The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase
ter Riet, Bas
Simmons, Jana M.
Hausinger, Robert P.
van Luenen, Henri G. A. M.
Rigden, Daniel J.
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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.
© 2007 The Author et al. 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. The definitive version was published in Nucleic Acids Research 35 (2007): 2107-2115, doi:10.1093/nar/gkm049.
Suggested CitationArticle: Yu, Zhong, Genest, Paul-Andre, ter Riet, Bas, Sweeney, Kate, DiPaolo, Courtney, Kieft, Rudo, Christodoulou, Evangelos, Perrakis, Anastassis, Simmons, Jana M., Hausinger, Robert P., van Luenen, Henri G. A. M., Rigden, Daniel J., Sabatini, Robert, Borst, Piet, "The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase", Nucleic Acids Research 35 (2007): 2107-2115, DOI:10.1093/nar/gkm049, https://hdl.handle.net/1912/1566
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