Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1976 Jul;127(1):498–504. doi: 10.1128/jb.127.1.498-504.1976

Genetic and physiological regulation of intrinsic proteins of the outer membrane of Salmonella typhimurium.

R L Bennett, L I Rothfield
PMCID: PMC233083  PMID: 776938

Abstract

Four major outer membrane polypeptides, accounting for approximately 20% of the total protein of the outer membrane of Salmonella typhimurium, were induced by growth in minimal medium. The polypeptides were tightly bound membrane components. Physiological and genetic evidence indicates that the four polypeptides fall in two separate regulation groups. Synthesis of one of these groups was coordinately regulated by the concentration of iron in the medium, and a mutant strain has been identified in which there is constitutive synthesis of this group of major outer membrane proteins.

Full text

PDF
498

Images in this article

Selected References

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

  1. Ames G. F. Resolution of bacterial proteins by polyacrylamide gel electrophoresis on slabs. Membrane, soluble, and periplasmic fractions. J Biol Chem. 1974 Jan 25;249(2):634–644. [PubMed] [Google Scholar]
  2. Carter P. Spectrophotometric determination of serum iron at the submicrogram level with a new reagent (ferrozine). Anal Biochem. 1971 Apr;40(2):450–458. doi: 10.1016/0003-2697(71)90405-2. [DOI] [PubMed] [Google Scholar]
  3. Di Masi D. R., White J. C., Schnaitman C. A., Bradbeer C. Transport of vitamin B12 in Escherichia coli: common receptor sites for vitamin B12 and the E colicins on the outer membrane of the cell envelope. J Bacteriol. 1973 Aug;115(2):506–513. doi: 10.1128/jb.115.2.506-513.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fox C. F., Law J. H., Tsukagoshi N., Wilson G. A density label for membranes. Proc Natl Acad Sci U S A. 1970 Oct;67(2):598–605. doi: 10.1073/pnas.67.2.598. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hantke K., Braun V. Membrane receptor dependent iron transport in Escherichia coli. FEBS Lett. 1975 Jan 1;49(3):301–305. doi: 10.1016/0014-5793(75)80771-x. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Lopes J., Gottfried S., Rothfield L. Leakage of periplasmic enzymes by mutants of Escherichia coli and Salmonella typhimurium: isolation of "periplasmic leaky" mutants. J Bacteriol. 1972 Feb;109(2):520–525. doi: 10.1128/jb.109.2.520-525.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Luckey M., Wayne R., Neilands J. B. In vitro competition between ferrichrome and phage for the outer membrane T5 receptor complex of Escherichia coli. Biochem Biophys Res Commun. 1975 May 19;64(2):687–693. doi: 10.1016/0006-291x(75)90375-7. [DOI] [PubMed] [Google Scholar]
  9. Moldow C., Robertson J., Rothfield L. Purification of bacterial membrane proteins. The use of guanidinium thiocyanate and urea. J Membr Biol. 1972;10(2):137–152. doi: 10.1007/BF01867850. [DOI] [PubMed] [Google Scholar]
  10. Neville D. M., Jr Molecular weight determination of protein-dodecyl sulfate complexes by gel electrophoresis in a discontinuous buffer system. J Biol Chem. 1971 Oct 25;246(20):6328–6334. [PubMed] [Google Scholar]
  11. Osborn M. J., Gander J. E., Parisi E., Carson J. Mechanism of assembly of the outer membrane of Salmonella typhimurium. Isolation and characterization of cytoplasmic and outer membrane. J Biol Chem. 1972 Jun 25;247(12):3962–3972. [PubMed] [Google Scholar]
  12. Pollack J. R., Ames B. N., Neilands J. B. Iron transport in Salmonella typhimurium: mutants blocked in the biosynthesis of enterobactin. J Bacteriol. 1970 Nov;104(2):635–639. doi: 10.1128/jb.104.2.635-639.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. ROTHFIELD L., OSBORN M. J., HORECKER B. L. BIOSYNTHESIS OF BACTERIAL LIPOPOLYSACCHARIDE. II. INCORPORATION OF GLUCOSE AND GALACTOSE CATALYZED BY PARTICULATE AND SOLUBLE ENZYMES IN SALMONELLA. J Biol Chem. 1964 Sep;239:2788–2795. [PubMed] [Google Scholar]
  14. Randall-Hazelbauer L., Schwartz M. Isolation of the bacteriophage lambda receptor from Escherichia coli. J Bacteriol. 1973 Dec;116(3):1436–1446. doi: 10.1128/jb.116.3.1436-1446.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Schnaitman C. A. Outer membrane proteins of Escherichia coli. IV. Differences in outer membrane proteins due to strain and cultural differences. J Bacteriol. 1974 May;118(2):454–464. doi: 10.1128/jb.118.2.454-464.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Wang C. C., Newton A. An additional step in the transport of iron defined by the tonB locus of Escherichia coli. J Biol Chem. 1971 Apr 10;246(7):2147–2151. [PubMed] [Google Scholar]
  17. Weigand R. A., Rothfield L. I. Genetic and physiological classification of periplasmic-leaky mutants of Salmonella typhimurium. J Bacteriol. 1976 Jan;125(1):340–345. doi: 10.1128/jb.125.1.340-345.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES