Skip to main content
SpringerLink
Log in

meoA is the structural gene for outer membrane protein c of Escherichia coli K12

  • Published:
Molecular and General Genetics MGG Aims and scope Submit manuscript

Summary

The isolation and characterization of two mutants of Escherichia coli K12 with an altered outer membrane protein c is described. The first mutant, strain CE1151, was isolated as a bacteriophage Mel resistant strain which contains normal levels of protein c. Mutant cells adsorbed the phage with a strongly decreased rate. Complexes of purified nonheat modified wild type protein c and wild type lipopolysaccharide inactivated phage Me1, indicating that these components are required for receptor activity for phage Me1. When wild type protein c was replaced by protein c of strain CE1151, the receptorcomplex was far less active, showing that protein c of strain CE1151 is altered. The second mutant produces a protein c with a decreased electrophoretic mobility, designated as protein c*. An altered apparent molecular weight was also observed for one or more fragments obtained after fragmentation of the mutant protein with cyanogen bromide, trypsin and chymotrypsin. Alteration of protein c was not accompanied by a detectable alteration in protein b or its fragments. Both mutations are located at minute 48 of the Escherichia coli K12 linkage map. The results strongly suggest that meoA is the structural gene for protein c.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  • Alphen, W. van, Boxtel, R. van, Selm, N. van, Lugtenberg, B.: Pores in the outer membrane of Escherichia coli K12. Involvement of proteins b and c in the permeation of cephaloridine and ampicillin. FEMS Lett. 3, 103–106 (1978b)

    Google Scholar 

  • Alphen, L. van, Havekes, L., Lugtenberg, B.: Major outer membrane protein d of Escherichia coli K12. Purification and in vitro activity of bacteriophage K3 and F-pilus mediated conjugation. FEBS Lett. 75, 285–290 (1977a)

    Google Scholar 

  • Alphen, W. van, Lugtenberg, B.: Influence of the osmolarity of the growth medium on the outer membrane protein pattern of Escherichia coli K12. J. Bacteriol. 131, 623–630 (1977)

    Google Scholar 

  • Alphen, W. van, Lugtenberg, B., Berendsen, W.: Heptose-deficient mutants of Escherichia coli K12 deficient in up to three major outer membrane proteins. Mol. Gen. Genet. 147, 263–269 (1976)

    Google Scholar 

  • Alphen, L. van, Lugtenberg, B., Boxtel, R. van, Verhoef, C.: Architecture of the outer membrane of Escherichia coli K12. I. Action of phospholipases A2 and C on wild type strains and outer membrane mutants. Biochim. Biophys. Acta 466, 257–268 (1977b)

    Google Scholar 

  • Alphen, W. van, Selm, N. van, Lugtenberg, B.: Pores in the outer membrane of Escherichia coli K12. Involvement of proteins b and e in the functioning of pores for nucleotides. Mol. Gen. Genet. 159, 75–83 (1978a)

    Google Scholar 

  • Ames, B.N., Dubin, D.T.: The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J. Biol. Chem. 235, 769–775 (1960)

    Google Scholar 

  • Bachmann, B.J., Low, K.B., Taylor, A.L.: Recalibrated linkage map of Escherichia coli K12. Bacteriol. Rev. 40, 116–167 (1976)

    Google Scholar 

  • Bassford, P.J., Jr., Diedrich, D.L., Schnaitman, C.A., Reeves, P.: Outer membrane proteins of Escherichia coli. VI. Protein alteration in bacteriophage-resistant mutants. J. Bacteriol. 131, 608–622 (1977)

    Google Scholar 

  • Bavoil, P., Nikaido, H., Meyenburg, K. von: Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein. Mol. Gen. Genet. 158, 23–33 (1978)

    Google Scholar 

  • Beacham, I.R., Haas, O., Yagil, E.: Mutants of Escherichia coli “cryptic” for certain periplasmic enzymes: evidence for an alteration of the outer membrane. J. Bacteriol. 129, 1034–1044 (1977)

    Google Scholar 

  • Boman, H.G., Monner, D.A.: Characterization of lipopolysaccharides from Escherichia coli K12 mutants. J. Bacteriol. 121, 455–464 (1975)

