Skip to main content
NCBI home page
Microbiological Reviews logoLink to Microbiological Reviews
. 1978 Jun;42(2):385–413. doi: 10.1128/mr.42.2.385-413.1978

Molecular genetics of bacteriophage P22.

M M Susskind, D Botstein
PMCID: PMC281435  PMID: 353481

Full text

PDF
385

Selected References

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

  1. Adhya S., Gottesman M., De Crombrugghe B. Release of polarity in Escherichia coli by gene N of phage lambda: termination and antitermination of transcription. Proc Natl Acad Sci U S A. 1974 Jun;71(6):2534–2538. doi: 10.1073/pnas.71.6.2534. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Barksdale L., Arden S. B. Persisting bacteriophage infections, lysogeny, and phage conversions. Annu Rev Microbiol. 1974;28(0):265–299. doi: 10.1146/annurev.mi.28.100174.001405. [DOI] [PubMed] [Google Scholar]
  3. Bertrand K., Yanofsky C. Regulation of transcription termination in the leader region of the tryptophan operon of Escherichia coli involves tryptophan or its metabolic product. J Mol Biol. 1976 May 15;103(2):339–349. doi: 10.1016/0022-2836(76)90316-8. [DOI] [PubMed] [Google Scholar]
  4. Bezdek M., Amati P. Evidence for two immunity regulator systems in temperature bacteriophages P22 and L. Virology. 1968 Dec;36(4):701–703. doi: 10.1016/0042-6822(68)90208-0. [DOI] [PubMed] [Google Scholar]
  5. Blattner F. R., Dahlberg J. E. RNA synthesis startpoints in bacteriophage lambda: are the promoter and operator transcribed? Nat New Biol. 1972 Jun 21;237(77):227–232. doi: 10.1038/newbio237227a0. [DOI] [PubMed] [Google Scholar]
  6. Botstein D., Chan R. K., Waddell C. H. Genetics of bacteriophage P22. II. Gene order and gene function. Virology. 1972 Jul;49(1):268–282. doi: 10.1016/s0042-6822(72)80028-x. [DOI] [PubMed] [Google Scholar]
  7. Botstein D., Herskowitz I. Properties of hybrids between Salmonella phage P22 and coliphage lambda. Nature. 1974 Oct 18;251(5476):584–589. doi: 10.1038/251584a0. [DOI] [PubMed] [Google Scholar]
  8. Botstein D., Levine M. Synthesis and maturation of phage P22 DNA. II. Properties of temperature-sensitive phage mutants defective in DNA metabolism. J Mol Biol. 1968 Jun 28;34(3):643–654. doi: 10.1016/0022-2836(68)90186-1. [DOI] [PubMed] [Google Scholar]
  9. Botstein D., Matz M. J. A recombination function essential to the growth of bacteriophage P22. J Mol Biol. 1970 Dec 28;54(3):417–440. doi: 10.1016/0022-2836(70)90119-1. [DOI] [PubMed] [Google Scholar]
  10. Botstein D. Synthesis and maturation of phage P22 DNA. I. Identification of intermediates. J Mol Biol. 1968 Jun 28;34(3):621–641. doi: 10.1016/0022-2836(68)90185-x. [DOI] [PubMed] [Google Scholar]
  11. Botstein D., Waddell C. H., King J. Mechanism of head assembly and DNA encapsulation in Salmonella phage p22. I. Genes, proteins, structures and DNA maturation. J Mol Biol. 1973 Nov 15;80(4):669–695. doi: 10.1016/0022-2836(73)90204-0. [DOI] [PubMed] [Google Scholar]
  12. Botstein K., Lew K. K., Jarvik V., Swanson C. A. Role of antirepressor in the bipartite control of repression and immunity by bacteriophage P22. J Mol Biol. 1975 Feb 5;91(4):439–462. doi: 10.1016/0022-2836(75)90271-5. [DOI] [PubMed] [Google Scholar]
  13. Bronson M. J., Levine M. Virulent mutants of bacteriophage p22.I. Isolation and genetic analysis. J Virol. 1971 May;7(5):559–568. doi: 10.1128/jvi.7.5.559-568.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Bronson M. J., Levine M. Virulent mutants of phage P22. II. Physiological analysis of P22 virB-3 and its component mutations. Virology. 1972 Mar;47(3):644–655. doi: 10.1016/0042-6822(72)90554-5. [DOI] [PubMed] [Google Scholar]
  15. Casjens S., King J. P22 morphogenesis. I: Catalytic scaffolding protein in capsid assembly. J Supramol Struct. 1974;2(2-4):202–224. doi: 10.1002/jss.400020215. [DOI] [PubMed] [Google Scholar]
