Chaperonin assisted polypeptide folding and assembly: implications for the production of functional proteins in bacteria.
Production of biologically active foreign proteins with correct three-dimensional structures is often difficult in bacteria. Recent advances demonstrate that, for some proteins at least, their correct folding and assembly is facilitated by a class of proteins known as molecular chaperones. An understanding of the function of molecular chaperones may assist in the synthesis in bacteria of functional foreign proteins produced by recombinant techniques.
Central Research & Development Department, E. I. Du Pont de Nemours & Co., Experimental Station, Wilmington, DE 19880-0402.
A A
AA
Gatenby
P V
PV
Viitanen
G H
GH
Lorimer
D001419:Bacteria / Q000378:metabolism*; D001426:Bacterial Proteins / Q000494:pharmacology*; D001709:Biotechnology; D018833:Chaperonins; D004926:Escherichia coli / Q000378:metabolism; D046911:Macromolecular Substances; D014176:Protein Biosynthesis; D011487:Protein Conformation / Q000187:drug effects; D011506:Proteins / Q000494:pharmacology*; D012273:Ribulose-Bisphosphate Carboxylase / Q000096:biosynthesis
D001426:Bacterial Proteins; D046911:Macromolecular Substances; D011506:Proteins; D018833:Chaperonins; D012273:Ribulose-Bisphosphate Carboxylase