Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1979 Nov;140(2):369–376. doi: 10.1128/jb.140.2.369-376.1979

Cyclic adenosine 3',5'-monophosphate regulation of the bacteriophage T6/colicin K receptor in Escherichia coli.

E M Alderman, S S Dills, T Melton, W J Dobrogosz
PMCID: PMC216658  PMID: 227838

Abstract

Mutant strains of Escherichia coli unable to synthesize cyclic adenosine 3',5'-monophosphate (cAMP) or the cyclic adenosine monophosphate receptor protein (CRP) were more resistant than wild-type cells to infection by bacteriophage T6. This resistance was found to be associated with the decreased production of specific T6 receptor protein (also the colicin K receptor) located in the outer membrane protein fraction of these cells. Transcription of this particular outer membrane protein was regulated by the cAMP-CRP complex. A novel affinity technique coupled with sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used in these investigations.

Full text

PDF
374

Selected References

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

  1. Bassford P. J., Jr, Diedrich D. L., Schnaitman C. L., Reeves P. Outer membrane proteins of Escherichia coli. VI. Protein alteration in bacteriophage-resistant mutants. J Bacteriol. 1977 Aug;131(2):608–622. doi: 10.1128/jb.131.2.608-622.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bertolini M. J., Tankersley D. L., Schroeder D. D. Staining and destaining polyacrylamide gels: a comparison of coomassie blue and fast green protein dyes. Anal Biochem. 1976 Mar;71(1):6–13. doi: 10.1016/0003-2697(76)90003-8. [DOI] [PubMed] [Google Scholar]
  3. Bragg P. D., Hou C. Organization of proteins in the native and reformed outer membrane of Escherichia coli. Biochim Biophys Acta. 1972 Aug 9;274(2):478–488. doi: 10.1016/0005-2736(72)90193-9. [DOI] [PubMed] [Google Scholar]
  4. Broman R. L., Dobrogosz W. J. Stimulation of cytochrome synthesis in Escherichia coli by cyclic AMP. Arch Biochem Biophys. 1974 Jun;162(2):595–601. doi: 10.1016/0003-9861(74)90220-3. [DOI] [PubMed] [Google Scholar]
  5. Dallas W. S., Tseng Y., Dobrogosz W. J. Regulation of membrane functions and fatty acid composition in Escherichia coli by cyclic AMP receptor protein. Arch Biochem Biophys. 1976 Jul;175(1):295–302. doi: 10.1016/0003-9861(76)90511-7. [DOI] [PubMed] [Google Scholar]
  6. Dills S. E., Dobrogosz W. J. Cyclic adenosine 3',5'-monophosphate regulation of membrane energetics in Escherichia coli. J Bacteriol. 1977 Sep;131(3):854–865. doi: 10.1128/jb.131.3.854-865.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Ezzell J. W., Dobrogosz W. J. Altered hexose transport and salt sensitivity in cyclic adenosine 3',5'-monophosphate-deficient Escherichia coli. J Bacteriol. 1975 Nov;124(2):815–824. doi: 10.1128/jb.124.2.815-824.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ezzell J. W., Dobrogosz W. J. Cyclic AMP regulation of the hexose phosphate transport system in Escherichia coli. J Bacteriol. 1978 Feb;133(2):1047–1049. doi: 10.1128/jb.133.2.1047-1049.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kumar S. Properties of adenyl cyclase and cyclic adenosine 3',5'-monophosphate receptor protein-deficient mutants of Escherichia coli. J Bacteriol. 1976 Feb;125(2):545–555. doi: 10.1128/jb.125.2.545-555.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. 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]
  11. Lee N., Inouye M. Outer membrane proteins of Escherichia coli: biosynthesis and assembly. FEBS Lett. 1974 Feb 15;39(2):167–170. doi: 10.1016/0014-5793(74)80043-8. [DOI] [PubMed] [Google Scholar]
  12. 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]
  13. Manning P. A., Reeves P. Outer membrane of Escherichia coli K-12: TSX mutants (resistant to bacteriophage T6 and colicin K) lack an outer membrane protein. Biochem Biophys Res Commun. 1976 Jul 26;71(2):466–471. doi: 10.1016/0006-291x(76)90810-x. [DOI] [PubMed] [Google Scholar]
  14. Pastan I., Adhya S. Cyclic adenosine 5'-monophosphate in Escherichia coli. Bacteriol Rev. 1976 Sep;40(3):527–551. doi: 10.1128/br.40.3.527-551.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Schnaitman C. A. Effect of ethylenediaminetetraacetic acid, Triton X-100, and lysozyme on the morphology and chemical composition of isolate cell walls of Escherichia coli. J Bacteriol. 1971 Oct;108(1):553–563. doi: 10.1128/jb.108.1.553-563.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Schnaitman C. A. Outer membrane proteins of Escherichia coli. 3. Evidence that the major protein of Escherichia coli O111 outer membrane consists of four distinct polypeptide species. J Bacteriol. 1974 May;118(2):442–453. doi: 10.1128/jb.118.2.442-453.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Schnaitman C. A. Outer membrane proteins of Escherichia coli. I. Effect of preparative conditions on the migration of protein in polyacrylamide gels. Arch Biochem Biophys. 1973 Aug;157(2):541–552. doi: 10.1016/0003-9861(73)90673-5. [DOI] [PubMed] [Google Scholar]
  18. Schnaitman C. A. Outer membrane proteins of Escherichia coli. II. Heterogeneity of major outer membrane polypeptides. Arch Biochem Biophys. 1973 Aug;157(2):553–560. doi: 10.1016/0003-9861(73)90674-7. [DOI] [PubMed] [Google Scholar]
  19. 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]
  20. Schnaitman C. A. Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100. J Bacteriol. 1971 Oct;108(1):545–552. doi: 10.1128/jb.108.1.545-552.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Shapiro A. L., Viñuela E., Maizel J. V., Jr Molecular weight estimation of polypeptide chains by electrophoresis in SDS-polyacrylamide gels. Biochem Biophys Res Commun. 1967 Sep 7;28(5):815–820. doi: 10.1016/0006-291x(67)90391-9. [DOI] [PubMed] [Google Scholar]
  22. Weiss M. J., Luria S. E. Reduction of membrane potential, an immediate effect of colicin K. Proc Natl Acad Sci U S A. 1978 May;75(5):2483–2487. doi: 10.1073/pnas.75.5.2483. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Yamamoto K. R., Alberts B. M., Benzinger R., Lawhorne L., Treiber G. Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification. Virology. 1970 Mar;40(3):734–744. doi: 10.1016/0042-6822(70)90218-7. [DOI] [PubMed] [Google Scholar]
  24. Yu J., Fischman D. A., Steck T. L. Selective solubilization of proteins and phospholipids from red blood cell membranes by nonionic detergents. J Supramol Struct. 1973;1(3):233–248. doi: 10.1002/jss.400010308. [DOI] [PubMed] [Google Scholar]

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

RESOURCES