Skip to main content
NCBI home page
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1995 Nov;61(11):4099–4104. doi: 10.1128/aem.61.11.4099-4104.1995

Identification of prophage genes expressed in lysogens of the Lactococcus lactis bacteriophage BK5-T.

J D Boyce 1, B E Davidson 1, A J Hillier 1
PMCID: PMC167717  PMID: 8526524

Abstract

Bacteriophage BK5-T is a small isometric-headed temperate phage that infects Lactococcus lactis subsp. cremoris. Northern (RNA) analysis of mRNA produced by lysogenic strains containing BK5-T prophage revealed four major BK5-T transcripts that are 0.8, 1.3, 1.8, and 1.8 kb in size and enabled a transcription map of the prophage genome to be prepared. The position and size of each transcript corresponded closely to the position and size of open reading frames predicted from the nucleotide sequence of BK5-T. Analysis of the transcripts suggested that one of them was derived from the gene encoding the BK5-T integrase and another was from the gene encoding the BK5-T homolog of the lambda cI repressor. Computer analysis of the nucleotide sequence upstream of the BK5-T cI homolog predicted the presence of a pair of divergent promoters and three inverted repeat sequences, features characteristic of temperature-phage immunity regions. By analogy with lambda, the three inverted repeat sequences could be binding sites for cI or Cro homologs and the two divergent promoters could initiate transcription through the BK5-T equivalents of cI and cro.

Full Text

The Full Text of this article is available as a PDF (739.3 KB).

