Biosynthesis of selenate reductase in Salmonella enterica: critical roles for the signal peptide and DmsD.
Biosynthesis of selenate reductase in Salmonella enterica: critical roles for the signal peptide and DmsD.
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DOI：
10.1099/mic.0.000381
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发表时间：
2016-12
期刊：
影响因子：
--
通讯作者：
Sargent F
中科院分区：
文献类型：
--
作者：
Connelly KRS;Stevenson C;Kneuper H;Sargent F
鼠伤寒沙门氏菌是一种革兰氏阴性菌，具有灵活的呼吸能力。在厌氧条件下，S.肠杆菌可以利用包括硒酸盐在内的一系列末端电子受体来维持呼吸电子传递。色葡萄肠硒酸还原酶是由ynfEFGH-dmsD操纵子编码的膜结合酶。预测活性酶包含至少三个亚基，其中YnfE是含铯的催化亚基。YnfE蛋白与N-末端双精氨酸信号肽合成，并且酶的生物合成由称为DmsD的信号肽结合分子伴侣协调。在这项工作中，S。已通过化学交联研究了肠道DmsD和YnfE信号肽。这些实验通过遗传方法进行补充，其鉴定了YnfE信号肽内的DmsD结合表位。YnfE信号肽残基L24和A28显示对于活性硒酸还原酶的组装是重要的。相反，一个随机的遗传筛选确定DmsD V16残基是重要的信号肽识别和硒酸还原酶组装。
Salmonella enterica serovar Typhimurium is a Gram-negative bacterium with a flexible respiratory capability. Under anaerobic conditions, S. enterica can utilize a range of terminal electron acceptors, including selenate, to sustain respiratory electron transport. The S. enterica selenate reductase is a membrane-bound enzyme encoded by the ynfEFGH-dmsD operon. The active enzyme is predicted to comprise at least three subunits where YnfE is a molybdenum-containing catalytic subunit. The YnfE protein is synthesized with an N-terminal twin-arginine signal peptide and biosynthesis of the enzyme is coordinated by a signal peptide binding chaperone called DmsD. In this work, the interaction between S. enterica DmsD and the YnfE signal peptide has been studied by chemical crosslinking. These experiments were complemented by genetic approaches, which identified the DmsD binding epitope within the YnfE signal peptide. YnfE signal peptide residues L24 and A28 were shown to be important for assembly of an active selenate reductase. Conversely, a random genetic screen identified the DmsD V16 residue as being important for signal peptide recognition and selenate reductase assembly.
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影响因子：
3.5
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