Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1973 Jun;114(3):1151–1157. doi: 10.1128/jb.114.3.1151-1157.1973

Restriction and Modification of Bacteriophage S2 in Haemophilus influenzae

Rosa Gromkova 1, John Bendler 1, Sol Goodgal 1
PMCID: PMC285376  PMID: 4145862

Abstract

The major conclusion from these studies is that variants of Haemophilus influenzae Rd which restrict and modify phage S2 are metastable and capable of giving rise to one another with high frequency. Nonrestrictive RdS cells segregate spontaneously to the restricting, modifying phenotype in about 5% of the progeny of a single clone. The restrictive cells derived from RdS revert to the nonrestrictive phenotype in 15 to 25% of the progeny of a single clone. These frequencies are not appreciably affected by treatment with acriflavine or ethidium bromide, compounds which affect plasmid stability, or by nitrosoguanidine, a powerful mutagen. The genetic locus for restriction and modification of bacteriophage S2 is found to have a chromosomal position between the biotin and proline loci. Restriction-modification of phage S2 has been shown to be a function of its deoxyribonucleic acid (DNA) in that transfection with S2 phage DNA or prophage DNA is subject to host restriction and modification. An enzyme preparation, which contains endodeoxyribonuclease but no appreciable exonuclease activity, from mutant H. influenzae com−10 did not restrict phage S2·RdS DNA or prophage DNA transfecting activity, indicating that this endodeoxyribonuclease is not responsible for phage restriction. A new restriction enzyme isolated from H. influenzae Rd was found to be the major enzyme involved in the restriction of bacteriophage S2. The enzyme inactivated the transfecting activity of unmodified phage DNA but did not attack modified phage DNA. Unlike endodeoxyribonuclease R, this enzyme requires adenosine triphosphate and S-adenosylmethionine.

