Research Institute of Molecular Pathology, Vienna, Austria.
Curr Opin Struct Biol. 2010 Apr;20(2):253-8. doi: 10.1016/j.sbi.2010.01.014. Epub 2010 Feb 24.
Structure-function analysis of DegP revealed a novel mechanism for protease and chaperone regulation. Binding of unfolded proteins induces the oligomer reassembly from the resting hexamer (DegP6) into the functional protease-chaperone DegP12/24. The newly formed cage exhibits the characteristics of a proteolytic folding chamber, shredding those proteins that are severely misfolded while stabilizing and protecting proteins present in their native state. Isolation of native DegP complexes with folded outer membrane proteins (OMPs) highlights the importance of DegP in OMP biogenesis. The encapsulated OMP beta-barrel is significantly stabilized in the hydrophobic chamber of DegP12/24 and thus DegP seems to employ a reciprocal mechanism to those chaperones assisting the folding of water soluble proteins via polar interactions. In addition, we discuss in this review similarities to other complex proteolytic machines that, like DegP, are under control of a substrate-induced or stress-induced oligomer conversion.
DegP 的结构-功能分析揭示了一种蛋白酶和伴侣蛋白调控的新机制。未折叠蛋白的结合诱导从静止六聚体（DegP6）重新组装成功能性蛋白酶-伴侣 DegP12/24。新形成的笼具有蛋白水解折叠腔的特征，可降解严重错误折叠的蛋白，同时稳定和保护其天然状态的蛋白。与折叠的外膜蛋白 (OMP) 分离的天然 DegP 复合物突出了 DegP 在 OMP 生物发生中的重要性。包封的 OMP β-桶在外膜蛋白 DegP12/24 的疏水性腔内得到显著稳定，因此 DegP 似乎采用了一种与那些通过极性相互作用辅助水溶性蛋白折叠的伴侣蛋白相反的机制。此外，我们在这篇综述中讨论了与其他复杂蛋白水解机器的相似之处，这些机器与 DegP 一样，受到底物诱导或应激诱导的寡聚转换的控制。