Selected References

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

  1. Arendt E. K., Daly C., Fitzgerald G. F., van de Guchte M. Molecular characterization of lactococcal bacteriophage Tuc2009 and identification and analysis of genes encoding lysin, a putative holin, and two structural proteins. Appl Environ Microbiol. 1994 Jun;60(6):1875–1883. doi: 10.1128/aem.60.6.1875-1883.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Boyce J. D., Davidson B. E., Hillier A. J. Sequence analysis of the Lactococcus lactis temperate bacteriophage BK5-T and demonstration that the phage DNA has cohesive ends. Appl Environ Microbiol. 1995 Nov;61(11):4089–4098. doi: 10.1128/aem.61.11.4089-4098.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boyce J. D., Davidson B. E., Hillier A. J. Spontaneous deletion mutants of the Lactococcus lactis temperate bacteriophage BK5-T and localization of the BK5-T attP site. Appl Environ Microbiol. 1995 Nov;61(11):4105–4109. doi: 10.1128/aem.61.11.4105-4109.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Brennan R. G., Matthews B. W. The helix-turn-helix DNA binding motif. J Biol Chem. 1989 Feb 5;264(4):1903–1906. [PubMed] [Google Scholar]
  5. Chandry P. S., Davidson B. E., Hillier A. J. Temporal transcription map of the Lactococcus lactis bacteriophage sk1. Microbiology. 1994 Sep;140(Pt 9):2251–2261. doi: 10.1099/13500872-140-9-2251. [DOI] [PubMed] [Google Scholar]
  6. Echols H. Constitutive integrative recombination by bacteriophage lambda. Virology. 1975 Apr;64(2):557–559. doi: 10.1016/0042-6822(75)90133-6. [DOI] [PubMed] [Google Scholar]
  7. Garriga X., Calero S., Barbé J. Nucleotide sequence analysis and comparison of the lexA genes from Salmonella typhimurium, Erwinia carotovora, Pseudomonas aeruginosa and Pseudomonas putida. Mol Gen Genet. 1992 Dec;236(1):125–134. doi: 10.1007/BF00279651. [DOI] [PubMed] [Google Scholar]
  8. Higgins D. G., Bleasby A. J., Fuchs R. CLUSTAL V: improved software for multiple sequence alignment. Comput Appl Biosci. 1992 Apr;8(2):189–191. doi: 10.1093/bioinformatics/8.2.189. [DOI] [PubMed] [Google Scholar]
  9. Horii T., Ogawa T., Ogawa H. Nucleotide sequence of the lexA gene of E. coli. Cell. 1981 Mar;23(3):689–697. doi: 10.1016/0092-8674(81)90432-3. [DOI] [PubMed] [Google Scholar]
  10. Johnson A. D., Meyer B. J., Ptashne M. Interactions between DNA-bound repressors govern regulation by the lambda phage repressor. Proc Natl Acad Sci U S A. 1979 Oct;76(10):5061–5065. doi: 10.1073/pnas.76.10.5061. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Johnson A. D., Poteete A. R., Lauer G., Sauer R. T., Ackers G. K., Ptashne M. lambda Repressor and cro--components of an efficient molecular switch. Nature. 1981 Nov 19;294(5838):217–223. doi: 10.1038/294217a0. [DOI] [PubMed] [Google Scholar]
  12. Lakshmidevi G., Davidson B. E., Hillier A. J. Circular Permutation of the Genome of a Temperate Bacteriophage from Streptococcus cremoris BK5. Appl Environ Microbiol. 1988 Apr;54(4):1039–1045. doi: 10.1128/aem.54.4.1039-1045.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Lillehaug D., Birkeland N. K. Characterization of genetic elements required for site-specific integration of the temperate lactococcal bacteriophage phi LC3 and construction of integration-negative phi LC3 mutants. J Bacteriol. 1993 Mar;175(6):1745–1755. doi: 10.1128/jb.175.6.1745-1755.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Pabo C. O., Sauer R. T. Protein-DNA recognition. Annu Rev Biochem. 1984;53:293–321. doi: 10.1146/annurev.bi.53.070184.001453. [DOI] [PubMed] [Google Scholar]
  15. Pearson W. R., Lipman D. J. Improved tools for biological sequence comparison. Proc Natl Acad Sci U S A. 1988 Apr;85(8):2444–2448. doi: 10.1073/pnas.85.8.2444. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Phizicky E. M., Roberts J. W. Kinetics of RecA protein-directed inactivation of repressors of phage lambda and phage P22. J Mol Biol. 1980 May 25;139(3):319–328. doi: 10.1016/0022-2836(80)90133-3. [DOI] [PubMed] [Google Scholar]
  17. Poteete A. R., Ptashne M. Control of transcription by the bacteriophage P22 repressor. J Mol Biol. 1982 May 5;157(1):21–48. doi: 10.1016/0022-2836(82)90511-3. [DOI] [PubMed] [Google Scholar]
  18. Ptashne M., Backman K., Humayun M. Z., Jeffrey A., Maurer R., Meyer B., Sauer R. T. Autoregulation and function of a repressor in bacteriophage lambda. Science. 1976 Oct 8;194(4261):156–161. doi: 10.1126/science.959843. [DOI] [PubMed] [Google Scholar]
  19. Raymond-Denise A., Guillen N. Identification of dinR, a DNA damage-inducible regulator gene of Bacillus subtilis. J Bacteriol. 1991 Nov;173(22):7084–7091. doi: 10.1128/jb.173.22.7084-7091.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Reisner A. H., Westwood N. H. Assessment of similarities of pairs and groups of proteins using transformed amino-acid-residue data. J Mol Evol. 1982;18(4):240–250. doi: 10.1007/BF01734102. [DOI] [PubMed] [Google Scholar]
  21. Sauer R. T., Anderegg R. Primary structure of the lambda repressor. Biochemistry. 1978 Mar 21;17(6):1092–1100. doi: 10.1021/bi00599a024. [DOI] [PubMed] [Google Scholar]
  22. Sauer R. T., Jordan S. R., Pabo C. O. Lambda repressor: a model system for understanding protein-DNA interactions and protein stability. Adv Protein Chem. 1990;40:1–61. doi: 10.1016/s0065-3233(08)60286-7. [DOI] [PubMed] [Google Scholar]
  23. Sauer R. T., Pan J., Hopper P., Hehir K., Brown J., Poteete A. R. Primary structure of the phage P22 repressor and its gene c2. Biochemistry. 1981 Jun 9;20(12):3591–3598. doi: 10.1021/bi00515a044. [DOI] [PubMed] [Google Scholar]
  24. Shimada K., Campbell A. Int-constitutive mutants of bacteriophage lambda. Proc Natl Acad Sci U S A. 1974 Jan;71(1):237–241. doi: 10.1073/pnas.71.1.237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Slilaty S. N., Little J. W. Lysine-156 and serine-119 are required for LexA repressor cleavage: a possible mechanism. Proc Natl Acad Sci U S A. 1987 Jun;84(12):3987–3991. doi: 10.1073/pnas.84.12.3987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Susskind M. M., Botstein D. Molecular genetics of bacteriophage P22. Microbiol Rev. 1978 Jun;42(2):385–413. doi: 10.1128/mr.42.2.385-413.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. van Rooijen R. J., de Vos W. M. Molecular cloning, transcriptional analysis, and nucleotide sequence of lacR, a gene encoding the repressor of the lactose phosphotransferase system of Lactococcus lactis. J Biol Chem. 1990 Oct 25;265(30):18499–18503. [PubMed] [Google Scholar]
  28. van de Guchte M., Daly C., Fitzgerald G. F., Arendt E. K. Identification of int and attP on the genome of lactococcal bacteriophage Tuc2009 and their use for site-specific plasmid integration in the chromosome of Tuc2009-resistant Lactococcus lactis MG1363. Appl Environ Microbiol. 1994 Jul;60(7):2324–2329. doi: 10.1128/aem.60.7.2324-2329.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. van de Guchte M., Daly C., Fitzgerald G. F., Arendt E. K. Identification of the putative repressor-encoding gene cI of the temperate lactococcal bacteriophage Tuc2009. Gene. 1994 Jun 24;144(1):93–95. doi: 10.1016/0378-1119(94)90209-7. [DOI] [PubMed] [Google Scholar]
  30. van de Guchte M., Kok J., Venema G. Gene expression in Lactococcus lactis. FEMS Microbiol Rev. 1992 Feb;8(2):73–92. doi: 10.1111/j.1574-6968.1992.tb04958.x. [DOI] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES