异质多亚基分子伴侣素研究进展

Hsp60 is also known as molecular chaperone, and molecular chaperone is divided into classes I and II. Class I is expressed in mitochondria and chloroplasts of prokaryotes and eukaryotes, and class II Hsp60 is mainly distributed in the cytoplasm of archaea and eukaryotes. Molecular chaperone is a kind of protein widely existed in biological body with high content. It can help large molecular proteins or denatured proteins fold correctly, play a role in stabilizing them and preventing protein denaturation. Studies have found that in eubacteria, archaea and eukaryotic cells, molecular chaperones with different structures form a complex folding system, through which proteins complete a biologically active three-dimensional conformation process. The addition of molecular chaperones in the process of protein expression can avoid protein misfolding, reduce the production of harmful substances and protein precipitation. In this paper, the structure and function of chaperones in chaperone families and polyunits are reviewed.