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首页> 外文期刊>EMBO Journal >Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli
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Methionine sulfoxide reductases protect Ffh from oxidative damages in Escherichia coli

机译：蛋氨酸亚砜还原酶保护Ffh在大肠杆菌氧化损害

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摘要

In proteins, methionine residues are primary targets for oxidation. Methionine oxidation is reversed by methionine sulfoxide reductases A and B, a class of highly conserved enzymes. Ffh protein, a component of the ubiquitous signal recognition particle, contains a methionine-rich domain, interacting with a small 4.5S RNA. In vitro analyses reported here show that: (i) oxidized Ffh is unable to bind 4.5S RNA, (ii) oxidized Ffh contains methionine sulfoxide residues, (iii) oxidized Ffh is a substrate for MsrA and MsrB enzymes; and (iv) MsrA/B repairing activities allow oxidized Ffh to recover 4.5S RNA-binding abilities. In vivo analyses reveal that: ( i) Ffh synthesized in the msrA msrB mutant contains methionine sulfoxide residues and is unstable, ( ii) msrA msrB mutant requires high levels of Ffh synthesis for growth and ( iii) msrA msrB mutation leads to defects in Ffh-dependent targeting of MalF. We conclude that MsrA and MsrB are required to repair Ffh oxidized by reactive oxygen species produced by aerobic metabolism, establishing an as-yet undescribed link between protein targeting and oxidation.
机译：在蛋白质中,蛋氨酸残留初选氧化的目标。逆转的蛋氨酸亚砜还原酶A和B,一类高度保守的酶。蛋白质,无处不在的信号的一个组成部分识别粒子,包含一个methionine-rich域,与一个小互动4.5 s RNA。体外分析报告显示:(i)氧化Ffh无法绑定4.5 s RNA, (2)氧化Ffh包含蛋氨酸亚砜残留物,(iii)氧化Ffh的基质同行和MsrB酶;活动使氧化Ffh恢复4.5秒rna结合的能力。: (i) Ffh msrA msrB合成突变体包含蛋氨酸亚砜残留是不稳定的,(2)微软msrB突变要求高吗增长水平的Ffh合成和(iii)同行msrB突变导致缺陷Ffh-dependent MalF的目标。同行和MsrB需要修复Ffh氧化有氧运动产生的活性氧新陈代谢,建立至今未定蛋白质定位和氧化之间的联系。

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