Skip to main content
Journal of Virology logoLink to Journal of Virology
. 1985 Mar;53(3):1008–1011. doi: 10.1128/jvi.53.3.1008-1011.1985

Subcellular localization of lethal lysis proteins of bacteriophages lambda and phiX174.

E Altman, K Young, J Garrett, R Altman, R Young
PMCID: PMC254745  PMID: 3156254

Abstract

The gene products of the lethal lysis genes S and E of the bacteriophages lambda and phiX174, respectively, were shown to be associated primarily with inner membrane material by isopycnic sucrose gradient centrifugation of lysates of infected cells. A small amount of each polypeptide appeared to be in the outer membrane fraction.

Full text

PDF
1008

Images in this article

Selected References

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

  1. Bienkowska-Szewczyk K., Lipinska B., Taylor A. The R gene product of bacteriophage lambda is the murein transglycosylase. Mol Gen Genet. 1981;184(1):111–114. doi: 10.1007/BF00271205. [DOI] [PubMed] [Google Scholar]
  2. CAMPBELL A. Sensitive mutants of bacteriophage lambda. Virology. 1961 May;14:22–32. doi: 10.1016/0042-6822(61)90128-3. [DOI] [PubMed] [Google Scholar]
  3. Emr S. D., Hanley-Way S., Silhavy T. J. Suppressor mutations that restore export of a protein with a defective signal sequence. Cell. 1981 Jan;23(1):79–88. doi: 10.1016/0092-8674(81)90272-5. [DOI] [PubMed] [Google Scholar]
  4. Garrett J. M., Young R. Lethal action of bacteriophage lambda S gene. J Virol. 1982 Dec;44(3):886–892. doi: 10.1128/jvi.44.3.886-892.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Garrett J., Fusselman R., Hise J., Chiou L., Smith-Grillo D., Schulz J., Young R. Cell lysis by induction of cloned lambda lysis genes. Mol Gen Genet. 1981;182(2):326–331. doi: 10.1007/BF00269678. [DOI] [PubMed] [Google Scholar]
  6. Hare J. F., Olden K., Kennedy E. P. Heterogeneity of membrane vesicles from Escherichia coli and their subfractionation with antibody to ATPase. Proc Natl Acad Sci U S A. 1974 Dec;71(12):4843–4846. doi: 10.1073/pnas.71.12.4843. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Henrich B., Lubitz W., Plapp R. Lysis of Escherichia coli by induction of cloned phi X174 genes. Mol Gen Genet. 1982;185(3):493–497. doi: 10.1007/BF00334146. [DOI] [PubMed] [Google Scholar]
  8. Hutchison C. A., 3rd, Sinsheimer R. L. The process of infection with bacteriophage phi-X174. X. Mutations in a phi-X Lysis gene. J Mol Biol. 1966 Jul;18(3):429–447. doi: 10.1016/s0022-2836(66)80035-9. [DOI] [PubMed] [Google Scholar]
  9. MacGregor C. H., Bishop C. W., Blech J. E. Localization of proteolytic activity in the outer membrane of Escherichia coli. J Bacteriol. 1979 Jan;137(1):574–583. doi: 10.1128/jb.137.1.574-583.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. 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]
  11. Pollock T. J., Tessman E. S., Tessman I. Identification of lysis protein E of bacteriophage phiX174. J Virol. 1978 Oct;28(1):408–410. doi: 10.1128/jvi.28.1.408-410.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Reader R. W., Siminovitch L. Lysis defective mutants of bacteriophage lambda: genetics and physiology of S cistron mutants. Virology. 1971 Mar;43(3):607–622. doi: 10.1016/0042-6822(71)90286-8. [DOI] [PubMed] [Google Scholar]
  13. Wilson D. B. Effect of the lambda S gene product on properties of the Escherichia coli inner membrane. J Bacteriol. 1982 Sep;151(3):1403–1410. doi: 10.1128/jb.151.3.1403-1410.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Young K. D., Young R. Lytic action of cloned phi X174 gene E. J Virol. 1982 Dec;44(3):993–1002. doi: 10.1128/jvi.44.3.993-1002.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Young R., Way J., Way S., Yin J., Syvanen M. Transposition mutagenesis of bacteriophage lambda: a new gene affecting cell lysis. J Mol Biol. 1979 Aug 15;132(3):307–322. doi: 10.1016/0022-2836(79)90262-6. [DOI] [PubMed] [Google Scholar]
  16. von Heijne G. How signal sequences maintain cleavage specificity. J Mol Biol. 1984 Feb 25;173(2):243–251. doi: 10.1016/0022-2836(84)90192-x. [DOI] [PubMed] [Google Scholar]
  17. von Heijne G. Membrane proteins: the amino acid composition of membrane-penetrating segments. Eur J Biochem. 1981 Nov;120(2):275–278. doi: 10.1111/j.1432-1033.1981.tb05700.x. [DOI] [PubMed] [Google Scholar]
  18. von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem. 1983 Jun 1;133(1):17–21. doi: 10.1111/j.1432-1033.1983.tb07424.x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES