大肠杆菌核糖体蛋白L12的甲硫氨酸残基氧化会降低该蛋白的生物活性。
Oxidation of the methionine residues of Escherichia coli ribosomal protein L12 decreases the protein's biological activity.
作者信息
Caldwell P, Luk D C, Weissbach H, Brot N
出版信息
Proc Natl Acad Sci U S A. 1978 Nov;75(11):5349-52. doi: 10.1073/pnas.75.11.5349.
Abstract
Oxidation of ribosomal protein L12 with hydrogen peroxide converts the three methionine residues to methionine sulfoxide. The oxidized protein has a decreased ability to bind to ribosomes, interact with ribosomal protein L10, be precipitated by L12 antiserum, and serve as substrate for the acetylating enzyme that converts L12 to L7. Full activity of L12 is regained when the protein is reduced with 2-mercaptoethanol. Sedimentation equilibrium analysis shows that oxidation of the methionine residues in L12 causes the conversion of the protein from the dimer to the monomer form, and the results indicate that the dimer is the active form of the protein in the above reactions.
摘要
用过氧化氢氧化核糖体蛋白L12会将三个甲硫氨酸残基转化为甲硫氨酸亚砜。氧化后的蛋白与核糖体结合的能力下降，与核糖体蛋白L10相互作用的能力下降，被L12抗血清沉淀的能力下降，并且作为将L12转化为L7的乙酰化酶的底物的能力也下降。当用2-巯基乙醇还原该蛋白时，L12可恢复全部活性。沉降平衡分析表明，L12中甲硫氨酸残基的氧化导致该蛋白从二聚体形式转变为单体形式，结果表明二聚体是该蛋白在上述反应中的活性形式。
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Oxidation of the methionine residues of Escherichia coli ribosomal protein L12 decreases the protein's biological activity.大肠杆菌核糖体蛋白L12的甲硫氨酸残基氧化会降低该蛋白的生物活性。
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