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

التفاصيل البيبلوغرافية
العنوان: The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase
المؤلفون: Evangelos Christodoulou, Rudo Kieft, Jana M. Simmons, Daniel J. Rigden, Henri G.A.M. van Luenen, Kate Sweeney, Zhong Yu, Piet Borst, Paul André Genest, Robert P. Hausinger, Robert Sabatini, Anastassis Perrakis, Courtney DiPaolo, Bas ter Riet
المصدر: Nucleic Acids Research
بيانات النشر: Oxford University Press, 2007.
سنة النشر: 2007
مصطلحات موضوعية: Base J, Molecular Sequence Data, Protozoan Proteins, Biology, DNA-binding protein, Dioxygenases, Mixed Function Oxygenases, chemistry.chemical_compound, Biosynthesis, Glucosides, Genetics, Animals, Amino Acid Sequence, Binding site, Uracil, Molecular Biology, Leishmania, Binding Sites, Molecular biology, Thymine, Protein Structure, Tertiary, DNA-Binding Proteins, chemistry, Biochemistry, Amino Acid Substitution, Thymidine, DNA
الوصف: 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.
اللغة: English
تدمد: 1362-4962
0305-1048
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::562f38f06907e7881e84de8bc7288dd3
http://europepmc.org/articles/PMC1874643
حقوق: OPEN
رقم الأكسشن: edsair.doi.dedup.....562f38f06907e7881e84de8bc7288dd3
قاعدة البيانات: OpenAIRE