  16. Chan R. K., Botstein D. Genetics of bacteriophage P22. I. Isolation of prophage deletions which affect immunity to superinfection. Virology. 1972 Jul;49(1):257–267. doi: 10.1016/s0042-6822(72)80027-8. [DOI] [PubMed] [Google Scholar]
  17. Chan R. K., Botstein D. Specialized transduction by bacteriophage P22 in Salmonella typhimurium: genetic and physical structure of the transducing genomes and the prophage attachment site. Genetics. 1976 Jul;83(3 PT2):433–458. [PMC free article] [PubMed] [Google Scholar]
  18. Chan R. K., Botstein D., Watanabe T., Ogata Y. Specialized transduction of tetracycline resistance by phage P22 in Salmonella typhimurium. II. Properties of a high-frequency-transducing lysate. Virology. 1972 Dec;50(3):883–898. doi: 10.1016/0042-6822(72)90442-4. [DOI] [PubMed] [Google Scholar]
  19. Chelala C. A., Margolin P. Effects of deletions on cotransduction linkage in Salmonella typhimurium: evidence that bacterial chromosome deletions affect the formation of transducing DNA fragments. Mol Gen Genet. 1974;131(2):97–112. doi: 10.1007/BF00266146. [DOI] [PubMed] [Google Scholar]
  20. Cowie D. B., Szafranski P. Thermal chromatography of DNA-DNA reactions. Biophys J. 1967 Sep;7(5):567–584. doi: 10.1016/S0006-3495(67)86607-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. DUBNAU E., STOCKER B. A. GENETICS OF PLASMIDS IN SALMONELLA TYPHIMURIUM. Nature. 1964 Dec 12;204:1112–1113. doi: 10.1038/2041112a0. [DOI] [PubMed] [Google Scholar]
  22. Dopatka H. D., Prell H. H. Amber mutants of Salmonella-phage P22 in genes engaged in the establishment of lysogeny. Mol Gen Genet. 1973 Jan 24;120(2):157–170. doi: 10.1007/BF00267244. [DOI] [PubMed] [Google Scholar]
  23. Earnshaw W., Casjens S., Harrison S. C. Assembly of the head of bacteriophage P22: x-ray diffraction from heads, proheads and related structures. J Mol Biol. 1976 Jun 25;104(2):387–410. doi: 10.1016/0022-2836(76)90278-3. [DOI] [PubMed] [Google Scholar]
  24. Ebel-Tsipis J., Botstein D., Fox M. S. Generalized transduction by phage P22 in Salmonella typhimurium. I. Molecular origin of transducing DNA. J Mol Biol. 1972 Nov 14;71(2):433–448. doi: 10.1016/0022-2836(72)90361-0. [DOI] [PubMed] [Google Scholar]
  25. Ebel-Tsipis J., Botstein D. Superinfection exclusion by P22 prophage in lysogens of Salmonella typhimurium. 1. Exclusion of generalized transducing particles. Virology. 1971 Sep;45(3):629–637. doi: 10.1016/0042-6822(71)90177-2. [DOI] [PubMed] [Google Scholar]
  26. Ebel-Tsipis J., Fox M. S., Botstein D. Generalized transduction by bacteriophage P22 in Salmonella typhimurium. II. Mechanism of integration of transducing DNA. J Mol Biol. 1972 Nov 14;71(2):449–469. doi: 10.1016/0022-2836(72)90362-2. [DOI] [PubMed] [Google Scholar]
  27. Echols H. Developmental pathways for the temperate phage: lysis vs lysogeny,. Annu Rev Genet. 1972;6(0):157–190. doi: 10.1146/annurev.ge.06.120172.001105. [DOI] [PubMed] [Google Scholar]
  28. Enomoto M. Composition of chromosome fragments participating in phage P22-mediated transduction of Salmonella typhimurium. Virology. 1967 Nov;33(3):474–482. doi: 10.1016/0042-6822(67)90123-7. [DOI] [PubMed] [Google Scholar]
  29. FUKAZAWA Y., HARTMAN P. E. A P22 BACTERIOPHAGE MUTANT DEFECTIVE IN ANTIGEN CONVERSION. Virology. 1964 Jun;23:279–283. doi: 10.1016/0042-6822(64)90296-x. [DOI] [PubMed] [Google Scholar]
  30. Feiss M., Fisher R. A., Crayton M. A., Egner C. Packaging of the bacteriophage lambda chromosome: effect of chromosome length. Virology. 1977 Mar;77(1):281–293. doi: 10.1016/0042-6822(77)90425-1. [DOI] [PubMed] [Google Scholar]
  31. Franklin N. C. Altered reading of genetic signals fused to the N operon of bacteriophage lambda: genetic evidence for modification of polymerase by the protein product of the N gene. J Mol Biol. 1974 Oct 15;89(1):33–48. doi: 10.1016/0022-2836(74)90161-2. [DOI] [PubMed] [Google Scholar]
