Bochkareva E S, Girshovich A S
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
J Biol Chem. 1992 Dec 25;267(36):25672-5.
To facilitate folding and assembly of different proteins, chaperonin GroEL requires the presence of its helper protein GroES. Using a photochemical cross-linking approach, we show that GroES and newly synthesized pre-beta-lactamase (pre-beta lac) contact with each other only within the ternary complex with GroEL. Possibly owing to this contact GroES is able to directly influence the pre-beta lac/GroEL interaction. Furthermore, the cross-linking of pre-beta lac to GroES suggests that the binding of the protein ligands to GroEL occurs near the GroES binding site, known to be in the central hole space of GroEL.
为促进不同蛋白质的折叠和组装，伴侣蛋白GroEL需要其辅助蛋白GroES的存在。我们采用光化学交联方法表明，GroES与新合成的前β-内酰胺酶（pre-β lac）仅在与GroEL形成的三元复合物中相互接触。可能由于这种接触，GroES能够直接影响pre-β lac与GroEL的相互作用。此外，pre-β lac与GroES的交联表明，蛋白质配体与GroEL的结合发生在GroES结合位点附近，已知该位点位于GroEL的中心孔空间。
