The Distinct Anchoring Mechanism of FtsY from Different Microbes
The Distinct Anchoring Mechanism of FtsY from Different Microbes
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不同微生物的 FtsY 的独特锚定机制
DOI：
10.1007/s00284-009-9439-2
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发表时间：
2009-09-01
影响因子：
2.6
通讯作者：
Li, Yong-Quan
中科院分区：
文献类型：
--
作者：
Dong, Hui-Jun;Jiang, Jun-Yun;Li, Yong-Quan
SRP受体FtsY参与膜蛋白的靶向和易位，一般由N端结构域和NG结构域组成。尽管微生物之间的FtsY在氨基酸组成和功能上高度同源，但不同细菌（如链球菌）的FtsY定位机制不同。本研究通过体内激光扫描共聚焦显微镜 (LSCM) 和体外分子技术发现了 coelicolor 和 E.coli。结果表明，S.coelicolorFtsY的N端结构域对于FtsY的锚定膜是不可缺少的，而E.coliFtsY的A结构域是可有可无的。此外，E的A结构域。根据位置图像和蛋白质印迹，大肠杆菌可能会促进自身结合膜。
The SRP receptor FtsY, which is involved in targeting and translocating membrane protein, is generally composed of the N-terminal domain and the NG domain. Although FtsY was highly homologous in the composition of amino acids and functions among microbes, the different mechanism in the location of FtsYs from different bacteria such asS. coelicolorandE.coliwere discovered in this study by laser scanning confocal microscope (LSCM) in vivo and molecular techniques in vitro. The results revealed that the N-terminal domain ofS.coelicolorFtsY was indispensable for FtsY’s anchoring membrane, and while the A domain ofE.coliFtsY was dispensable. Moreover, the A domain ofE. coliFtsY might promote itself to bind the membrane depending on the location images and Western blotting.