1887

Abstract

Summary: Organisms of three independently isolated mutants of failed to form colonies on glucose minimal agar (glucose MA) at 44 °C after growth in glucose minimal salts medium at 37 °C, although all three strains formed colonies on nutrient agar at 44 °C. Supplementation of the glucose MA with individual amino acids including L-methionine and/or L-cysteine did not allow colony formation at 44 °C, although addition of 0·1% Casamino acids was effective; replacement of glucose with other energy sources or ammonium ions with glutamate also did not allow growth at 44 °C. The failure to form colonies at 44 °C was not due to killing of the organisms, because colonies were formed if plates of the mutant initially incubated at 44 °C were shifted to 30 °C after 16 h. Introduction of the ColV, I-K94 plasmid into P678-54 , 1131 or an mutant suppressed the 44 °C growth lesion, but other plasmids (F , R483ColIa, RI, ColB-K98, R124) tested in P678-54 did not. Growth of the ColV, I-K94 derivative at 44 °C was due to a suppressing effect of the plasmid rather than to introduction of the plasmid into a variant with normal or altered OmpA protein. An attempt was made to ascertain which component(s) encoded by ColV, I-K94 was (were) responsible for allowing growth at 44 °C. Transfer components appeared unlikely to be involved and plasmids which conferred individual colicins (plus the corresponding immunity component) did not suppress. The findings that the ColV, I-K94-encoded VmpA protein resembles the OmpA protein () immunologically and () in being a transmembrane component of the outer membrane suggested that it might be the presence of the VmpA protein which allowed growth at 44 °C. Several experiments were in accord with this possibility.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-132-8-2287
1986-08-01
2024-04-20
Loading full text...

Full text loading...

/deliver/fulltext/micro/132/8/mic-132-8-2287.html?itemId=/content/journal/micro/10.1099/00221287-132-8-2287&mimeType=html&fmt=ahah

References

  1. Braun V. 1978; Structure-function relationships of the Gram-negative bacterial cell envelope. Symposia of the Society for General Microbiology 28:111–138
    [Google Scholar]
  2. Burnell E., Van Alphen L., Verkleij A., De Kruijff B., Lugtenberg B. 1980; 31P Nuclear magnetic resonance and freeze fracture electron microscopy studies on Escherichia coli. Biochimica et biophysica acta 591:518–532
    [Google Scholar]
  3. Chen R., Schmidmayr W., Kramer C., Henning U. 1980; Primary structure of major outer membrane protein II* (OmpA protein) of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America 71:4592–4596
    [Google Scholar]
  4. Cole S. T., Chen-Schmeisser U., Hindennach I., Henning U. 1983; Apparent bacteriophage-binding region of an Escherichia coli K 12 outer membrane protein. Journal of Bacteriology 153:581–587
    [Google Scholar]
  5. Davis B. D., Mingioli E. S. 1950; Mutants of Escherichia coli requiring methionine or vitamin B 12. Journal of Bacteriology 60:17–28
    [Google Scholar]
  6. Hardy K. G. 1975; Colicinogeny and related phenomena. Bacteriological Reviews 39:464–515
    [Google Scholar]
  7. Henning U., Hindennach I., Haller I. 1976; The major proteins of the Escherichia coli cell envelope membrane: evidence for the structural gene of protein II*. FEBS Letters 61:46–48
    [Google Scholar]
  8. Ito K., Sato T., Yura T. 1977; Synthesis and assembly of the membrane proteins in E. coli. Cell 11:551–559
    [Google Scholar]
  9. Kamio Y., Nikaido H. 1977; Outer membrane of Salmonella typhimurium. Identification of proteins exposed on cell surface Biochimica et biophysica acta 46:589–601
    [Google Scholar]
  10. Lugtenberg B., Meijers J., Peters R., Van Der Hock P., Van Alphen L. 1975; Electrophoretic resolution of the ‘major outer membrane protein’ of Escherichia coli K 12 into four bands. FEBS Letters 58:254–258
    [Google Scholar]
  11. Ljktenhaus J. F. 1977; Role of major outer membrane protein in Escherichia coli. Journal of Bacteriology 131:631–637
    [Google Scholar]
  12. Manning P. A., Puspurs A., Reeves P. 1976; Outer membrane of Escherichia coli K 12: isolation of mutants with altered protein 3A by using host range mutants of bacteriophage K3. Journal of Bacteriology 127:1080–1084
    [Google Scholar]
  13. Manning P. A., Pugsley A. P., Reeves P. 1977; Defective growth functions in mutants of Escherichia coli K12 lacking a major outer membrane protein. Journal of Molecular Biology 116:285–300
    [Google Scholar]
  14. Moores J. C., Rowbury R. J. 1982; A new major outer membrane protein in derivatives of Escherichia coli carrying the virulence plasmid CoIV-K94. Zeitschr ft fur allgemeine Mikrobiologie 22:465–475
    [Google Scholar]
  15. Morona R., Klose M., Henning U. 1984; Escherichia coli K 12 outer membrane protein (OmpA) as a bacteriophage receptor: analysis of mutant genes expressing altered proteins. Journal OJ Bacteriology 159:570–578
    [Google Scholar]
  16. Nikaido H. 1979; Non-specific transport through the outer membrane. In Bacterial Outer Membranes pp 361–408 Edited by Inouye M. New York:: Wiley;
    [Google Scholar]
  17. Ron E. Z. 1975; Growth of enterobacteriaceae at elevated temperatures : limitation by methionine. Journal of Bacteriology 124:243–246
    [Google Scholar]
  18. Rosenbusch J. P. 1974; Characterisation of the major envelope protein from Escherichia coli. Regular arrangement on the peptidoglycan and unusual dodecyl sulfate binding. Journal of Biological Chemistry 249:8019–8029
    [Google Scholar]
  19. Rossouw F. T., Rowbury R. J. 1984; Effects of the resistance plasmid R124 on the level of the OmpF outer membrane protein and on the response of Escherichia coli to environmental agents. Journal of Applied Bacteriology 56:63–79
    [Google Scholar]
  20. Rowbury R. J., Deeney C. M., Reakes C., Rossouw F. T., Smith D. G., Tewari R. 1985; Envelope protein changes, autoagglutination, sensitivity to hydrophobic agents and a conditional division lesion in Escherichia coli strains carrying ColV virulence plasmids. Annales de I'lnstitut Pasteur 136A147–157
    [Google Scholar]
  21. Skurray R. A., Hancock R. E. W., Reeves P. 1974; Con-mutants: class of mutants in Escherichia coli K 12 lacking a major cell wall protein and defective in conjugation and adsorption of bacteriophage. Journal of Bacteriology 119:726–735
    [Google Scholar]
  22. Sonntag I., Schwarz H., Hirota Y., Henning U. 1978; Cell envelope and shape of Escherichia coli: multiple mutants missing the outer membrane lipoprotein and other major outer membrane proteins. Journal of Bacteriology 136:280–285
    [Google Scholar]
  23. Williams P. H. 1979; Important component in the virulence of invasive strains of Escherichia coli. Infection and Immunity 26:925–932
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-132-8-2287
Loading
/content/journal/micro/10.1099/00221287-132-8-2287
Loading

Data & Media loading...

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error