The SurA periplasmic PPlase lacking its parvulin domains functions in vivo and has chaperone activity
The SurA periplasmic PPlase lacking its parvulin domains functions in vivo and has chaperone activity
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DOI：
10.1093/emboj/20.1.285
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发表时间：
2001-01-15
期刊：
影响因子：
11.4
通讯作者：
Gross, CA
中科院分区：
文献类型：
--
作者：
Behrens, S;Maier, R;Gross, CA
大肠杆菌周质肽基脯氨酸异构酶（PPIase） SurA参与外膜孔蛋白的成熟，SurA由一个实质性的n端区域、两个迭代的parvulin样结构域和一个c端尾部组成。在这里，我们发现缺乏两个parvulin样结构域的SurA变体在体外表现出不依赖ppiase的伴侣样活性，并且几乎完全补充了完整SurA的体内功能。与其他类似大小的蛋白质相比，SurA与体外合成的孔蛋白优先相互作用（>50倍），这使我们认为SurA的伴侣蛋白样功能优先促进外膜蛋白的成熟。
The Escherichia coli periplasmic peptidyl-prolyl isomerase (PPIase) SurA is involved in the maturation of outer membrane porins, SurA consists of a substantial N-terminal region, two iterative parvulin-like domains and a C-terminal tail. Here we show that a variant of SurA lacking both parvulin-like domains exhibits a PPIase-independent chaperone-like activity in vitro and almost completely complements the in vivo function of intact SurA. SurA interacts preferentially (>50-fold) with in vitro synthesized porins over other similarly sized proteins, leading us to suggest that the chaperone-like function of SurA preferentially facilitates maturation of outer membrane proteins.