A set of specified protein

the molecular chaperones

could bind with other proteins which are not in native state and could promote them to achieve their functional conformations.MRJ (Mouse Related J-protein) is a kind of newly discovered chaperones and is the homologue of humandnaJ.By using denatured luci ferase as a molecular model to study the protein refolding and renaturation processes

the authors incubated the denatured luciferase with three kinds of chaper ones:MRJ

Hsp60

Hsp70

and their different combinations

respectively.Then

the bioluminescence from luciferin-ATP-Mg system

which catalyzed by differe nt ly treated luciferase

was measured.The results showed that all these chaperone s

MRJ

Hsp60 and Hap70

could somewhat increase the luminescence from the systems.But only the combination of these three chaperones did have the most signifi cant and most stable effects.The authors also found the whole processes were ob viously ATP-dependent.From the experiment the author concluded that (1) As a molecular chaperone

MRJ could facilitate the refolding of denatured luciferase; (2) Luminescence assay was a sensitive

accurate and quick method for the chape rone studies.