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MoaE 参与 对氧化应激的响应。

MoaE Is Involved in Response to Oxidative Stress in .

机构信息

MOE Key Laboratory of Biosystems Homeostasis and Protection, Institute of Biophysics, College of Life Sciences, Zhejiang University, Hangzhou 310027, China.

出版信息

Int J Mol Sci. 2023 Jan 26;24(3):2441. doi: 10.3390/ijms24032441.

DOI:10.3390/ijms24032441
PMID:36768763
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC9916421/
Abstract

Molybdenum ions are covalently bound to molybdenum pterin (MPT) to produce molybdenum cofactor (Moco), a compound essential for the catalytic activity of molybdenum enzymes, which is involved in a variety of biological functions. MoaE is the large subunit of MPT synthase and plays a key role in Moco synthesis. Here, we investigated the function of MoaE in (DrMoaE) in vitro and in vivo, demonstrating that the protein contributed to the extreme resistance of . The crystal structure of DrMoaE was determined by 1.9 Å resolution. DrMoaE was shown to be a dimer and the dimerization disappeared after Arg110 had been mutated. The deletion of resulted in sensitivity to DNA damage stress and a slower growth rate in . The increase in transcript levels the and accumulation of intracellular reactive oxygen species levels under oxidative stress suggested that it was involved in the antioxidant process in . In addition, treatment with the base analog 6-hydroxyaminopurine decreased survival and increased intracellular mutation rates in deletion mutant strains. Our results reveal that MoaE plays a role in response to external stress mainly through oxidative stress resistance mechanisms in .

摘要

钼离子与钼喋呤(MPT)共价结合,产生钼辅因子(Moco),这是钼酶催化活性所必需的化合物,参与多种生物学功能。MoaE 是 MPT 合酶的大亚基,在 Moco 合成中起着关键作用。在这里,我们研究了 DrMoaE 在体外和体内的功能,证明该蛋白有助于 (DrMoaE)的极端耐药性。通过 1.9 Å 分辨率确定了 DrMoaE 的晶体结构。结果表明 DrMoaE 是二聚体,Arg110 突变后二聚体消失。缺失导致对 DNA 损伤应激的敏感性增加和 在 中的生长速度减慢。在氧化应激下 转录水平的增加 和细胞内活性氧水平的积累表明它参与了 在抗氧化过程中的作用。此外,用碱基类似物 6-羟基氨基嘌呤处理会降低 在 删除突变株中的存活率并增加细胞内突变率。我们的研究结果表明,MoaE 通过在 中抵抗氧化应激的机制,主要在应对外部应激中发挥作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/150972f3d655/ijms-24-02441-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/bb0ed8f2690e/ijms-24-02441-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/b62e863014a5/ijms-24-02441-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/690188e1bcee/ijms-24-02441-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/8800c676b4c3/ijms-24-02441-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/541c6f168637/ijms-24-02441-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/150972f3d655/ijms-24-02441-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/bb0ed8f2690e/ijms-24-02441-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/b62e863014a5/ijms-24-02441-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/690188e1bcee/ijms-24-02441-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/8800c676b4c3/ijms-24-02441-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/541c6f168637/ijms-24-02441-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/477b/9916421/150972f3d655/ijms-24-02441-g006.jpg

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