Activity of chloramphenicol acetyltransferase overproduced in E. coli with wild-type and mutant GroEL.
The homo-oligomeric protein chloramphenicol acetyltransferase (CAT) has previously been shown to interact with a chaperone GroEL in vitro, suggesting a possible involvement of GroEL in CAT assembly. CAT was overproduced to various levels in the presence and absence of GroEL overproduction, and in groEL mutants. CAT was accumulated to 9-45% of total cellular protein in a fully soluble form, without formation of inclusion bodies. In all cases, even with groEL mutants, CAT specific activity was shown proportional to the amount of protein produced, indicating the formation of active trimer CAT structure does not need GroEL in Escherichia coli.
Kim
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HB
Department of Life Science, Korea Advanced Institute of Science and Technology, Taejon.
Kang
C
C
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D018834:Chaperonin 60; D015500:Chloramphenicol O-Acetyltransferase / Q000096:biosynthesis / Q000378:metabolism*; D003470:Culture Media; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D006360:Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006358:Hot Temperature; D009154:Mutation; D010957:Plasmids / Q000235:genetics
D001426:Bacterial Proteins; D018834:Chaperonin 60; D003470:Culture Media; D006360:Heat-Shock Proteins; D015500:Chloramphenicol O-Acetyltransferase