The emergence of the chaperone machines.
To ensure proper polypeptide folding, oligomerization and transport, elaborate molecular 'chaperone machines' have evolved. These machines are usually composed of a major chaperone protein that binds promiscuously to nascent, unfolded, misfolded or aggregated polypeptides and a set of chaperone 'cohorts', whose function is to enhance efficiency and ensure recycling. These chaperone machines can function by themselves or synergistically to carry out their various tasks.
Georgopoulos
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Département de Biochimie Médicale, Centre Médical Universitaire, Geneve, Switzerland.
D001426:Bacterial Proteins / Q000378:metabolism; D018833:Chaperonins; D006360:Heat-Shock Proteins / Q000378:metabolism; D006706:Homeostasis / Q000235:genetics; D017510:Protein Folding; D011499:Protein Processing, Post-Translational; D011506:Proteins
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D011506:Proteins; C057842:SecB protein, Bacteria; D018833:Chaperonins