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首页> 外文期刊>Biochemistry >Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli
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Characterization of FimC, a periplasmic assembly factor for biogenesis of type 1 pili in Escherichia coli

机译：FimC的表征，FimC是大肠埃希氏菌中1型菌毛生物发生的周质组装因子

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摘要

Assembly of type 1 pill from Escherichia coli is mediated by FimC, a periplasmic chaperone (assembly factor) consisting of two immunoglobulin-like domains. FimC is assumed to recognize the individual pilus subunits in the periplasm mainly via their conserved C-terminal segments and to deliver the:subunits to an assembly platform in the outer membrane. Here we present the first biochemical characterization of a periplasmic pilus chaperone and analyze the importance of the two chaperone domains for stability and function. Comparison of the isolated C-terminal domain with wild-type FimC revealed a strongly reduced thermodynamic stability, indicating strong interdomain interactions. The affinity of FimC toward a peptide corresponding to the 11 C-terminal residues of the type 1 pilus adhesin FimH is at least 1000-fold lower compared to binding of intact FimH, confirming that bacterial pilus chaperones, unlike other chaperones, specifically interact with folded pilus subunits. [References: 43]
机译：大肠杆菌1型药丸的组装由FimC介导，FimC是一种由两个免疫球蛋白样结构域组成的周质伴侣（组装因子）。假设FimC主要通过其保守的C末端片段识别周质中的各个菌毛亚基，并将亚基递送到外膜的组装平台。在这里，我们介绍周质菌毛伴侣的第一个生化特征，并分析两个伴侣域对于稳定性和功能的重要性。分离的C末端域与野生型FimC的比较显示，热力学稳定性大大降低，表明域间相互作用很强。与完整FimH的结合相比，FimC对对应于1型菌毛粘附素FimH的11个C末端残基的肽的亲和力至少低1000倍，证实细菌菌毛伴侣分子与其他伴侣分子特异性相互作用菌毛亚基。 [参考：43]

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