Chaperonins dependent increase of Cu,Zn superoxide dismutase production in Escherichia coli.
Over-expression of the chaperonins GroEL and GroES significantly suppressed the temperature-dependent pattern of expression of Cu,Zn superoxide dismutases in Escherichia coli and increased the yield of active enzyme. The results obtained indicate that chaperonins prevent degradation of metal-deficient enzyme molecules. GroEL was shown to form a complex with unfolded Cu,Zn superoxide dismutase in vitro, confirming that GroEL can interact with beta-stranded proteins.
Battistoni
A
A
Department of Biology, University of Rome Tor Vergata, Italy.
Carri
M T
MT
Steinkühler
C
C
Rotilio
G
G
D000818:Animals; D001426:Bacterial Proteins / Q000378:metabolism; D002417:Cattle; D018835:Chaperonin 10; D018834:Chaperonin 60; D018833:Chaperonins; D004926:Escherichia coli / Q000201:enzymology*; D015870:Gene Expression; D006360:Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D008670:Metals / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D013482:Superoxide Dismutase / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism; D014982:Xenopus laevis
D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D008670:Metals; D011506:Proteins; D013482:Superoxide Dismutase; D018833:Chaperonins