Bioluminescence Assay for the Human Chaperone MRJ Facilitated Refolding of Luciferase in Vitro

Compared with the exactly accompHshed Human Genome Project, the Functional Genome Plan is even more arduous and complex. The folding of polypeptide, as well as the assembling and disassembling of oligomeric protein complex, are the hinge steps from which the newly translated proteins transformed to their functional conformation. How these are accomplished constitutes a central problem in biology. Because the unfolded proteins can reach their native state spontaneously in vitro, it had been assumed that the folding and the assembling of newly synthesized polypeptides in vivo can occur spontaneously without the catalysis and the input of metabolic energy. This Long-held view has been revised in recent years owing to the discovery that in the cells the correct folding of many proteins depends on the function of a pre-existing protein machinery—the molecular chaperones (Hartl, F. U., 1996). In the presence of ATP, the chaperones worked in coordination and assisted the nascent polypeptide chains to fold up into steric structures. The correct destiny of new proteins was then guaranted (Frydman, J. and Hartl, F. u., 1996). So, the chaperone study is a zealous topic in Post-Genome era.