Motojima Fumihiro, Yoshida Masasuke
Department of Molecular Bioscience, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto, 603-8555, Japan.
Biochem Biophys Res Commun. 2015 Oct 9;466(1):72-5. doi: 10.1016/j.bbrc.2015.08.108. Epub 2015 Aug 29.
Many proteins in bacterial cells fold in the chaperonin cage made of the central cavity of GroEL capped by GroES. Recent studies indicate that the polypeptide in the cage spends the most time as a state tethered dynamically to the GroEL/GroES interface region, in which folding occurs in the polypeptide segments away from the tethered site (F. Motojima & M. Yoshida, EMBO J. (2010) 29, 4008-4019). In support of this, we show here that a polypeptide in the cage tethered covalently to an appropriate site in the GroEL/GroES interface region can fold to a near-native structure.
细菌细胞中的许多蛋白质在由GroEL中央腔室构成并由GroES封闭的伴侣蛋白笼中折叠。最近的研究表明，笼中的多肽大部分时间处于动态连接到GroEL/GroES界面区域的状态，在该状态下，多肽链段在远离连接位点的区域发生折叠（F. Motojima和M. Yoshida，《欧洲分子生物学组织杂志》（2010年）29卷，4008 - 4019页）。作为对此的支持，我们在此表明，笼中与GroEL/GroES界面区域中适当位点共价连接的多肽能够折叠成接近天然的结构。
