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. 1994 Jun;60(6):1875–1883. doi: 10.1128/aem.60.6.1875-1883.1994

Molecular characterization of lactococcal bacteriophage Tuc2009 and identification and analysis of genes encoding lysin, a putative holin, and two structural proteins.

E K Arendt 1, C Daly 1, G F Fitzgerald 1, M van de Guchte 1
PMCID: PMC201575  PMID: 8031083

Abstract

Bacteriophage Tuc2009 is a temperate bacteriophage with a small isometric head and is isolated from Lactococcus lactis subsp. cremoris UC509. The phage genome is packaged by a headful mechanism, giving rise to circularly permuted molecules with terminal redundancy. The unit genome size is approximately 39 kb. A map of the phage genome on which several determinants could be localized was constructed: pac, the site of initiation of DNA packaging; lys (1,287 bp), specifying the phage lysin; S (267 bp), specifying a putative holin; and mp1 (522 bp) and mp2 (498 bp), each specifying one of the phage's structural proteins. lys, S, mp1, and mp2 were further characterized. lys and S are partially overlapping and appear to be part of one operon. The lysin shows homology to the lysins of the Streptococcus pneumoniae phages Cp-9, Cp-1, and Cp-7. The putative holin, which is thought to be involved in the release of lysin from the cytoplasm, contains two strongly hydrophobic presumptive transmembrane domains and a highly charged C-terminal domain.