Full text

PDF
1151

Selected References

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

  1. ALEXANDER H. E., LEIDY G. Induction of streptomycin resistance in sensitive Hemophilus influenzae by extracts containing desoxyribonucleic acid from resistant Hemophilus influenzae. J Exp Med. 1953 Jan;97(1):17–31. doi: 10.1084/jem.97.1.17. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Arber W., Linn S. DNA modification and restriction. Annu Rev Biochem. 1969;38:467–500. doi: 10.1146/annurev.bi.38.070169.002343. [DOI] [PubMed] [Google Scholar]
  3. BARNHART B. J., HERRIOTT R. M. PENETRATION OF DEOXYRIBONUCLEIC ACID INTO HEMOPHILUS INFLUENZAE. Biochim Biophys Acta. 1963 Sep 17;76:25–39. [PubMed] [Google Scholar]
  4. BERNS K. I., THOMAS C. A., Jr ISOLATION OF HIGH MOLECULAR WEIGHT DNA FROM HEMOPHILUS INFLUENZAE. J Mol Biol. 1965 Mar;11:476–490. doi: 10.1016/s0022-2836(65)80004-3. [DOI] [PubMed] [Google Scholar]
  5. Bouanchaud D. H., Scavizzi M. R., Chabbert Y. A. Elimination by ethidium bromide of antibiotic resistance in enterobacteria and staphylococci. J Gen Microbiol. 1968 Dec;54(3):417–425. doi: 10.1099/00221287-54-3-417. [DOI] [PubMed] [Google Scholar]
  6. Caster J. H., Postel E. H., Goodgal S. H. Competence mutants: isolation of transformation deficient strains of Haemophilus influenzae. Nature. 1970 Aug 1;227(5257):515–517. doi: 10.1038/227515a0. [DOI] [PubMed] [Google Scholar]
  7. Catlin B. W., Bendler J. W., 3rd, Goodgal S. H. The type b capsulation locus of Haemophilus influenzae: map location and size. J Gen Microbiol. 1972 May;70(3):411–422. doi: 10.1099/00221287-70-3-411. [DOI] [PubMed] [Google Scholar]
  8. DUSSOIX D., ARBER W. Host specificity of DNA produced by Escherichia coli. II. Control over acceptance of DNA from infecting phage lambda. J Mol Biol. 1962 Jul;5:37–49. doi: 10.1016/s0022-2836(62)80059-x. [DOI] [PubMed] [Google Scholar]
  9. Eisen H., Pereira da Silva L., Jacob F. The regulation and mechanism of DNA synthesis in bacteriophage lambda. Cold Spring Harb Symp Quant Biol. 1968;33:755–764. doi: 10.1101/sqb.1968.033.01.086. [DOI] [PubMed] [Google Scholar]
  10. GOODGAL S. H., HERRIOTT R. M. Studies on transformations of Hemophilus influenzae. I. Competence. J Gen Physiol. 1961 Jul;44:1201–1227. doi: 10.1085/jgp.44.6.1201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Glover S. W., Piekarowicz A. Host specificity of DNA in Haemophilus influenzae: restriction and modification in strain Rd. Biochem Biophys Res Commun. 1972 Feb 25;46(4):1610–1617. doi: 10.1016/0006-291x(72)90793-0. [DOI] [PubMed] [Google Scholar]
  12. Gromkova R., Goodgal S. H. Action of haemophilus endodeoxyribonuclease on biologically active deoxyribonucleic acid. J Bacteriol. 1972 Mar;109(3):987–992. doi: 10.1128/jb.109.3.987-992.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Gunther J. K., Goodgal S. H. An exonuclease specific for double stranded deoxyribonucleic acid. J Biol Chem. 1970 Oct 25;245(20):5341–5349. [PubMed] [Google Scholar]
  14. HARM W., RUPERT C. S. INFECTION OF TRANSFORMABLE CELLS OF HAEMOPHILUS INFLUENZAE BY BACTERIOPHAGE AND BACTERIOPHAGE DNA. Z Vererbungsl. 1963 Dec 30;94:336–348. doi: 10.1007/BF00897593. [DOI] [PubMed] [Google Scholar]
  15. HIROTA Y., LIJIMA T. Acriflavine as an effective agent for eliminating F-factor in Escherichia coli K-12. Nature. 1957 Sep 28;180(4587):655–656. doi: 10.1038/180655a0. [DOI] [PubMed] [Google Scholar]
  16. Iino T. Genetics and chemistry of bacterial flagella. Bacteriol Rev. 1969 Dec;33(4):454–475. doi: 10.1128/br.33.4.454-475.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Lederberg J, Iino T. Phase Variation in Salmonella. Genetics. 1956 Sep;41(5):743–757. doi: 10.1093/genetics/41.5.743. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Meselson M., Yuan R. DNA restriction enzyme from E. coli. Nature. 1968 Mar 23;217(5134):1110–1114. doi: 10.1038/2171110a0. [DOI] [PubMed] [Google Scholar]
  19. Michalka J., Goodgal S. H. Genetic and physical map of the chromosome of Hemophilus influenzae. J Mol Biol. 1969 Oct 28;45(2):407–421. doi: 10.1016/0022-2836(69)90115-6. [DOI] [PubMed] [Google Scholar]
  20. Neubauer Z., Calef E. Immunity phase-shift in defective lysogens: non-mutational hereditary change of early regulation of lambda prophage. J Mol Biol. 1970 Jul 14;51(1):1–13. doi: 10.1016/0022-2836(70)90265-2. [DOI] [PubMed] [Google Scholar]
  21. Piekarowicz A., Glover S. W. Host specificity of DNA in Haemophilus influenzae: the two restriction and modification systems in strain Ra. Mol Gen Genet. 1972;116(1):11–25. doi: 10.1007/BF00334255. [DOI] [PubMed] [Google Scholar]
  22. Setlow J. K., Randolph M. L., Boling M. E., Mattingly A., Price G., Gordon M. P. Repair of DNA in Haemophilus influenzae. II. Excision, repair of single-strand breaks, defects in transformation, and host cell modification in UV-sensitive mutants. Cold Spring Harb Symp Quant Biol. 1968;33:209–218. doi: 10.1101/sqb.1968.033.01.024. [DOI] [PubMed] [Google Scholar]
  23. Smith H. O., Wilcox K. W. A restriction enzyme from Hemophilus influenzae. I. Purification and general properties. J Mol Biol. 1970 Jul 28;51(2):379–391. doi: 10.1016/0022-2836(70)90149-x. [DOI] [PubMed] [Google Scholar]
  24. Stuy J. H. Phage resistance in Haemophilus influenzae. Biochem Biophys Res Commun. 1968 Nov 25;33(4):682–687. doi: 10.1016/0006-291x(68)90350-1. [DOI] [PubMed] [Google Scholar]

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

RESOURCES