DnaK、DnaJ和GroEL在伴侣蛋白介导的蛋白质折叠途径中的连续作用。
Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding.
作者信息
Langer T, Lu C, Echols H, Flanagan J, Hayer M K, Hartl F U
机构信息
Rockefeller Research Laboratories, Sloan-Kettering Institute, New York, New York 10021.
出版信息
Nature. 1992 Apr 23;356(6371):683-9. doi: 10.1038/356683a0.
The main stress proteins of Escherichia coli function in an ordered protein-folding reaction. DnaK (heat-shock protein 70) recognizes the folding polypeptide as an extended chain and cooperates with DnaJ in stabilizing an intermediate conformational state lacking ordered tertiary structure. Dependent on GrpE and ATP hydrolysis, the protein is then transferred to GroEL (heat-shock protein 60) which acts catalytically in the production of the native state. This sequential mechanism of chaperone action may represent an important pathway for the folding of newly synthesized polypeptides.
大肠杆菌的主要应激蛋白在有序的蛋白质折叠反应中发挥作用。DnaK（热休克蛋白70）将折叠中的多肽识别为伸展链，并与DnaJ协同作用，以稳定缺乏有序三级结构的中间构象状态。然后，依赖于GrpE和ATP水解，该蛋白被转移至GroEL（热休克蛋白60），后者在天然状态的产生中起催化作用。伴侣蛋白作用的这种顺序机制可能代表了新合成多肽折叠的一条重要途径。
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