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Selected References

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

  1. Altschul S. F., Gish W., Miller W., Myers E. W., Lipman D. J. Basic local alignment search tool. J Mol Biol. 1990 Oct 5;215(3):403–410. doi: 10.1016/S0022-2836(05)80360-2. [DOI] [PubMed] [Google Scholar]
  2. Birnboim H. C., Doly J. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 1979 Nov 24;7(6):1513–1523. doi: 10.1093/nar/7.6.1513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Boizet B., Lahbib-Mansais Y., Dupont L., Ritzenthaler P., Mata M. Cloning, expression and sequence analysis of an endolysin-encoding gene of Lactobacillus bulgaricus bacteriophage mv1. Gene. 1990 Sep 28;94(1):61–67. doi: 10.1016/0378-1119(90)90468-7. [DOI] [PubMed] [Google Scholar]
  4. Bradley D. E. Ultrastructure of bacteriophage and bacteriocins. Bacteriol Rev. 1967 Dec;31(4):230–314. doi: 10.1128/br.31.4.230-314.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Casjens S., Huang W. M., Hayden M., Parr R. Initiation of bacteriophage P22 DNA packaging series. Analysis of a mutant that alters the DNA target specificity of the packaging apparatus. J Mol Biol. 1987 Apr 5;194(3):411–422. doi: 10.1016/0022-2836(87)90671-1. [DOI] [PubMed] [Google Scholar]
  6. Chung D. K., Kim J. H., Batt C. A. Cloning and nucleotide sequence of the major capsid protein from Lactococcus lactis ssp. cremoris bacteriophage F4-1. Gene. 1991 May 15;101(1):121–125. doi: 10.1016/0378-1119(91)90233-2. [DOI] [PubMed] [Google Scholar]
  7. Díaz E., López R., García J. L. EJ-1, a temperate bacteriophage of Streptococcus pneumoniae with a Myoviridae morphotype. J Bacteriol. 1992 Sep;174(17):5516–5525. doi: 10.1128/jb.174.17.5516-5525.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Fitzgerlad G. F., Daly C., Brown L. R., Gingeras T. R. ScrFI: a new sequence-specific endonuclease from Streptococcus cremoris. Nucleic Acids Res. 1982 Dec 20;10(24):8171–8179. doi: 10.1093/nar/10.24.8171. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. García P., García J. L., García E., Sánchez-Puelles J. M., López R. Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Gene. 1990 Jan 31;86(1):81–88. doi: 10.1016/0378-1119(90)90116-9. [DOI] [PubMed] [Google Scholar]
  10. Jarvis A. W., Fitzgerald G. F., Mata M., Mercenier A., Neve H., Powell I. B., Ronda C., Saxelin M., Teuber M. Species and type phages of lactococcal bacteriophages. Intervirology. 1991;32(1):2–9. doi: 10.1159/000150179. [DOI] [PubMed] [Google Scholar]
  11. 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]
  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. McKay L. L., Baldwin K. A. Applications for biotechnology: present and future improvements in lactic acid bacteria. FEMS Microbiol Rev. 1990 Sep;7(1-2):3–14. doi: 10.1111/j.1574-6968.1990.tb04876.x. [DOI] [PubMed] [Google Scholar]
  14. Moran C. P., Jr, Lang N., LeGrice S. F., Lee G., Stephens M., Sonenshein A. L., Pero J., Losick R. Nucleotide sequences that signal the initiation of transcription and translation in Bacillus subtilis. Mol Gen Genet. 1982;186(3):339–346. doi: 10.1007/BF00729452. [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. Platteeuw C., de Vos W. M. Location, characterization and expression of lytic enzyme-encoding gene, lytA, of Lactococcus lactis bacteriophage phi US3. Gene. 1992 Sep 1;118(1):115–120. doi: 10.1016/0378-1119(92)90257-p. [DOI] [PubMed] [Google Scholar]
  17. Rottländer E., Trautner T. A. Genetic and transfection studies with B, subtilis phage SP 50. I. Phage mutants with restricted growth on B. subtilis strain 168. Mol Gen Genet. 1970;108(1):47–60. doi: 10.1007/BF00343184. [DOI] [PubMed] [Google Scholar]
  18. Shearman C., Underwood H., Jury K., Gasson M. Cloning and DNA sequence analysis of a Lactococcus bacteriophage lysin gene. Mol Gen Genet. 1989 Aug;218(2):214–221. doi: 10.1007/BF00331271. [DOI] [PubMed] [Google Scholar]
  19. Steiner M., Lubitz W., Bläsi U. The missing link in phage lysis of gram-positive bacteria: gene 14 of Bacillus subtilis phage phi 29 encodes the functional homolog of lambda S protein. J Bacteriol. 1993 Feb;175(4):1038–1042. doi: 10.1128/jb.175.4.1038-1042.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Studier F. W., Moffatt B. A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol. 1986 May 5;189(1):113–130. doi: 10.1016/0022-2836(86)90385-2. [DOI] [PubMed] [Google Scholar]
  21. Terzaghi B. E., Sandine W. E. Improved medium for lactic streptococci and their bacteriophages. Appl Microbiol. 1975 Jun;29(6):807–813. doi: 10.1128/am.29.6.807-813.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Vasala A., Dupont L., Baumann M., Ritzenthaler P., Alatossava T. Molecular comparison of the structural proteins encoding gene clusters of two related Lactobacillus delbrueckii bacteriophages. J Virol. 1993 Jun;67(6):3061–3068. doi: 10.1128/jvi.67.6.3061-3068.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Ward L. J., Beresford T. P., Lubbers M. W., Jarvis B. D., Jarvis A. W. Sequence analysis of the lysin gene region of the prolate lactococcal bacteriophage c2. Can J Microbiol. 1993 Aug;39(8):767–774. doi: 10.1139/m93-113. [DOI] [PubMed] [Google Scholar]
  24. Young R. Bacteriophage lysis: mechanism and regulation. Microbiol Rev. 1992 Sep;56(3):430–481. doi: 10.1128/mr.56.3.430-481.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. van de Guchte M., Kok J., Venema G. Distance-dependent translational coupling and interference in Lactococcus lactis. Mol Gen Genet. 1991 May;227(1):65–71. doi: 10.1007/BF00260708. [DOI] [PubMed] [Google Scholar]
  26. 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]
  27. van de Guchte M., van der Wal F. J., Kok J., Venema G. Lysozyme expression in Lactococcus lactis. Appl Microbiol Biotechnol. 1992 May;37(2):216–224. doi: 10.1007/BF00178174. [DOI] [PubMed] [Google Scholar]

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