-transparent.png){kind=logo}
The iron superoxide dismutase (FeSOD) gene of Escherichia coli was cloned in Saccharomyces cerevisiae cells deficient in copper,zinc superoxide dismutase (Cu,ZnSOD). FeSOD replaced Cu,ZnSOD in protecting the yeast cells against oxidative stress. In the recombinant strains the FeSOD gene, which was under the transcriptional control of the yeast phosphoglycerate kinase gene promoter, was functionally expressed at two different levels on episomal and centromeric plasmids. Despite suppression of methionine and lysine auxotrophy, the higher level of FeSOD activity was more beneficial to growth of the mutant yeast cells only when these were exposed to higher levels of oxidative stress induced by paraquat or 100% oxygen. In the presence of paraquat, there was a novel stimulation of FeSOD activity. This was associated with a marked increase in catalase activity, and a decrease in glutathione reductase activity.
D R Agius, and
W H Bannister, and
R Balzan
September 2009,
PloS one,
D R Agius, and
W H Bannister, and
R Balzan
May 2021,
Pesticide biochemistry and physiology,
D R Agius, and
W H Bannister, and
R Balzan
November 1992,
Proceedings of the National Academy of Sciences of the United States of America,
D R Agius, and
W H Bannister, and
R Balzan
May 1995,
Proceedings of the National Academy of Sciences of the United States of America,
D R Agius, and
W H Bannister, and
R Balzan
June 2011,
Free radical biology & medicine,
D R Agius, and
W H Bannister, and
R Balzan
November 1996,
The Journal of biological chemistry,
D R Agius, and
W H Bannister, and
R Balzan
January 2022,
Frontiers in plant science,
D R Agius, and
W H Bannister, and
R Balzan
August 2003,
The Biochemical journal,
D R Agius, and
W H Bannister, and
R Balzan
June 1999,
Yeast (Chichester, England),
D R Agius, and
W H Bannister, and
R Balzan
September 1993,
Proceedings of the National Academy of Sciences of the United States of America,
