Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1976 Oct;128(1):248–256. doi: 10.1128/jb.128.1.248-256.1976

Properties of Escherichia coli mutants with alterations in Mg2+-adenosine triphosphatase.

L W Adler, B P Rosen
PMCID: PMC232850  PMID: 135756

Abstract

A mutant Escherichia coli, selected for resistance to the antibiotic neomycin, was unable to utilize nonfermentable carbon sources for growth. Two strains were selected from this mutant on the basis of their ability to grow utilizing succinate as a carbon source. All three strains had approximately equal amounts of the Mg2+-adenosine triphosphatase (ATPase) (EC 3.6.1.3) protein, but the activity of the enzyme differed in each strain. The Mg2+-ATPase from each of the three strains lost activity upon solubilization and appeared to undergo rapid dissociation once solubilized. This dissociation is similar to that described for the wild type after cold exposure.

Full text

PDF
251

Images in this article

253Image
on p.253
254Image
on p.254
256Image
on p.256

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Butlin J. D., Cox G. B., Gibson F. Oxidative phosphorylation in Escherichia coli K12. Mutations affecting magnesium ion- or calcium ion-stimulated adenosine triphosphatase. Biochem J. 1971 Aug;124(1):75–81. doi: 10.1042/bj1240075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. GLANSDORFF N. TOPOGRAPHY OF COTRANSDUCIBLE ARGININE MUTATIONS IN ESCHERICHIA COLI K-12. Genetics. 1965 Feb;51:167–179. doi: 10.1093/genetics/51.2.167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. HAYASHI S., KOCH J. P., LIN E. C. ACTIVE TRANSPORT OF L-ALPHA-GLYCEROPHOSPHATE IN ESCHERICHIA COLI. J Biol Chem. 1964 Sep;239:3098–3105. [PubMed] [Google Scholar]
  4. Kanner B. I., Gutnick D. L. Use of neomycin in the isolation of mutants blocked in energy conservation in Escherichia coli. J Bacteriol. 1972 Jul;111(1):287–289. doi: 10.1128/jb.111.1.287-289.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kobayashi H., Anraku Y. Membrane-bound adenosine triphosphatase of Escherichia coli. I. Partial purification and properties. J Biochem. 1972 Mar;71(3):387–399. [PubMed] [Google Scholar]
  6. LAURELL C. B. ANTIGEN-ANTIBODY CROSSED ELECTROPHORESIS. Anal Biochem. 1965 Feb;10:358–361. doi: 10.1016/0003-2697(65)90278-2. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Roisin M. P., Kepes A. The membrane ATPase of Escherichia coli. I. Release into solution, allotopic properties and reconstitution of membrane-bound ATPase. Biochim Biophys Acta. 1973 May 30;305(2):249–259. doi: 10.1016/0005-2728(73)90173-4. [DOI] [PubMed] [Google Scholar]
  9. Rosen B. P., Adler L. W. The maintenance of the energized membrane state and its relation to active transport in Escherichia coli. Biochim Biophys Acta. 1975 Apr 14;387(1):23–36. doi: 10.1016/0005-2728(75)90049-3. [DOI] [PubMed] [Google Scholar]
  10. Rosen B. P. Restoration of active transport in an Mg2+-adenosine triphosphatase-deficient mutant of Escherichia coli. J Bacteriol. 1973 Dec;116(3):1124–1129. doi: 10.1128/jb.116.3.1124-1129.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Schairer H. U., Haddock B. A. -Galactoside accumulation in a Mg 2+ -,Ca 2+ -activated ATPase deficient mutant of E.coli. Biochem Biophys Res Commun. 1972 Aug 7;48(3):544–551. doi: 10.1016/0006-291x(72)90382-8. [DOI] [PubMed] [Google Scholar]
  12. Simoni R. D., Postma P. W. The energetics of bacterial active transport. Annu Rev Biochem. 1975;44:523–554. doi: 10.1146/annurev.bi.44.070175.002515. [DOI] [PubMed] [Google Scholar]
  13. Simoni R. D., Shallenberger M. K. Coupling of energy to active transport of amino acids in Escherichia coli. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2663–2667. doi: 10.1073/pnas.69.9.2663. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Tanaka S., Lerner S. A., Lin E. C. Replacement of a phosphoenolpyruvate-dependent phosphotransferase by a nicotinamide adenine dinucleotide-linked dehydrogenase for the utilization of mannitol. J Bacteriol. 1967 Feb;93(2):642–648. doi: 10.1128/jb.93.2.642-648.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Tsuchiya T., Rosen B. P. Energy transduction in Escherichia coli. The role of the Mg2+ATPase. J Biol Chem. 1975 Nov 10;250(21):8409–8415. [PubMed] [Google Scholar]
  16. Turnock G., Erickson S. K., Ackrell B. A., Birch B. A mutant of Escherichia coli with a defect in energy metabolism. J Gen Microbiol. 1972 May;70(3):507–515. doi: 10.1099/00221287-70-3-507. [DOI] [PubMed] [Google Scholar]
  17. Yamamoto T. H., Mével-Ninio M., Valentine R. C. Essential role of membrane ATPase or coupling factor for anaerobic growth and anaerobic active transport in Escherichia coli. Biochim Biophys Acta. 1973 Sep 26;314(3):267–275. doi: 10.1016/0005-2728(73)90111-4. [DOI] [PubMed] [Google Scholar]
  18. van Thienen G., Postma P. W. Coupling between energy conservation and active transport of serine in Escherichia coli. Biochim Biophys Acta. 1973 Oct 25;323(3):429–440. doi: 10.1016/0005-2736(73)90188-0. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES