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. 1980 Sep;143(3):1374–1383. doi: 10.1128/jb.143.3.1374-1383.1980

Pleiotropic mutations rendering Escherichia coli K-12 resistant to bacteriophage TP1.

C Wandersman, F Moreno, M Schwartz
PMCID: PMC294516  PMID: 6997269

Abstract

tpo mutations, located at 74 min on the genetic map, rendered Escherichia coli K-12 resistant to TP1, a phage which can use either the OmpF protein or the LamB protein as its receptor. tpo mutants synthesized decreased amounts of OmpF and LamB proteins but increased amounts of the OmpC product, another outer membrane protein. The effect of the tpo mutations in lam B gene expression was transcriptional. It is one facet of the following effect on the maltose regulon: strong decreases in the syntheses of the LamB protein and the periplasmic MalE protein occurred when the regulon was uninduced; a lesser decrease occurred in the syntheses of the LamB protein the MalE protein, and the cytoplasmic MalQ protein (amylomaltase) when the regulon was induced. The tpo mutants were found to be phenotypically identical to the perA mutant recently described by Wanner et al. (J. Bacteriol. 140:229--239, 1979) and to some of the ompB mutants described by Verhoef et al. (Mol. Gen. Genet. 169:137--146, 1979). Mapping and complementation analysis suggested that these three types of mutations belong to the same cistron. Our results bring to at least four the number of clearly distinct phenotypes which can result from mutations at, or close to, ompB, a locus which appears increasingly complex.

