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Nucleic Acids Research Advance Access originally published online on March 27, 2007
Nucleic Acids Research 2007 35(7):2107-2115; doi:10.1093/nar/gkm049
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Nucleic Acids Research, 2007, Vol. 35, No. 7 2107-2115
© 2007 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.

Molecular Biology

The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase

Zhong Yu1, Paul-André Genest1, Bas ter Riet1, Kate Sweeney2, Courtney DiPaolo2, Rudo Kieft2,{dagger}, Evangelos Christodoulou3, Anastassis Perrakis3, Jana M. Simmons4, Robert P. Hausinger4,5, Henri G.A.M. van Luenen1, Daniel J. Rigden6, Robert Sabatini2,{dagger} and Piet Borst1,*

1Division of Molecular Biology and Centre of Biomedical Genetics, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands, 2Global Infectious Diseases Program Marine Biological Laboratory, Woods Hole, MA 02543, USA, 3Division of Molecular Carcinogenesis, The Netherlands Cancer Institute, 1066 CX Amsterdam, The Netherlands, 4Department of Biochemistry & Molecular Biology and 5Department of Microbiology & Molecular Genetics, Michigan State University, East Lansing, MI 48824-4320, USA and 6School of Biological Sciences, University of Liverpool, Liverpool L69 7ZB, UK

*To whom correspondence should be addressed. Tel: +31 20 512 2880; Fax: +31 20 669 1383; Email: p.borst{at}nki.nl

Received October 11, 2006. Revised January 10, 2007. Accepted January 16, 2007.

Trypanosomatids contain an unusual DNA base J (ß-D-glucosylhydroxymethyluracil), which replaces a fraction of thymine in telomeric and other DNA repeats. To determine the function of base J, we have searched for enzymes that catalyze J biosynthesis. We present evidence that a protein that binds to J in DNA, the J-binding protein 1 (JBP1), may also catalyze the first step in J biosynthesis, the conversion of thymine in DNA into hydroxymethyluracil. We show that JBP1 belongs to the family of Fe2+ and 2-oxoglutarate-dependent dioxygenases and that replacement of conserved residues putatively involved in Fe2+ and 2-oxoglutarate-binding inactivates the ability of JBP1 to contribute to J synthesis without affecting its ability to bind to J-DNA. We propose that JBP1 is a thymidine hydroxylase responsible for the local amplification of J inserted by JBP2, another putative thymidine hydroxylase.

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

{dagger}Present Address: University of Georgia, Department of Biochemistry & Molecular Biology, Life Sciences Building, Room A130, 120 Green Street, Athens, GA 30602–7229.


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D. K. Ekanayake, M. J. Cipriano, and R. Sabatini
Telomeric co-localization of the modified base J and contingency genes in the protozoan parasite Trypanosoma cruzi
Nucleic Acids Res., October 8, 2007; 35(19): 6367 - 6377.
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