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.

Keywords

BiologyDNAThymineBiochemistryThymidineEnzymeDNA-binding proteinBiosynthesisMolecular biologyGeneTranscription factor

MeSH Terms

Amino Acid SequenceAmino Acid SubstitutionAnimalsBinding SitesDNA-Binding ProteinsDioxygenasesGlucosidesLeishmaniaMixed Function OxygenasesMolecular Sequence DataProtein StructureTertiaryProtozoan ProteinsUracil

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Publication Info

Year
2007
Type
article
Volume
35
Issue
7
Pages
2107-2115
Citations
87
Access
Closed

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Cite This

Zhong Yu, Paul-André Genest, Bas ter Riet et al. (2007). The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase. Nucleic Acids Research , 35 (7) , 2107-2115. https://doi.org/10.1093/nar/gkm049

Identifiers

DOI
10.1093/nar/gkm049
PMID
17389644
PMCID
PMC1874643

Data Quality

Data completeness: 86%