  32. Friedman D. I., Ponce-Campos R. Differential effect of phage regulator functions on transcription from various promoters: evidence that the P22 gene 24 and the lambda gene N products distinguish three classes of promoters. J Mol Biol. 1975 Nov 5;98(3):537–549. doi: 10.1016/s0022-2836(75)80085-4. [DOI] [PubMed] [Google Scholar]
  33. Gemski P., Jr, Baron L. S., Yamamoto N. Formation of hybrids between coliphage lambda and Salmonella phage P22 with a Salmonella typhimurium hybrid sensitive to these phages. Proc Natl Acad Sci U S A. 1972 Nov;69(11):3110–3114. doi: 10.1073/pnas.69.11.3110. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Gilbert W., Dressler D. DNA replication: the rolling circle model. Cold Spring Harb Symp Quant Biol. 1968;33:473–484. doi: 10.1101/sqb.1968.033.01.055. [DOI] [PubMed] [Google Scholar]
  35. Gottesman M. M., Gottesman M. E., Gottesman S., Gellert M. Characterization of bacteriophage lambda reverse as an Escherichia coli phage carrying a unique set of host-derived recombination functions. J Mol Biol. 1974 Sep 15;88(2):471–487. doi: 10.1016/0022-2836(74)90496-3. [DOI] [PubMed] [Google Scholar]
  36. Gough M., Levine M. The circularity of the phage P22 linkage map. Genetics. 1968 Feb;58(2):161–169. doi: 10.1093/genetics/58.2.161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Gough M., Scott J. V. Location of the prophage conversion gene of P22. Virology. 1972 Nov;50(2):603–605. doi: 10.1016/0042-6822(72)90411-4. [DOI] [PubMed] [Google Scholar]
  38. Gough M. Second locus of bacteriophage P22 necessary for the maintenance of lysogeny. J Virol. 1968 Oct;2(10):992–998. doi: 10.1128/jvi.2.10.992-998.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Gough M., Tokuno S. Further structural and functional analogies between the repressor regions of phages P22 and lambda. Mol Gen Genet. 1975;138(1):71–79. doi: 10.1007/BF00268829. [DOI] [PubMed] [Google Scholar]
  40. Herskowitz I. Control of gene expression in bacteriophage lambda. Annu Rev Genet. 1973;7:289–324. doi: 10.1146/annurev.ge.07.120173.001445. [DOI] [PubMed] [Google Scholar]
  41. Herskowitz I., Signer E. R. A site essential for expression of all late genes in bacteriophage lambda. J Mol Biol. 1970 Feb 14;47(3):545–556. doi: 10.1016/0022-2836(70)90321-9. [DOI] [PubMed] [Google Scholar]
  42. Herskowitz I., Signer E. R. Substitution mutation in bacteriophage lambda with new specificity for late gene expression. Virology. 1974 Sep;61(1):112–119. doi: 10.1016/0042-6822(74)90246-3. [DOI] [PubMed] [Google Scholar]
  43. Hilliker S., Botstein D. An early regulatory gene of Salmonella phage P22 analogous to gene N of coliphage lambda. Virology. 1975 Dec;68(2):510–524. doi: 10.1016/0042-6822(75)90291-3. [DOI] [PubMed] [Google Scholar]
  44. Hilliker S., Botstein D. Specificity of genetic elements controlling regulation of early functions in temperate bacteriophages. J Mol Biol. 1976 Sep 25;106(3):537–566. doi: 10.1016/0022-2836(76)90251-5. [DOI] [PubMed] [Google Scholar]
  45. Hoffman B., Levine M. Bacteriophage P22 virion protein which performs an essential early function. I. Analysis of 16-ts mutants. J Virol. 1975 Dec;16(6):1536–1546. doi: 10.1128/jvi.16.6.1536-1546.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Hoffman B., Levine M. Bacteriophage P22 virion protein which performs an essential early function. II. Characterization of the gene 16 function. J Virol. 1975 Dec;16(6):1547–1559. doi: 10.1128/jvi.16.6.1547-1559.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Hong J. S., Smith G. R., Ames B. N. Adenosine 3':5'-cyclic monophosphate concentration in the bacterial host regulates the viral decision between lysogeny and lysis. Proc Natl Acad Sci U S A. 1971 Sep;68(9):2258–2262. doi: 10.1073/pnas.68.9.2258. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Honigman A., Oppenheim A., Oppenheim A. B. A pleiotropic regulatory mutation in lambda bacteriophage. Mol Gen Genet. 1975;138(2):85–111. doi: 10.1007/BF02428115. [DOI] [PubMed] [Google Scholar]
