The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase.
The protein that binds to DNA base J in trypanosomatids has features of a thymidine hydroxylase.
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与锥形剂中与DNA碱基J结合的蛋白质具有胸苷羟化酶的特征。
DOI：
10.1093/nar/gkm049
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发表时间：
2007
影响因子：
14.9
通讯作者：
Borst, Piet
中科院分区：
文献类型：
--
作者：
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
锥虫含有一个不寻常的DNA碱基J（β-d-葡糖基羟甲基尿嘧啶），它取代了端粒和其他DNA重复序列中的一部分胸腺嘧啶。为了确定碱基J的功能，我们寻找催化J生物合成的酶。我们提出的证据表明，结合到DNA中的J的蛋白质，J-结合蛋白1（JBP 1），也可以催化J生物合成的第一步，DNA中的胸腺嘧啶转化为羟甲基尿嘧啶。我们表明，JBP 1属于家庭的Fe 2+和2-酮戊二酸依赖性双加氧酶和保守残基puponium参与Fe 2+和2-酮戊二酸结合的替代灭活的能力JBP 1有助于J的合成，而不影响其能力结合到J-DNA。我们建议，JBP 1是一种胸苷羟化酶负责本地放大J插入JBP 2，另一个假定的胸苷羟化酶。
Trypanosomatids contain an unusual DNA base J (β-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.