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. 1974 Mar;117(3):954–959. doi: 10.1128/jb.117.3.954-959.1974

Proteins of the Inner Membrane of Escherichia coli: Changes in Composition Associated with Anaerobic Growth and Fumarate Reductase Amber Mutation

Margaret E Spencer a,1, J R Guest a
PMCID: PMC246571  PMID: 4591961

Abstract

The inner membrane fractions of Escherichia coli grown anaerobically and aerobically were isolated, and their proteins were compared by electrophoresis in polyacrylamide gels. To maximimize the differences between the preparations, the anaerobic cultures were grown on complex medium with added glucose, but glucose was omitted from the aerobic cultures to prevent catabolite repression. The pattern of bands in the two types of preparation differed considerably, and changes in approximately 20 components were observed. In particular, the band identified as succinate dehydrogenase in aerobic preparations was greatly reduced in anaerobic preparations. Mutants lacking fumarate reductase were isolated, and inner membrane preparations of an frd amber mutant were deficient in a major component of 75,000 daltons and possibly a minor one of 87,500 daltons. The former was also present in greater amounts in anaerobic preparations and could represent a fumarate reductase subunit.

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Selected References

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

  1. Faust P. J., Vandemark P. J. Phosphorylation coupled to NADH oxidation with fumarate in Streptococcus faecalis 10Cl. Arch Biochem Biophys. 1970 Apr;137(2):392–398. doi: 10.1016/0003-9861(70)90454-6. [DOI] [PubMed] [Google Scholar]
  2. Gray C. T., Wimpenny J. W., Hughes D. E., Mossman M. R. Regulation of metabolism in facultative bacteria. I. Structural and functional changes in Escherichia coli associated with shifts between the aerobic and anaerobic states. Biochim Biophys Acta. 1966 Mar 28;117(1):22–32. doi: 10.1016/0304-4165(66)90148-6. [DOI] [PubMed] [Google Scholar]
  3. HIRSCH C. A., RASMINSKY M., DAVIS B. D., LIN E. C. A FUMARATE REDUCTASE IN ESCHERICHIA COLI DISTINCT FROM SUCCINATE DEHYDROGENASE. J Biol Chem. 1963 Nov;238:3770–3774. [PubMed] [Google Scholar]
  4. Herbert A. A., Guest J. R. Biochemical and genetic studies with lysine+methionine mutants of Escherichia coli: lipoic acid and alpha-ketoglutarate dehydrogenase-less mutants. J Gen Microbiol. 1968 Oct;53(3):363–381. doi: 10.1099/00221287-53-3-363. [DOI] [PubMed] [Google Scholar]
  5. Holland I. B., Tuckett S. Study of envelope proteins in E. coli cet and recA mutants by SDS acrylamide gel electrophoresis. J Supramol Struct. 1972;1(2):77–97. doi: 10.1002/jss.400010202. [DOI] [PubMed] [Google Scholar]
  6. Inouye M., Pardee A. B. Changes of membrane proteins and their relation to deoxyribonucleic acid synthesis and cell division of Escherichia coli. J Biol Chem. 1970 Nov 10;245(21):5813–5819. [PubMed] [Google Scholar]
  7. Kröger A., Dadák V. On the role of quinones in bacterial electron transport. The respiratory system of Bacillus megaterium. Eur J Biochem. 1969 Dec;11(2):328–340. doi: 10.1111/j.1432-1033.1969.tb00776.x. [DOI] [PubMed] [Google Scholar]
  8. Kung H. F., Henning U. Limiting availability of binding sites for dehydrogenases on the cell membrane of Escherichia coli. Proc Natl Acad Sci U S A. 1972 Apr;69(4):925–929. doi: 10.1073/pnas.69.4.925. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. MAGASANIK B. Catabolite repression. Cold Spring Harb Symp Quant Biol. 1961;26:249–256. doi: 10.1101/sqb.1961.026.01.031. [DOI] [PubMed] [Google Scholar]
  10. MacGregor C. H., Schnaitman C. A. Alterations in the cytoplasmic membrane proteins of various chlorate-resistant mutants of Escherichia coli. J Bacteriol. 1971 Oct;108(1):564–570. doi: 10.1128/jb.108.1.564-570.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. MacGregor C. H., Schnaitman C. A. Reconstitution of nitrate reductase activity and formation of membrane particles from cytoplasmic extracts of chlorate-resistant mutants of Escherichia coli. J Bacteriol. 1973 Jun;114(3):1164–1176. doi: 10.1128/jb.114.3.1164-1176.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Miki K., Lin E. C. Enzyme complex which couples glycerol-3-phosphate dehydrogenation to fumarate reduction in Escherichia coli. J Bacteriol. 1973 May;114(2):767–771. doi: 10.1128/jb.114.2.767-771.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Rolfe B., Onodera K. Genes, enzymes and membrane proteins of the nitrate respiration system of Escherichia coli. J Membr Biol. 1972;9(2):195–207. [PubMed] [Google Scholar]
  14. Schnaitman C. A. Examination of the protein composition of the cell envelope of Escherichia coli by polyacrylamide gel electrophoresis. J Bacteriol. 1970 Nov;104(2):882–889. doi: 10.1128/jb.104.2.882-889.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Shapiro B. M., Siccardi A. G., Hirota Y., Jacob F. On the process of cellular division in Escherichia coli. Membrane prtein alterations associated with mutations affecting the initiation of DNA synthesis. J Mol Biol. 1970 Aug 28;52(1):75–89. doi: 10.1016/0022-2836(70)90178-6. [DOI] [PubMed] [Google Scholar]
  16. Showe M. K., DeMoss J. A. Localization and regulation of synthesis of nitrate reductase in Escherichia coli. J Bacteriol. 1968 Apr;95(4):1305–1313. doi: 10.1128/jb.95.4.1305-1313.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Spencer M. E., Guest J. R. Isolation and properties of fumarate reductase mutants of Escherichia coli. J Bacteriol. 1973 May;114(2):563–570. doi: 10.1128/jb.114.2.563-570.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Spencer M. E., Guest J. R. Proteins of the inner membrane of Escherichia coli: identification of succinate dehydrogenase by polyacrylamide gel electrophoresis with sdh amber mutants. J Bacteriol. 1974 Mar;117(3):947–953. doi: 10.1128/jb.117.3.947-953.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. de Vries W., van Wyck-Kapteyn W. M., Stouthamer A. H. Generation of ATP during cytochrome-linked anaerobic electron transport in propionic acid bacteria. J Gen Microbiol. 1973 May;76(1):31–41. doi: 10.1099/00221287-76-1-31. [DOI] [PubMed] [Google Scholar]

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