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Nucleic Acids Research Advance Access originally published online on March 26, 2008
Nucleic Acids Research 2008 36(8):2739-2755; doi:10.1093/nar/gkn030
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Nucleic Acids Research, 2008, Vol. 36, No. 8 2739-2755
© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Structural Biology

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

Sunggeon Ko1,3,{dagger}, Sung-Hoon Jun2,{dagger}, Hansol Bae2, Jung-Sue Byun2,3, Woong Han1,3, Heeyoung Park1,3, Seong Wook Yang2, Sam-Yong Park4, Young Ho Jeon5, Chaejoon Cheong5, Woo Taek Kim2,*, Weontae Lee1,3,* and Hyun-Soo Cho2,3,*

1Department of Biochemistry, 2Department of Biology, 3Protein Network Research Center, College of Life Sciences and Biotechnology, Yonsei University, Seoul 120-749, Korea, 4Protein Design Laboratory, Yokohama City University, Suehiro 1-7-29, Tsurumi-ku, Yokohama 230-0045, Japan and 5Magnetic Resonance Team, Korea Basic Science Institute (KBSI), Ochang, Chungbuk 363-883, Korea

*To whom correspondence should be addressed. Tel: +82 2 2123 5651; Fax: +82 2 312 5657; Email: hscho8{at}yonsei.ac.kr, wlee{at}spin.yonsei.ac.kr, wtkim{at}yonsei.ac.kr

Received September 2, 2007. Revised January 17, 2008. Accepted January 18, 2008.

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 {alpha}-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.

{dagger}The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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