DiPaolo Courtney

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  • Article
    The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase
    (Oxford University Press, 2007-03-27) 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
    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.