Okochi Mina, Kanie Kei, Kurimoto Masaki, Yohda Masafumi, Honda Hiroyuki
Department of Biotechnology, School of Engineering, Nagoya University, Furo-cho, Chikusa-ku, Nagoya, Japan.
Appl Microbiol Biotechnol. 2008 Jun;79(3):443-9. doi: 10.1007/s00253-008-1450-1. Epub 2008 Apr 29.
Prefoldin is a jellyfish-shaped hexameric chaperone that captures a protein-folding intermediate and transfers it to the group II chaperonin for correct folding. In this work, we characterized the organic solvent tolerance of Escherichia coli cells that overexpress prefoldin and group II chaperonin from a hyperthermophilic archeaum, Pyrococcus horikoshii OT3. The colony-forming efficiency of E. coli cells overexpressing prefoldin increased by 1,000-fold and decreased the accumulation of intracellular organic solvent. The effect was impaired by deletions of the region responsible for the chaperone function of prefoldin. Therefore, we concluded that prefoldin endows E. coli cells by preventing accumulation of intracellular organic solvent through its molecular chaperone activity.
预折叠蛋白是一种水母状的六聚体伴侣蛋白，它捕获蛋白质折叠中间体并将其转移到Ⅱ型伴侣蛋白中进行正确折叠。在这项研究中，我们对过表达来自嗜热古菌火球菌OT3的预折叠蛋白和Ⅱ型伴侣蛋白的大肠杆菌细胞的有机溶剂耐受性进行了表征。过表达预折叠蛋白的大肠杆菌细胞的集落形成效率提高了1000倍，并减少了细胞内有机溶剂的积累。预折叠蛋白负责伴侣功能的区域缺失会削弱这种效果。因此，我们得出结论，预折叠蛋白通过其分子伴侣活性防止细胞内有机溶剂的积累，从而赋予大肠杆菌细胞耐受性。
