Cotranslational folding of proteins.
Many unfolded polypeptides are capable of refolding into their native structure upon the removal of the denaturant. However, the folding of the mature protein during renaturation does not accurately reflect the folding process of nascent proteins in the interior of the cell. This view resulted from the discovery of molecular chaperones known to modulate protein folding. Recent publications discussing the possible role and mechanisms of chaperone action suggest that folding in vivo may be a posttranslational process. Here we discuss data that indicate the final native structure and biological activity can be attainted can be nascent protein on the ribosome, thus supporting the cotranslational folding hypothesis.
Kolb
V A
VA
Institute of Protein Research, Academy of Sciences of Russia, Moscow Region, Russia.
Makeyev
E V
EV
Kommer
A
A
Spirin
A S
AS
D005914:Globins / Q000235:genetics; D008156:Luciferases / Q000235:genetics; D018832:Molecular Chaperones / Q000502:physiology; D014176:Protein Biosynthesis; D017510:Protein Folding
D018832:Molecular Chaperones; D005914:Globins; D008156:Luciferases