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. 1990 Dec;172(12):7275–7277. doi: 10.1128/jb.172.12.7275-7277.1990

Lysis protein S of phage lambda functions in Saccharomyces cerevisiae.

J Garrett 1, C Bruno 1, R Young 1
PMCID: PMC210856  PMID: 2147680

Abstract

The lambda S lysis gene was cloned into a Saccharomyces cerevisiae expression vector under GAL1 control. Induction with galactose in S. cerevisiae terminated cell growth and prevented colony formation. Several membrane proteins immunoreactive with anti-S antibody accumulated in the membranes, indicating that sodium dodecyl sulfate-resistant oligomers of S are formed, similar to those observed in the membranes of Escherichia coli cells killed by expression of the S gene. These observations suggest that the S gene product functions as a cytotoxic protein in the yeast cytoplasmic membrane as it does in the bacterial membrane.

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Selected References

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  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. Bläsi U., Chang C. Y., Zagotta M. T., Nam K. B., Young R. The lethal lambda S gene encodes its own inhibitor. EMBO J. 1990 Apr;9(4):981–989. doi: 10.1002/j.1460-2075.1990.tb08200.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bläsi U., Nam K., Hartz D., Gold L., Young R. Dual translational initiation sites control function of the lambda S gene. EMBO J. 1989 Nov;8(11):3501–3510. doi: 10.1002/j.1460-2075.1989.tb08515.x. [DOI] [PMC free article] [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. Ito H., Fukuda Y., Murata K., Kimura A. Transformation of intact yeast cells treated with alkali cations. J Bacteriol. 1983 Jan;153(1):163–168. doi: 10.1128/jb.153.1.163-168.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Johnston M., Davis R. W. Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces cerevisiae. Mol Cell Biol. 1984 Aug;4(8):1440–1448. doi: 10.1128/mcb.4.8.1440. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Kunkel T. A., Roberts J. D., Zakour R. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 1987;154:367–382. doi: 10.1016/0076-6879(87)54085-x. [DOI] [PubMed] [Google Scholar]
  8. Nam K., Bläsi U., Zagotta M. T., Young R. Conservation of a dual-start motif in P22 lysis gene regulation. J Bacteriol. 1990 Jan;172(1):204–211. doi: 10.1128/jb.172.1.204-211.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Raab R., Neal G., Sohaskey C., Smith J., Young R. Dominance in lambda S mutations and evidence for translational control. J Mol Biol. 1988 Jan 5;199(1):95–105. doi: 10.1016/0022-2836(88)90381-6. [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. 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]
  12. Towbin H., Gordon J. Immunoblotting and dot immunobinding--current status and outlook. J Immunol Methods. 1984 Sep 4;72(2):313–340. doi: 10.1016/0022-1759(84)90001-2. [DOI] [PubMed] [Google Scholar]
  13. Yaffe M. P., Schatz G. Two nuclear mutations that block mitochondrial protein import in yeast. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4819–4823. doi: 10.1073/pnas.81.15.4819. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Zagotta M. T., Wilson D. B. Oligomerization of the bacteriophage lambda S protein in the inner membrane of Escherichia coli. J Bacteriol. 1990 Feb;172(2):912–921. doi: 10.1128/jb.172.2.912-921.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]

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