Structure of the DNA-binding domain of NgTRF1 reveals unique features of plant telomere-binding proteins

Sunggeon Ko, Sung Hoon Jun, Hansol Bae, Jung Sue Byun, Woong Han, Heeyoung Park, Seong Wook Yang, Sam Yong Park, Young Ho Jeon, Chaejoon Cheong, Woo Taek Kim, Weontae Lee, Hyun Soo Cho

Research output: Contribution to journalArticle

21 Citations (Scopus)


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 (NgTRF1561-681), and was composed of 4 α-helices. We also determined the structure of NgTRF1561-681 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 NgTRF1561-681 with the DNA-binding domain of hTRF1. The interaction of Arg-638 with the telomeric DNA, which is unique in NgTRF1561-681, may provide the structural explanation for the specificity of NgTRF1 to the plant telomere sequences, (TTTAGGG)n.

Original languageEnglish
Pages (from-to)2739-2755
Number of pages17
JournalNucleic acids research
Issue number8
Publication statusPublished - 2008 May

All Science Journal Classification (ASJC) codes

  • Genetics

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