Co-expression of GroEL/ES enhances the expression of plant catalase in bacterial cytosol.
Expression of plant proteins in E. coli is frequently unsuccessful, but soluble and functional rice catalase-B can be produced in E. coli when it is co-expressed with the chaperone GroEL/ES. The rice catalase exhibited properties typical for a catalase including the decomposition of H(2)O(2) and inhibition by aminotriazole, a specific inhibitor for plant and animal catalases. This achievement records for first time the successful expression of a both native and variant rice plant catalase in bacterial cytosol suggesting that it may be an option to be considered for the expression of other plant proteins in E. coli.
Mondal
Prosenjit
P
Stress Biology Laboratory, Gene Function and Regulation Group, Institute of Life Sciences, Nalco Square, Chandrasekharpur, Bhubaneswar-23, Orissa, India.
Ray
Mamata
M
Sahu
Sushmita
S
Sabat
Surendra Chandra
SC
D000640:Amitrole / Q000494:pharmacology; D000818:Animals; D002374:Catalase / Q000037:antagonists & inhibitors / Q000096:biosynthesis* / Q000737:chemistry / Q000235:genetics; D018835:Chaperonin 10 / Q000235:genetics*; D018834:Chaperonin 60 / Q000235:genetics*; D003600:Cytosol / Q000378:metabolism*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004926:Escherichia coli / Q000166:cytology* / Q000235:genetics*; D015870:Gene Expression; D012275:Oryza / Q000201:enzymology* / Q000235:genetics; D011994:Recombinant Proteins / Q000037:antagonists & inhibitors / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics; D012995:Solubility
D018835:Chaperonin 10; D018834:Chaperonin 60; D004791:Enzyme Inhibitors; D011994:Recombinant Proteins; D002374:Catalase; D000640:Amitrole