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• W2018084833 startingPage "2096" @default.
• W2018084833 abstract "The folding of many proteins including luciferase in vivo requires the assistance of molecular chaperone proteins. To understand how a chaperone targets luciferase, we took three luciferases that give different bioluminescence with the same luciferin substrate and with differences in homology. The three luciferase genes, firefly luciferase (FF-Luc) (from Pyrocoelia miyako), and red (RE-Luc) and green (GR-Luc) bioluminescence-emitting luciferases (from Phrixothrix railroad-worms), were expressed in Escherichia coli to produce fusion proteins with predicted molecular masses. Subsequently, we observed that DnaK and GroEL were co-purified along with recombinant luciferase. Although the amount of co-purified DnaK was almost the same compared to FF-Luc, GroEL was 25 and 32 times higher in GR-Luc and RE-Luc respectively. Furthermore, co-expression of GroEL/GroES along with luciferase substantially refolded RE-Luc and GR-Luc compared to FF-Luc." @default.
• W2018084833 created "2016-06-24" @default.
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• W2018084833 date "2004-01-01" @default.
• W2018084833 modified "2023-09-23" @default.
• W2018084833 title "GroEL Chaperone Binding to Beetle Luciferases and the Implications for Refolding When Co-expressed" @default.
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• W2018084833 doi "https://doi.org/10.1271/bbb.68.2096" @default.
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