terminal Myb-extension that is characteristic of plant double-stranded telomere-binding proteins. It encompassed amino acids 561-681 (NgTRF1(561-681)), and was composed of 4 alpha-helices. We also determined the structure of NgTRF1(561-681) bound to plant telomeric DNA. We identified several amino acid residues that interacted directly with DNA, and confirmed their role in the binding of NgTRF1 to telomere using site-directed mutagenesis. Based on a structural comparison of the DNA-binding domains of NgTRF1 and human TRF1 (hTRF1), NgTRF1 has both common and unique DNA-binding properties. Interaction of Myb-like domain with telomeric sequences is almost identical in NgTRF1(561-681) with the DNA-binding domain of hTRF1. The interaction of Arg-638 with the telomeric DNA, which is unique in NgTRF1(561-681), may provide the structural explanation for the specificity of NgTRF1 to the plant telomere sequences, (TTTAGGG)(n).
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