Abstract
Several mutants of Escherichia coli K-12 defective in aerobic metabolism were isolated. One such mutant was found to be deficient in cytochromes, heme, and catalase. Aerobically grown cells did not consume oxygen and could grow only on fermentable carbon sources. Supplementation of the growth medium with delta-aminolevulonic acid, protoporphyrin IX, or hemin did not restore aerobic metabolism. The lack of heme and catalase in mutant cells grown on glucose was not due to catabolite repression, since the addition of exogenous cyclic AMP did not restore the normal phenotype. When grown aerobically on complex medium containing glucose, the mutant produced lactic acid as the principal fermentation product. This pleotropic mutation was attributed to an inability of the cells to synthesize heme, and preliminary data mapped the mutation to between 8 and 13 min on the E. coli genome.
Full text
PDF





Images in this article
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- BEERS R. F., Jr, SIZER I. W. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem. 1952 Mar;195(1):133–140. [PubMed] [Google Scholar]
- Bachmann B. J. Linkage map of Escherichia coli K-12, edition 7. Microbiol Rev. 1983 Jun;47(2):180–230. doi: 10.1128/mr.47.2.180-230.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem. 1971 Nov;44(1):276–287. doi: 10.1016/0003-2697(71)90370-8. [DOI] [PubMed] [Google Scholar]
- Bremer E., Silhavy T. J., Weinstock G. M. Transposable lambda placMu bacteriophages for creating lacZ operon fusions and kanamycin resistance insertions in Escherichia coli. J Bacteriol. 1985 Jun;162(3):1092–1099. doi: 10.1128/jb.162.3.1092-1099.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Broman R. L., Dobrogosz W. J. Stimulation of cytochrome synthesis in Escherichia coli by cyclic AMP. Arch Biochem Biophys. 1974 Jun;162(2):595–601. doi: 10.1016/0003-9861(74)90220-3. [DOI] [PubMed] [Google Scholar]
- Carlioz A., Touati D. Isolation of superoxide dismutase mutants in Escherichia coli: is superoxide dismutase necessary for aerobic life? EMBO J. 1986 Mar;5(3):623–630. doi: 10.1002/j.1460-2075.1986.tb04256.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Christman M. F., Morgan R. W., Jacobson F. S., Ames B. N. Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell. 1985 Jul;41(3):753–762. doi: 10.1016/s0092-8674(85)80056-8. [DOI] [PubMed] [Google Scholar]
- Clare D. A., Duong M. N., Darr D., Archibald F., Fridovich I. Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase. Anal Biochem. 1984 Aug 1;140(2):532–537. doi: 10.1016/0003-2697(84)90204-5. [DOI] [PubMed] [Google Scholar]
- DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
- Haddock B. A. The reconstitution of oxidase activity in membranes derived from a 5-aminolaevulinic acid-requiring mutant of Escherichia coli. Biochem J. 1973 Dec;136(4):877–884. doi: 10.1042/bj1360877. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hassan H. M. Exacerbation of superoxide radical formation by paraquat. Methods Enzymol. 1984;105:523–532. doi: 10.1016/s0076-6879(84)05072-2. [DOI] [PubMed] [Google Scholar]
- Hassan H. M., Fridovich I. Enzymatic defenses against the toxicity of oxygen and of streptonigrin in Escherichia coli. J Bacteriol. 1977 Mar;129(3):1574–1583. doi: 10.1128/jb.129.3.1574-1583.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hassan H. M., Fridovich I. Physiological function of superoxide dismutase in glucose-limited chemostat cultures of Escherichia coli. J Bacteriol. 1977 May;130(2):805–811. doi: 10.1128/jb.130.2.805-811.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hassan H. M., Fridovich I. Regulation of the synthesis of catalase and peroxidase in Escherichia coli. J Biol Chem. 1978 Sep 25;253(18):6445–6420. [PubMed] [Google Scholar]
- Hassan H. M., Fridovich I. Superoxide, hydrogen peroxide, and oxygen tolerance of oxygen-sensitive mutants of Escherichia coli. Rev Infect Dis. 1979 Mar-Apr;1(2):357–369. doi: 10.1093/clinids/1.2.357. [DOI] [PubMed] [Google Scholar]
- Kono Y., Fridovich I. Isolation and characterization of the pseudocatalase of Lactobacillus plantarum. J Biol Chem. 1983 May 25;258(10):6015–6019. [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Loewen P. C., Switala J., Triggs-Raine B. L. Catalases HPI and HPII in Escherichia coli are induced independently. Arch Biochem Biophys. 1985 Nov 15;243(1):144–149. doi: 10.1016/0003-9861(85)90782-9. [DOI] [PubMed] [Google Scholar]
- Loewen P. C., Triggs B. L., George C. S., Hrabarchuk B. E. Genetic mapping of katG, a locus that affects synthesis of the bifunctional catalase-peroxidase hydroperoxidase I in Escherichia coli. J Bacteriol. 1985 May;162(2):661–667. doi: 10.1128/jb.162.2.661-667.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Low B. Rapid mapping of conditional and auxotrophic mutations in Escherichia coli K-12. J Bacteriol. 1973 Feb;113(2):798–812. doi: 10.1128/jb.113.2.798-812.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- McConville M. L., Charles H. P. Isolation of haemin-requiring mutants of Escherichia coli K12. J Gen Microbiol. 1979 Jul;113(1):155–164. doi: 10.1099/00221287-113-1-155. [DOI] [PubMed] [Google Scholar]
- McConville M. L., Charles H. P. Mutants of Escherichia coli K12 permeable to haemin. J Gen Microbiol. 1979 Jul;113(1):165–168. doi: 10.1099/00221287-113-1-165. [DOI] [PubMed] [Google Scholar]
- Moody C. S., Hassan H. M. Anaerobic biosynthesis of the manganese-containing superoxide dismutase in Escherichia coli. J Biol Chem. 1984 Oct 25;259(20):12821–12825. [PubMed] [Google Scholar]
- Poole R. K., Baines B. S., Appleby C. A. Haemoprotein b-590 (Escherichia coli), a reducible catalase and peroxidase: evidence for its close relationship to hydroperoxidase I and a 'cytochrome a1b' preparation. J Gen Microbiol. 1986 Jun;132(6):1525–1539. doi: 10.1099/00221287-132-6-1525. [DOI] [PubMed] [Google Scholar]
- Powell K. A., Cox R., McConville M., Charles H. P. Mutations affecting porphyrin biosynthesis in Escherichia coli. Enzyme. 1973;16(1):65–73. doi: 10.1159/000459363. [DOI] [PubMed] [Google Scholar]
- Săsărman A., Horodniceanu T. Locus determining normal colony formation on the chromosome of Escherichia coli K-12. J Bacteriol. 1967 Oct;94(4):1268–1269. doi: 10.1128/jb.94.4.1268-1269.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Wanner B. L. Novel regulatory mutants of the phosphate regulon in Escherichia coli K-12. J Mol Biol. 1986 Sep 5;191(1):39–58. doi: 10.1016/0022-2836(86)90421-3. [DOI] [PubMed] [Google Scholar]

