Literature DB >> 1732228

Suppression of oxidative envelope damage by pseudoreversion of a superoxide dismutase-deficient mutant of Escherichia coli.

J A Imlay1, I Fridovich.   

Abstract

Mutants of Escherichia coli that are devoid of superoxide dismutase (SOD) fail to grow in aerobic minimal medium. This is largely because of the O2- sensitivities of several amino acid biosynthetic pathways, since amino acid supplements can restore growth, albeit at a slow rate. We now report that growth in amino acid-supplemented medium can be further stimulated by the presence of extracellular osmolytes. Osmolytes also partially suppress the amino acid requirements of the SOD mutant. These data suggest that the combination of oxidative injury and turgor pressure permeabilizes the cell envelope and that critical metabolites, including the limiting products of damaged biosynthetic pathways, escape from the cell. External osmolytes may offer protection by countervailing the usual turgor pressure and thus stabilizing the damaged envelope. This model is consistent with the previous observation that deficiency of cell wall components is lethal to SOD mutants. A pseudorevertant that can grow at a moderate rate in normosmotic medium without amino acid supplementation has been obtained (J. A. Imlay and I. Fridovich, Mol. Gen. Genet. 228:410-416, 1991). Analysis suggests that the suppressor mutation allows the envelope either to resist or to tolerate oxidative lesions. Study of the pseudorevertant may illuminate the molecular basis of this oxidative envelope injury.

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Year:  1992        PMID: 1732228      PMCID: PMC206175          DOI: 10.1128/jb.174.3.953-961.1992

Source DB:  PubMed          Journal:  J Bacteriol        ISSN: 0021-9193            Impact factor:   3.490


  37 in total

1.  A yeast mutant lacking mitochondrial manganese-superoxide dismutase is hypersensitive to oxygen.

Authors:  A P van Loon; B Pesold-Hurt; G Schatz
Journal:  Proc Natl Acad Sci U S A       Date:  1986-06       Impact factor: 11.205

2.  Characterization of the Bacillus stearothermophilus manganese superoxide dismutase gene and its ability to complement copper/zinc superoxide dismutase deficiency in Saccharomyces cerevisiae.

Authors:  C Bowler; L Van Kaer; W Van Camp; M Van Montagu; D Inzé; P Dhaese
Journal:  J Bacteriol       Date:  1990-03       Impact factor: 3.490

3.  Chemistry of dioxygen.

Authors:  M J Green; H A Hill
Journal:  Methods Enzymol       Date:  1984       Impact factor: 1.600

4.  Human copper-zinc superoxide dismutase complements superoxide dismutase-deficient Escherichia coli mutants.

Authors:  D O Natvig; K Imlay; D Touati; R A Hallewell
Journal:  J Biol Chem       Date:  1987-10-25       Impact factor: 5.157

5.  Normal growth and division of Escherichia coli with a reduced amount of murein.

Authors:  R Prats; M A de Pedro
Journal:  J Bacteriol       Date:  1989-07       Impact factor: 3.490

6.  Null mutation of copper/zinc superoxide dismutase in Drosophila confers hypersensitivity to paraquat and reduced longevity.

Authors:  J P Phillips; S D Campbell; D Michaud; M Charbonneau; A J Hilliker
Journal:  Proc Natl Acad Sci U S A       Date:  1989-04       Impact factor: 11.205

7.  Cloned manganese superoxide dismutase reduces oxidative stress in Escherichia coli and Anacystis nidulans.

Authors:  M Y Gruber; B R Glick; J E Thompson
Journal:  Proc Natl Acad Sci U S A       Date:  1990-04       Impact factor: 11.205

Review 8.  The measurement and mechanism of lipid peroxidation in biological systems.

Authors:  J M Gutteridge; B Halliwell
Journal:  Trends Biochem Sci       Date:  1990-04       Impact factor: 13.807

9.  Oxyradical reactions: from bond-dissociation energies to reduction potentials.

Authors:  W H Koppenol
Journal:  FEBS Lett       Date:  1990-05-21       Impact factor: 4.124

10.  Glutathione in Escherichia coli is dispensable for resistance to H2O2 and gamma radiation.

Authors:  J T Greenberg; B Demple
Journal:  J Bacteriol       Date:  1986-11       Impact factor: 3.490

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  25 in total

1.  Role of superoxide dismutase activity in the physiology of Porphyromonas gingivalis.

Authors:  M C Lynch; H K Kuramitsu
Journal:  Infect Immun       Date:  1999-07       Impact factor: 3.441

Review 2.  Role of oxidants in microbial pathophysiology.

Authors:  R A Miller; B E Britigan
Journal:  Clin Microbiol Rev       Date:  1997-01       Impact factor: 26.132

3.  NADPH: ferredoxin oxidoreductase acts as a paraquat diaphorase and is a member of the soxRS regulon.

Authors:  S I Liochev; A Hausladen; W F Beyer; I Fridovich
Journal:  Proc Natl Acad Sci U S A       Date:  1994-02-15       Impact factor: 11.205

4.  An intracellular iron chelator pleiotropically suppresses enzymatic and growth defects of superoxide dismutase-deficient Escherichia coli.

Authors:  S Maringanti; J A Imlay
Journal:  J Bacteriol       Date:  1999-06       Impact factor: 3.490

5.  Pseudomonas aeruginosa sodA and sodB mutants defective in manganese- and iron-cofactored superoxide dismutase activity demonstrate the importance of the iron-cofactored form in aerobic metabolism.

Authors:  D J Hassett; H P Schweizer; D E Ohman
Journal:  J Bacteriol       Date:  1995-11       Impact factor: 3.490

6.  Superoxide poisons mononuclear iron enzymes by causing mismetallation.

Authors:  Mianzhi Gu; James A Imlay
Journal:  Mol Microbiol       Date:  2013-06-07       Impact factor: 3.501

7.  Escherichia coli produces linoleic acid during late stationary phase.

Authors:  H D Rabinowitch; D Sklan; D H Chace; R D Stevens; I Fridovich
Journal:  J Bacteriol       Date:  1993-09       Impact factor: 3.490

Review 8.  Simple biological systems for assessing the activity of superoxide dismutase mimics.

Authors:  Artak Tovmasyan; Julio S Reboucas; Ludmil Benov
Journal:  Antioxid Redox Signal       Date:  2013-10-19       Impact factor: 8.401

9.  Rapid viability loss on exposure to air in a superoxide dismutase-deficient mutant of Porphyromonas gingivalis.

Authors:  K Nakayama
Journal:  J Bacteriol       Date:  1994-04       Impact factor: 3.490

10.  Increased isolevuglandin-modified proteins in glaucomatous astrocytes.

Authors:  Bharathi Govindarajan; Anna Junk; Mabel Algeciras; Robert G Salomon; Sanjoy K Bhattacharya
Journal:  Mol Vis       Date:  2009-06-01       Impact factor: 2.367

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