A regulatory domain controls the transport activity of a twin-arginine signal peptide.
A regulatory domain controls the transport activity of a twin-arginine signal peptide.
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调节结构域控制双精氨酸信号肽的转运活性。
DOI：
10.1016/j.febslet.2013.09.005
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发表时间：
2013
期刊：
影响因子：
3.5
通讯作者：
Bowman L
中科院分区：
文献类型：
--
作者：
Bowman L
双精氨酸转运（达特）途径是细菌跨膜转运折叠蛋白的途径。蛋白质通过信号肽靶向达特移位酶，所述信号肽具有由极性n-区、疏水性h-区和极性c-区组成的共同三重结构。本文对大肠杆菌[NiFe]氢化酶-1的信号肽进行了研究。氢化酶-1信号肽包含具有保守的一级结构的延伸的n-区。遗传学和生物化学的方法表明，信号肽N-区是必不可少的氢化酶组装和作为一个调节结构域控制的信号肽的运输活动。
The twin-arginine translocation (Tat) pathway is used by bacteria for the transmembrane transport of folded proteins. Proteins are targeted to the Tat translocase by signal peptides that have common tripartite structures consisting of polar n-regions, hydrophobic h-regions, and polar c-regions. In this work, the signal peptide of [NiFe] hydrogenase-1 fromEscherichia colihas been studied. The hydrogenase-1 signal peptide contains an extended n-region that has a conserved primary structure. Genetic and biochemical approaches reveal that the signal peptide n-region is essential for hydrogenase assembly and acts as a regulatory domain controlling transport activity of the signal peptide.