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Chaperon DnaK and ATP participate in the in vivo folding of firefly luciferase synthesized in E. coli cells



Chaperon DnaK and ATP participate in the in vivo folding of firefly luciferase synthesized in E. coli cells



Biochemistry 61(4): 524-527



The time courses of luciferase protein content and activity of Luciola mingrelica firefly luciferase synthesized from the pJG-lambda plasmid in E. coli strains OMEGA-238 (DnaK-deficient) and B178groE7 (GroEL-deficient) and the respective control strains OMEGA-237 and W3110 were studied. The luciferase protein contents synthesized in all strains were approximately equal (3.0-3.9% of total cell protein). Luciferase was synthesized in catalytically inactive form but was transformed into active enzyme during incubation at 21 degree C. In the DnaK-deficient E. coli strain OMEGA-238 the enzyme did not transform into the catalytically active form; this shows the participation of DnaK-chaperon in the transformation of newly synthesized luciferase into catalytically active form. The folding of luciferase was accelerated with increased ATP concentration inside the cell, which can achieved by treatment of the cells with polymyxin and addition of ATP into the medium.

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