Skip to main content
Journal of Virology logoLink to Journal of Virology
. 1977 Sep;23(3):626–636. doi: 10.1128/jvi.23.3.626-636.1977

Genetic and physiological control of host cell lysis by bacteriophage lambda.

B G Rolfe, J H Campbell
PMCID: PMC515874  PMID: 330879

Abstract

The timing of host cell lysis at the end of the lytic cycle of phage lambda is under complex control. The lambda S protein stimulates lysis. Another physiological system, the lysis regulator, inhibitis lysis from occurring prematurely. The effects of a series of phage and bacterial mutations on these controls are described. They show that the lambda rex gene plays a role in regulating lysis under suboptimal growth conditions. In certain mutant cells, and especially under anaerobic culture conditions, the rex gene aids in the scheduling of host cell lysis. The data also suggest that the lysis regulator may control the transition of the lambda S protein from an inactive to an active state.

Full text

PDF
626

Selected References

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

  1. Bernstein A., Rolfe B., Onodera K. Pleiotropic properties and genetic organization of the tolA,B locus of Escherichia coli K-12. J Bacteriol. 1972 Oct;112(1):74–83. doi: 10.1128/jb.112.1.74-83.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Butlin J. D., Cox G. B., Gibson F. Oxidative phosphorylation in Escherichia coli K-12: the genetic and biochemical characterisations of a strain carrying a mutation in the uncB gene. Biochim Biophys Acta. 1973 Feb 22;292(2):366–375. doi: 10.1016/0005-2728(73)90043-1. [DOI] [PubMed] [Google Scholar]
  3. Butlin J. D., Cox G. B., Gibson F. Oxidative phosphorylation in Escherichia coli K12. Mutations affecting magnesium ion- or calcium ion-stimulated adenosine triphosphatase. Biochem J. 1971 Aug;124(1):75–81. doi: 10.1042/bj1240075. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Calendar R., Lindqvist B., Sironi G., Clark A. J. Characterization of REP- mutants and their interaction with P2 phage. Virology. 1970 Jan;40(1):72–83. doi: 10.1016/0042-6822(70)90380-6. [DOI] [PubMed] [Google Scholar]
  5. Campbell J. H., Rolfe B. G. Evidence for a dual control of the initiation of host-cell lysis caused by phage lambda. Mol Gen Genet. 1975 Aug 5;139(1):1–8. doi: 10.1007/BF00267990. [DOI] [PubMed] [Google Scholar]
  6. Christensen J. R., Geiman J. M. A new effect of the rex gene of phage lambda: premature lysis after infection by phage T1. Virology. 1973 Nov;56(1):285–290. doi: 10.1016/0042-6822(73)90306-1. [DOI] [PubMed] [Google Scholar]
  7. Goldberg A. R., Howe M. New mutations in the S cistron of bacteriophage lambda affecting host cell lysis. Virology. 1969 May;38(1):200–202. doi: 10.1016/0042-6822(69)90148-2. [DOI] [PubMed] [Google Scholar]
  8. Gussin G. N., Peterson V. Isolation and properties of rex - mutants of bacteriophage lambda. J Virol. 1972 Oct;10(4):760–765. doi: 10.1128/jvi.10.4.760-765.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. MONOD J., CHANGEUX J. P., JACOB F. Allosteric proteins and cellular control systems. J Mol Biol. 1963 Apr;6:306–329. doi: 10.1016/s0022-2836(63)80091-1. [DOI] [PubMed] [Google Scholar]
  10. 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]
  11. Reader R. W., Siminovitch L. Lysis defective mutants of bacteriophage lambda: on the role of the S function in lysis. Virology. 1971 Mar;43(3):623–637. doi: 10.1016/0042-6822(71)90287-x. [DOI] [PubMed] [Google Scholar]
  12. Rolfe B. G., Campbell J. H. A relationship between tolerance to colicin K and the mechanism of phage-induced host cell lysis. Mol Gen Genet. 1974;133(4):293–297. doi: 10.1007/BF00332705. [DOI] [PubMed] [Google Scholar]
  13. Rolfe B., Schell J., Becker A., Heip J., Onodera K., Schell-Frederick E. A colicin-tolerant mutant of Escherichia coli with reduced levels of cyclic AMP and a strong bias towards lambda lysogeny. Mol Gen Genet. 1973 Jan 18;120(1):1–16. doi: 10.1007/BF00332980. [DOI] [PubMed] [Google Scholar]
  14. SUSSMAN R., JACOB F. [On a thermosensitive repression system in the Escherichia coli lambda bacteriophage]. C R Hebd Seances Acad Sci. 1962 Feb 19;254:1517–1519. [PubMed] [Google Scholar]
  15. Siegel E. C. Ultraviolet-sensitive mutator mutU4 of Escherichia coli inviable with polA. J Bacteriol. 1973 Jan;113(1):161–166. doi: 10.1128/jb.113.1.161-166.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Taylor A. Endopeptidase activity of phage lamba-endolysin. Nat New Biol. 1971 Dec 1;234(48):144–145. doi: 10.1038/newbio234144a0. [DOI] [PubMed] [Google Scholar]
  17. Yokota T., Gots J. S. Requirement of adenosine 3', 5'-cyclic phosphate for flagella formation in Escherichia coli and Salmonella typhimurium. J Bacteriol. 1970 Aug;103(2):513–516. doi: 10.1128/jb.103.2.513-516.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES