title: Chaperonins dependent increase of Cu,Zn superoxide dismutase production in Escherichia coli.
abstract: 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.
authors.affiliation: Department of Biology, University of Rome Tor Vergata, Italy.
authors.forename: A
authors.initials: A
authors.lastname: Battistoni
authors.forename: M T
authors.initials: MT
authors.lastname: Carri
authors.forename: C
authors.initials: C
authors.lastname: Steinkühler
authors.forename: G
authors.initials: G
authors.lastname: Rotilio
mesh_terms: 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
chemical_list: D001426:Bacterial Proteins; D018835:Chaperonin 10; D018834:Chaperonin 60; D006360:Heat-Shock Proteins; D008670:Metals; D011506:Proteins; D013482:Superoxide Dismutase; D018833:Chaperonins