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Nucleic Acids Research Advance Access originally published online on January 12, 2009
Nucleic Acids Research 2009 37(5):1541-1554; doi:10.1093/nar/gkn1081
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Nucleic Acids Research, 2009, Vol. 37, No. 5 1541-1554
© 2009 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

The effect of the TRF2 N-terminal and TRFH regions on telomeric G-quadruplex structures

Ilene M. Pedroso, William Hayward and Terace M. Fletcher*

Department of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, FL 33101-6129, USA

*To whom correspondence should be addressed. Tel: +1 305 243 6297; Fax: +1 305 243 3955; Email: tfletcher{at}med.miami.edu

Received September 16, 2008. Revised December 20, 2008. Accepted December 23, 2008.

The sequence of human telomeric DNA consists of tandem repeats of 5'-d(TTAGGG)-3'. This guanine-rich DNA can form G-quadruplex secondary structures which may affect telomere maintenance. A current model for telomere protection by the telomere-binding protein, TRF2, involves the formation of a t-loop which is stabilized by a strand invasion-like reaction. This type of reaction may be affected by G-quadruplex structures. We analyzed the influence of the arginine-rich, TRF2 N-terminus (TRF2B), as well as this region plus the TRFH domain of TRF2 (TRF2BH), on the structure of G-quadruplexes. Circular dichroism results suggest that oligonucleotides with 4, 7 and 8 5'-d(TTAGGG)-3' repeats form hybrid structures, a mix of parallel/antiparallel strand orientation, in K+. TRF2B stimulated the formation of parallel-stranded structures and, in some cases, intermolecular structures. TRF2BH also stimulated intermolecular but not parallel-stranded structures. Only full-length TRF2 and TRF2BH stimulated uptake of a telomeric single-stranded oligonucleotide into a plasmid containing telomeric DNA in the presence of K+. The results in this study suggest that G-quadruplex formation inhibits oligonucleotide uptake into the plasmid, but the inhibition can be overcome by TRF2. This study is the first analysis of the effects of TRF2 domains on G-quadruplex structures and has implications for the role of G-quadruplexes and TRF2 in the formation of t-loops.


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A. M. Baker, Q. Fu, W. Hayward, S. M. Lindsay, and T. M. Fletcher
The Myb/SANT domain of the telomere-binding protein TRF2 alters chromatin structure
Nucleic Acids Res., August 1, 2009; 37(15): 5019 - 5031.
[Abstract] [Full Text] [PDF]


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