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Selected References

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

  1. Anderson C. W., Baum P. R., Gesteland R. F. Processing of adenovirus 2-induced proteins. J Virol. 1973 Aug;12(2):241–252. doi: 10.1128/jvi.12.2.241-252.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bachmann B. J., Low K. B., Taylor A. L. Recalibrated linkage map of Escherichia coli K-12. Bacteriol Rev. 1976 Mar;40(1):116–167. doi: 10.1128/br.40.1.116-167.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bavoil P., Nikaido H., von Meyenburg K. Pleiotropic transport mutants of Escherichia coli lack porin, a major outer membrane protein. Mol Gen Genet. 1977 Dec 14;158(1):23–33. doi: 10.1007/BF00455116. [DOI] [PubMed] [Google Scholar]
  4. Datta D. B., Arden B., Henning U. Major proteins of the Escherichia coli outer cell envelope membrane as bacteriophage receptors. J Bacteriol. 1977 Sep;131(3):821–829. doi: 10.1128/jb.131.3.821-829.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Debarbouille M., Schwartz M. The use of gene fusions to study the expression of malT the positive regulator gene of the maltose regulon. J Mol Biol. 1979 Aug 15;132(3):521–534. doi: 10.1016/0022-2836(79)90273-0. [DOI] [PubMed] [Google Scholar]
  6. DiRienzo J. M., Nakamura K., Inouye M. The outer membrane proteins of Gram-negative bacteria: biosynthesis, assembly, and functions. Annu Rev Biochem. 1978;47:481–532. doi: 10.1146/annurev.bi.47.070178.002405. [DOI] [PubMed] [Google Scholar]
  7. Débarbouillé M., Shuman H. A., Silhavy T. J., Schwartz M. Dominant constitutive mutations in malT, the positive regulator gene of the maltose regulon in Escherichia coli. J Mol Biol. 1978 Sep 15;124(2):359–371. doi: 10.1016/0022-2836(78)90304-2. [DOI] [PubMed] [Google Scholar]
  8. Hall M. N., Silhavy T. J. Transcriptional regulation of Escherichia coli K-12 major outer membrane protein 1b. J Bacteriol. 1979 Nov;140(2):342–350. doi: 10.1128/jb.140.2.342-350.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Hantke K. Major outer membrane proteins of E. coli K12 serve as receptors for the phages T2 (protein Ia) and 434 (protein Ib). Mol Gen Genet. 1978 Aug 17;164(2):131–135. doi: 10.1007/BF00267377. [DOI] [PubMed] [Google Scholar]
  10. Hatfield D., Hofnung M., Schwartz M. Genetic analysis of the maltose A region in Escherichia coli. J Bacteriol. 1969 May;98(2):559–567. doi: 10.1128/jb.98.2.559-567.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hofnung M., Schwartz M., Hatfield D. Complementation studies in the maltose-A region of the Escherichia coli K12 genetic map. J Mol Biol. 1971 Nov 14;61(3):681–694. doi: 10.1016/0022-2836(71)90072-6. [DOI] [PubMed] [Google Scholar]
  12. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  13. Marchal C., Perrin D., Hedgpeth J., Hofnung M. Synthesis and maturation of lambda receptor in Escherichia coli K-12: in vivo and in vitro expression of gene lamB under lac promoter control. Proc Natl Acad Sci U S A. 1980 Mar;77(3):1491–1495. doi: 10.1073/pnas.77.3.1491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Nakae T. Identification of the outer membrane protein of E. coli that produces transmembrane channels in reconstituted vesicle membranes. Biochem Biophys Res Commun. 1976 Aug 9;71(3):877–884. doi: 10.1016/0006-291x(76)90913-x. [DOI] [PubMed] [Google Scholar]
  15. Raibaud O., Roa M., Braun-Breton C., Schwartz M. Structure of the malB region in Escherichia coli K12. I. Genetic map of the malK-lamB operon. Mol Gen Genet. 1979 Jul 24;174(3):241–248. doi: 10.1007/BF00267796. [DOI] [PubMed] [Google Scholar]
  16. 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]
  17. Roa M. Interaction of bacteriophage K10 with its receptor, the lamB protein of Escherichia coli. J Bacteriol. 1979 Nov;140(2):680–686. doi: 10.1128/jb.140.2.680-686.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Sanzey B. Modulation of gene expression by drugs affecting deoxyribonucleic acid gyrase. J Bacteriol. 1979 Apr;138(1):40–47. doi: 10.1128/jb.138.1.40-47.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Sarma V., Reeves P. Genetic locus (ompB) affecting a major outer-membrane protein in Escherichia coli K-12. J Bacteriol. 1977 Oct;132(1):23–27. doi: 10.1128/jb.132.1.23-27.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Schwartz M. Expression phénotypique et localisation génétique de mutations affectant le métabolisme du maltose chez Escherichia coli K 12. Ann Inst Pasteur (Paris) 1967 Jun;112(6):673–698. [PubMed] [Google Scholar]
  21. Schwartz M., Kellermann O., Szmelcman S., Hazelbauer G. L. Further studies on the binding of maltose to the maltose-binding protein of Escherichia coli. Eur J Biochem. 1976 Dec;71(1):167–170. doi: 10.1111/j.1432-1033.1976.tb11102.x. [DOI] [PubMed] [Google Scholar]
  22. Schwartz M. Reversible interaction between coliphage lambda and its receptor protein. J Mol Biol. 1975 Nov 25;99(1):185–201. doi: 10.1016/s0022-2836(75)80167-7. [DOI] [PubMed] [Google Scholar]
  23. Schwartz M. Sur l'existence chez Escherichia coli K 12 d'une régulation commune à la biosynthèse des récepteurs du bactériophage et au métabolisme du maltose. Ann Inst Pasteur (Paris) 1967 Nov;113(5):685–704. [PubMed] [Google Scholar]
  24. Silhavy T. J., Shuman H. A., Beckwith J., Schwartz M. Use of gene fusions to study outer membrane protein localization in Escherichia coli. Proc Natl Acad Sci U S A. 1977 Dec;74(12):5411–5415. doi: 10.1073/pnas.74.12.5411. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Szmelcman S., Hofnung M. Maltose transport in Escherichia coli K-12: involvement of the bacteriophage lambda receptor. J Bacteriol. 1975 Oct;124(1):112–118. doi: 10.1128/jb.124.1.112-118.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Verhoef C., Lugtenberg B., van Boxtel R., de Graaff P., Verheij H. Genetics and biochemistry of the peptidoglycan-associated proteins b and c of Escherichia coli K12. Mol Gen Genet. 1979 Jan 31;169(2):137–146. doi: 10.1007/BF00271664. [DOI] [PubMed] [Google Scholar]
  27. Wandersman C., Schwartz M., Ferenci T. Escherichia coli mutants impaired in maltodextrin transport. J Bacteriol. 1979 Oct;140(1):1–13. doi: 10.1128/jb.140.1.1-13.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Wandersman C., Schwartz M. Protein Ia and the lamB protein can replace each other in the constitution of an active receptor for the same coliphage. Proc Natl Acad Sci U S A. 1978 Nov;75(11):5636–5639. doi: 10.1073/pnas.75.11.5636. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Wanner B. L., Sarthy A., Beckwith J. Escherichia coli pleiotropic mutant that reduces amounts of several periplasmic and outer membrane proteins. J Bacteriol. 1979 Oct;140(1):229–239. doi: 10.1128/jb.140.1.229-239.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]

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