Spotlight onTracy Palmer.
Spotlight onTracy Palmer.
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聚焦特雷西·帕尔默。
DOI：
10.1093/femsle/fnw271
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发表时间：
2016
影响因子：
2.1
通讯作者：
Palmer T
中科院分区：
文献类型：
--
作者：
Palmer T
我的团队致力于研究细菌中蛋白质运输的机制。自从1996年开始独立工作以来，我一直对了解细菌如何组装呼吸所必需的复杂金属酶感兴趣。我的工作与英国和加拿大的同事一起，帮助确定了模式生物大肠杆菌中的双精氨酸蛋白转运（达特）系统（萨金特等人，1998;韦纳等人，1998）。达特途径转运折叠蛋白穿过细菌细胞质膜，底物被达特机制识别，因为它们具有含有保守的双精氨酸基序的N-末端信号肽（Berks 1996）。大肠杆菌中有28个左右的达特底物蛋白。大肠杆菌，其中约三分之二的结合氧化还原辅因子非-
My group works on mechanisms of protein transport in bacteria. Since I started my independent career in 1996, I have been interested in understanding how bacteria assemble the complex metalloenzymes that are essential for respiration. My work, alongside that of colleagues in the UK and Canada, helped to define the twin arginine protein transport (Tat) system in the model organism Escherichia coli (Sargent et al. 1998; Weiner et al.1998). The Tat pathway transports folded proteins across the bacterial cytoplasmic membrane and substrates are recognised by the Tat machinery because they have an N-terminal signal peptide containing a conserved twin-arginine motif (Berks 1996). There are some 28 or so Tat substrate proteins in E. coli, and approximately two-thirds of them bind redox cofactors non-