PMID:17389644
| Citation |
Yu, Z, Genest, PA, ter Riet, B, Sweeney, K, DiPaolo, C, Kieft, R, Christodoulou, E, Perrakis, A, Simmons, JM, Hausinger, RP, van Luenen, HG, Rigden, DJ, Sabatini, R and Borst, P (2007) The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase. Nucleic Acids Res. 35:2107-15 |
|---|---|
| Abstract |
Trypanosomatids contain an unusual DNA base J (beta-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 Fe(2+) and 2-oxoglutarate-dependent dioxygenases and that replacement of conserved residues putatively involved in Fe(2+) 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. |
| Links |
PubMed PMC1874643 Online version:10.1093/nar/gkm049 |
| Keywords |
Amino Acid Sequence; Amino Acid Substitution; Animals; Binding Sites; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/classification; DNA-Binding Proteins/metabolism; Dioxygenases/classification; Glucosides/biosynthesis; Glucosides/chemistry; Glucosides/metabolism; Leishmania/genetics; Mixed Function Oxygenases/chemistry; Mixed Function Oxygenases/classification; Mixed Function Oxygenases/metabolism; Molecular Sequence Data; Protein Structure, Tertiary; Protozoan Proteins/chemistry; Protozoan Proteins/classification; Protozoan Proteins/metabolism; Uracil/analogs & derivatives; Uracil/biosynthesis; Uracil/chemistry; Uracil/metabolism |
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