Pathways of Protein Remodeling by Escherichia Coli Molecular Chaperones

摘要: A new concept in molecular biology that has evolved over the past ten years is proteins fold with assistance from other proteins, collectively referred to as chaperones. All organisms, bacteria humans, possess several classes of highly conserved chaperones, defined generally bind non-native conformations and facilitate correct folding native promote refolding. Extensive work shown function well structure chaperones are results obtained studies one organism usually applicable organisms (1–3). This review will focus on ATP-dependent chaperone systems Escherichia coli, including (i) DnaK, its co-chaperones, DnaJ GrpE, (ii) Clp (iii) GroEL co-chaperone, GroES (summarized Table 1).