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.
Département de Biochimie Médicale, Centre Médical Universitaire, Geneve, Switzerland.
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Georgopoulos
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