DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus
DmsD is required for the biogenesis of DMSO reductase in Escherichia coli but not for the interaction of the DmsA signal peptide with the Tat apparatus
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DOI：
10.1016/s0014-5793(02)03839-5
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发表时间：
2003-01-16
期刊：
影响因子：
3.5
通讯作者：
Robinson, C
中科院分区：
文献类型：
--
作者：
Ray, N;Oates, J;Robinson, C
DmsD 蛋白对于大肠杆菌中 DMSO 还原酶的生物合成至关重要，并结合 DmsA 亚基（Tat 底物）的信号肽。这表明其作为将 DmsA 前靶向易位酶的指导因子。在这里，我们分析了融合蛋白的输出，其中 DmsA 和 TorA 信号肽与绿色荧光蛋白融合。两种嵌合体都有效地输出到野生型大肠杆菌细胞的周质，并且我们表明它们的输出效率在缺乏 DmsD 的突变体中基本相同。真正的 Tat 底物 TMAO 还原酶也在 dmsD 突变体中有效输出。数据表明 DmsD 在 DMSO 还原酶生物发生/组装中发挥关键作用，但对于 DmsA 信号肽的功能不是必需的。 (C) 2002 年欧洲生化学会联合会。由 Elsevier Science B.V. 出版。保留所有权利。
The DmsD protein is essential for the biogenesis of DMSO reductase in Escherichia coli, and binds the signal peptide of the DmsA subunit, a Tat substrate. This suggests a role as a guidance factor to target pre-DmsA to the translocase. Here, we have analysed the export of fusion proteins in which the DmsA and TorA signal peptides are fused to green fluorescent protein. Both chimeras are efficiently exported to the periplasm in wild-type E. coli cells and we show that their export efficiencies are essentially identical in a mutant lacking DmsD. An authentic Tat substrate, TMAO reductase, is also efficiently exported in the dmsD mutant. The data indicate that DmsD carries out a critical role in DMSO reductase biogenesis/assembly but is not required for the functioning of the DmsA signal peptide. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.