The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr (YpdA) disulfide reductase reduce S-bacillithiolated proteins.
The Bacillus subtilis monothiol bacilliredoxin BrxC (YtxJ) and the Bdr (YpdA) disulfide reductase reduce S-bacillithiolated proteins.
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枯草芽孢杆菌单硫醇杆菌氧还蛋白BrxC（YtxJ）和Bdr（YpdA）二硫键还原酶还原S-杆菌硫醇化蛋白。
DOI：
10.1016/j.redox.2021.101935
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发表时间：
2021-06
期刊：
影响因子：
11.4
通讯作者：
Helmann JD
中科院分区：
文献类型：
--
作者：
Gaballa A;Su TT;Helmann JD
细菌细胞质通常是还原环境，其中蛋白质半胱氨酸残基保持其硫醇形式。低分子量硫醇杆菌硫醇 (BSH) 在多种细菌物种中充当通用硫醇还原剂，类似于谷胱甘肽。通过 BSH（S-杆菌硫醇化）形成二硫键修饰的蛋白质在杆菌氧化还蛋白、BrxA 和 BrxB 的作用下被还原。在这里，YtxJ 蛋白被鉴定为单硫醇杆菌氧化还蛋白，重命名为 BrxC，并且参与从氧化胞质蛋白（包括甘油醛 3-磷酸脱氢酶 GapA 和 GapB）中去除 BSH。 BrxC 还可以使杆菌氧化还蛋白 BrxB 的混合二硫化物形式脱杆菌硫醇。 Bdr 是一种硫氧还蛋白还原酶样黄素蛋白，具有二硫化杆菌硫醇 (BSSB) 还原酶活性。在此，Bdr 还显示出作为杆菌氧化还蛋白还原酶的功能。 Bdr 和 BrxB 协同发挥作用，使 OhrR 脱硫基化，OhrR 是一种转录因子，受其唯一半胱氨酸残基上的 S-硫基化调节。总的来说，这些结果扩展了我们对 BSH 氧化还原网络的理解，该网络由三种杆菌氧化还蛋白和一种 BSSB 还原酶组成，可对抗二硫键应激条件下引起的广泛的蛋白质 S-杆菌硫醇化。芽孢杆菌硫醇是枯草芽孢杆菌中主要的低分子量硫醇。氧化应激导致蛋白质 S-杆菌硫醇化。 BrxC 作为单硫醇类杆菌氧化还蛋白发挥作用。 Bdr 杆菌硫醇二硫化物还原酶也是一种杆菌氧化还蛋白。
The bacterial cytosol is generally a reducing environment with protein cysteine residues maintained in their thiol form. The low molecular weight thiol bacillithiol (BSH) serves as a general thiol reductant, analogous to glutathione, in a wide range of bacterial species. Proteins modified by disulfide bond formation with BSH (S-bacillithiolation) are reduced by the action of bacilliredoxins, BrxA and BrxB. Here, the YtxJ protein is identified as a monothiol bacilliredoxin, renamed BrxC, and is implicated in BSH removal from oxidized cytosolic proteins, including the glyceraldehyde 3-phosphate dehydrogenases GapA and GapB. BrxC can also debacillithiolate the mixed disulfide form of the bacilliredoxin BrxB. Bdr is a thioredoxin reductase-like flavoprotein with bacillithiol-disulfide (BSSB) reductase activity. Here, Bdr is shown to additionally function as a bacilliredoxin reductase. Bdr and BrxB function cooperatively to debacillithiolate OhrR, a transcription factor regulated by S-bacillithiolation on its sole cysteine residue. Collectively, these results expand our understanding of the BSH redox network comprised of three bacilliredoxins and a BSSB reductase that serve to counter the widespread protein S-bacillithiolation that results from conditions of disulfide stress. Bacillithiol is the major low molecular weight thiol in Bacillus subtilis. Oxidative stress leads to protein S-bacillithiolation. BrxC functions as a monothiol class bacilliredoxin. The Bdr bacillithiol disulfide reductase is also a bacilliredoxin.
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影响因子：
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作者：
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