    Google Scholar 

  • Chai, T., Foulds, J.: Escherichia coli K12 tolF mutants: alterations in protein composition of the outer membrane. J. Bacteriol. 130, 781–786 (1977)

    Google Scholar 

  • Datta, D.B., Arden, B., Henning, U.: Major proteins of the Escherichia coli outer cell envelope membrane as bacteriophage receptors. J. Bacteriol. 131, 821–829 (1977)

    Google Scholar 

  • Dröge, W., Lehmann, V., Lüderitz, O., Westphal, O.: Structural investigations on the 2-keto-3-deoxyoctonate region of lipopolysaccharides. Eur. J. Biochem. 14, 175–184 (1970)

    Google Scholar 

  • Foulds, J.: tolf locus in Escherichia coli: chromosomal location and relationship to loci cmlB and tolD. J. Bacteriol. 128, 604–608 (1976)

    Google Scholar 

  • Hasegawa, Y., Yamada, H., Mizushima, S.: Interactions of outer membrane proteins O8 and O9 with the peptidoglycan sacculus of Escherichia coli K12. J. Biochem. (Japan) 12, 1401–1409 (1976)

    Google Scholar 

  • Henning, U., Schmidmayr, W., Hindennach, I.: Major proteins of the outer cell envelope membrane of Escherichia coli K12: multiple species of protein I. Mol. Gen. Genet. 154, 293–298 (1977)

    Google Scholar 

  • Hindennach, I., Henning, U.: The major proteins of the Escherichia coli outer cell envelope membrane. Eur. J. Biochem. 59, 207–213 (1975)

    Google Scholar 

  • Ichihara, S., Mizushima, S.: Characterization of major outer membrane proteins O8 and O9 of Escherichia coli K12. Evidence that structural genes for the two proteins are different. J. Biochem. (Japan) 83, 1095–1100 (1978)

    Google Scholar 

  • Lennox, E.G.: Transduction of linked genetic characters of the host by bacteriophage P1. Virology 1, 190–206 (1955)

    Google Scholar 

  • Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J.: Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265–275 (1951)

    Google Scholar 

  • Lugtenberg, B., Bronstein, H., Selm, N. van, Peters, R.: Peptidoglycan-associated outer membrane proteins in Gramnegative bacteria. Biochim. Biophys. Acta 465, 571–578 (1977)

    Google Scholar 

  • Lugtenberg, B., Meijers, J., Peters, R., Hoek, P. van der, Alphen, L. van: Electrophoretic resolution of the ‘major outer membrane protein’ of Escherichia coli K12 into four bands. FEBS-Lett. 58, 254–258 (1975)

    Google Scholar 

  • Lugtenberg, B., Peters, R., Bernheimer, H., Berendsen, W.: Influence of cultural conditions and mutations on the composition of the outer membrane proteins of Escherichia coli. Mol. Gen. Genet. 147, 251–262 (1976)

    Google Scholar 

  • Lutkenhaus, J.F.: Role of major outer membrane protein in Escherichia coli. J. Bacteriol. 131, 631–637 (1977)

    Google Scholar 

  • McMichael, J.C., Ou, J.T.: Metal ion dependence of a heat-modifiable protein from the outer membrane of Escherichia coli upon sodium dodecyl sulphate gel electrophoresis. J. Bacteriol. 132, 314–320 (1977)

    Google Scholar 

  • Miller, J.H.: Experiments in molecular genetics. Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory 1972

    Google Scholar 

  • Nagata, T., Horiuchi, T.: Isolation and characterization of a temperature sensitive amber suppressor mutant of Escherichia coli K12. Mol. Gen. Genet. 123, 77–88 (1973)

    Google Scholar 

  • Nakae, T.: Identification of the outer membrane protein of E. coli that produces transmembrane channels in reconstituted vesicle membranes. Biochem. Biophys. Res. Commun. 71, 877–884 (1976)

    Google Scholar 

  • Nakamura, K., Mizushima, S.: Effects of heating in dodecyl sulfate solution on the conformation and electrophoretic mobility of isolated major outer membrane proteins from Escherichia coli K12. J. Biochem. (Japan) 80, 1411–1422 (1976)

