毒理学相关资料,第四章内容参考文献24.docVIP

Top of Form Nature ? 1996 Macmillan Magazines Ltd. Volume 381(6583)? ? ? ? ? ? ?13 June 1996? ? ? ? ? ? ?pp 571-580 Molecular chaperones in cellular protein folding [REVIEW ARTICLE] Hartl, F. Ulrich F. Ulrich Hartl is in the Howard Hughes Medical Institute and Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, New York 10021, USA. Outline Abstract Origins of the chaperone concept Folding in vitro versus folding in vivo (1) Molecular crowding and protein aggregation. (2) Folding and translation. The Hsp70 chaperone system Structure of Hsp70 and DnaJ. Peptide binding. The Hsp70 reaction cycle in protein folding. Function under stress conditions. Protein translocation across membranes. The chaperonin system GroEL and GroES structure. Polypeptide binding. The chaperonin cycle in folding. Folding in the GroEL cage. Chaperonin specificity: GroEL versus TRiC. Cellular protein folding pathways Bacterial cytosol and mitochondrial matrix: homologous folding compartments. Folding in the eukaryotic cytosol. Perspectives REFERENCES Graphics Table 1 Figure 1 Figure 5 Figure 2 Figure 3 Figure 4 Figure 6 Abstract The folding of many newly synthesized proteins in the cell depends on a set of conserved proteins known as molecular chaperones. These prevent the formation of misfolded protein structures, both under normal conditions and when cells are exposed to stresses such as high temperature. Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.  PROTEIN folding is the process by which the linear information contained in the amino-acid sequence of a polypeptide gives rise to the well-defined three-dimensional conformation of the functional protein. How this is accomplished constitutes a central problem in biology. Because unfolded proteins can reach their