Precluding uracil from DNA.
نویسندگان
چکیده
Two enzymes, dUTP pyrophosphatase and uracil-DNA glycosylase, prevent the misincorporation of uracil into the genome in distinct manners. The atomic structures of these proteins complexed with substrate analogs reveal the structural basis for uracil recognition and suggest a novel mechanism of DNA repair.
منابع مشابه
AB Initio Calculations and IR Studies of Tautometric forms of Uracil and Cytosine and comparing results in different temperatures (25˚C, 37˚C and 40˚C).
In this paper,the molecular geometry for three tautomers of uracil and four tautomers of cytosine has been analyzed. vibrational IR spectra of the tautomers were investigated at HF and B3LYP level using the AB initio 6-31G* and LANL2DZ basis sets from the program package Gaussian 98 (A.7 Public Domain version). The physico-chemical and biochemical properties of uracil and cytosine are one of...
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The DNA repair enzyme uracil-DNA glycosylase from Mycoplasma lactucae (831-C4) was purified 1,657-fold by using affinity chromatography and chromatofocusing techniques. The only substrate for the enzyme was DNA that contained uracil residues, and the Km of the enzyme was 1.05 +/- 0.12 microM for dUMP containing DNA. The product of the reaction was uracil, and it acted as a noncompetitive inhibi...
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متن کاملNovel activities of human uracil DNA N-glycosylase for cytosine-derived products of oxidative DNA damage.
Uracil DNA N-glycosylase is a repair enzyme that releases uracil from DNA. A major function of this enzyme is presumably to protect the genome from pre-mutagenic uracil resulting from deamination of cytosine in DNA. Here, we report that human uracil DNA N-glycosylase also recognizes three uracil derivatives that are generated as major products of cytosine in DNA by hydroxyl radical attack or ot...
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عنوان ژورنال:
- Structure
دوره 4 12 شماره
صفحات -
تاریخ انتشار 1996