    Google Scholar 

  • Osborn, M.J.: Studies on the gram-negative cell wall, I. Evidence for the role of 2-keto-3-deoxyoctonate in the lipopolysaccharide of Salmonella typhimurium. Proc. Natl. Acad. Sci. USA 50, 499–506 (1963)

    Google Scholar 

  • Rosenbusch, J.P.: Characterization of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulphate binding. J. Biol. Chem. 249, 8019–8029 (1974)

    Google Scholar 

  • Rothfield, L., Horne, R.W.: Reassociation of purified lipopolysaccharide and phospholipid of the bacterial cell envelope: electron microscopic and monolayer studies. J. Bacteriol. 93, 1705–1721 (1967)

    Google Scholar 

  • Sarma, V., Reeves, P.: Genetic locus (ompB) affecting a major outer membrane protein in Escherichia coli K12. J. Bacteriol. 132, 23–27 (1977)

    Google Scholar 

  • Schmitges, C.J., Henning, U.: The major proteins of the Escherichia coli outer cell-envelope membrane. Heterogeneity of protein I. Eur. J. Biochem. 63, 47–52 (1976)

    Google Scholar 

  • Sekizawa, J., Inouye, S., Halegoua, S., Inouye, M.: Precursors of major outer membrane proteins of Escherichia coli. Biochem. Biophys. Res. Commun. 77, 1126–1133 (1977)

    Google Scholar 

  • Verhoef, C., Graaff, P.J. de, Lugtenberg, B.: Mapping of a gene for a major outer membrane protein of Escherichia coli K12 with the aid of a newly isolated bacteriophage. Mol. Gen. Genet. 150, 103–105 (1977)

    Google Scholar 

  • Verhoef, C., Lugtenberg, B., Boxtel, R. van, Graaff, P. de, Verheij, H.: Genetics and biochemistry of the peptidoglycan-associated proteins b and c of Escherichia coli K12. Mol. Gen. Genet. 169, 137–146 (1979)

    Google Scholar 

  • Yagil, E., Beacham, I.R., Nissim, A., Price, G.: Crypticity of periplasmic enzymes. Involvement of protein b in the permeability of the outer membrane of Escherichia coli. FEBS Lett. 85, 133–136 (1978)

    Google Scholar 

  • Yu, F., Mizushima, S.: Stimulation by lipopolysaccharide of the binding of outer membrane proteins O-8 and O-9 to the peptidoglycan layer of Escherichia coli K-12. Biochem. Biophys. Res. Commun. 74, 1397–1402 (1977)

    Google Scholar 

Download references

Author information

Author notes

  1. Louis Havekes

    Present address: Gaubius Institute, TNO Health Organization, Herenstraat 5d, Leiden, The Netherlands

Authors and Affiliations

  1. Department of Molecular Cell Biology, Section Microbiology, State University of Utrecht, Transitorium 3, Padualaan 8, Utrecht, The Netherlands

    Loek van Alphen, Ben Lugtenberg, Ria van Boxtel, Anne-Marie Hack, Cornelis Verhoef & Louis Havekes

  2. Institute for Molecular Biology, State University of Utrecht, Transitorium 3, Padualaan 8, Utrecht, The Netherlands

    Loek van Alphen, Ben Lugtenberg, Ria van Boxtel, Anne-Marie Hack, Cornelis Verhoef & Louis Havekes

Authors
  1. Loek van Alphen
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Ben Lugtenberg
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Ria van Boxtel
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Anne-Marie Hack
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Cornelis Verhoef
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. Louis Havekes
    View author publications

    You can also search for this author in PubMed Google Scholar

Additional information

Communicated by H.G. Wittmann

Rights and permissions

Reprints and permissions

About this article

Cite this article

van Alphen, L., Lugtenberg, B., van Boxtel, R. et al. meoA is the structural gene for outer membrane protein c of Escherichia coli K12. Molec. Gen. Genet. 169, 147–155 (1979). https://doi.org/10.1007/BF00271665

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00271665

Keywords

Search

Navigation