  49. Hoppe I., Roth J. Specialized transducing phages derived from salmonella phage P22. Genetics. 1974 Apr;76(4):633–654. doi: 10.1093/genetics/76.4.633. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Israel J. V., Anderson T. F., Levine M. in vitro MORPHOGENESIS OF PHAGE P22 FROM HEADS AND BASE-PLATE PARTS. Proc Natl Acad Sci U S A. 1967 Feb;57(2):284–291. doi: 10.1073/pnas.57.2.284. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Israel V. E proteins of bacteriophage P22. I. Identification and ejection from wild-type and defective particles. J Virol. 1977 Jul;23(1):91–97. doi: 10.1128/jvi.23.1.91-97.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Israel V., Rosen H., Levine M. Binding of bacteriophage P22 tail parts to cells. J Virol. 1972 Dec;10(6):1152–1158. doi: 10.1128/jvi.10.6.1152-1158.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Iwashita S., Kanegasaki S. Smooth specific phage adsorption: endorhamnosidase activity of tail parts of P22. Biochem Biophys Res Commun. 1973 Nov 16;55(2):403–409. doi: 10.1016/0006-291x(73)91101-7. [DOI] [PubMed] [Google Scholar]
  54. Jackson E. N., Jackson D. A., Deans R. J. EcoRI analysis of bacteriophage P22 DNA packaging. J Mol Biol. 1978 Jan 25;118(3):365–388. doi: 10.1016/0022-2836(78)90234-6. [DOI] [PubMed] [Google Scholar]
  55. Jackson E. N., Miller H. I., Adams M. L. EcoRI restriction endonuclease cleavage site map of bacteriophage P22DNA. J Mol Biol. 1978 Jan 25;118(3):347–363. doi: 10.1016/0022-2836(78)90233-4. [DOI] [PubMed] [Google Scholar]
  56. Jarvik J., Botstein D. A genetic method for determining the order of events in a biological pathway. Proc Natl Acad Sci U S A. 1973 Jul;70(7):2046–2050. doi: 10.1073/pnas.70.7.2046. [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. Jarvik J., Botstein D. Conditional-lethal mutations that suppress genetic defects in morphogenesis by altering structural proteins. Proc Natl Acad Sci U S A. 1975 Jul;72(7):2738–2742. doi: 10.1073/pnas.72.7.2738. [DOI] [PMC free article] [PubMed] [Google Scholar]
  58. Jessop A. P. A specialised transducing phage of P22 for which the ability to form plagues is associated with transduction of the proAB region. Mol Gen Genet. 1972;114(3):214–222. doi: 10.1007/BF01788890. [DOI] [PubMed] [Google Scholar]
  59. Jessop A. P. Specialized transducing phages derived from phage P22 that carry the pro AB region of the host, Salmonella typhimurium: genetic evidence for their structure and mode of transduction. Genetics. 1976 Jul;83(3 PT2):459–475. [PMC free article] [PubMed] [Google Scholar]
  60. KAISER A. D. Mutations in a temperate bacteriophage affecting its ability to lysogenize Escherichia coli. Virology. 1957 Feb;3(1):42–61. doi: 10.1016/0042-6822(57)90022-3. [DOI] [PubMed] [Google Scholar]
  61. Kaiser D., Masuda T. In vitro assembly of bacteriophage Lambda heads. Proc Natl Acad Sci U S A. 1973 Jan;70(1):260–264. doi: 10.1073/pnas.70.1.260. [DOI] [PMC free article] [PubMed] [Google Scholar]
  62. Kaye R., Barravecchio J., Roth J. Isolation of P22 specialized transducing phage followong F'-episome fusion. Genetics. 1974 Apr;76(4):655–667. doi: 10.1093/genetics/76.4.655. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Kemper J. Gene order and co-transduction in the leu-ara-fol-pyrA region of the Salmonella typhimurium linkage map. J Bacteriol. 1974 Jan;117(1):94–99. doi: 10.1128/jb.117.1.94-99.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. King J., Casjens S. Catalytic head assembling protein in virus morphogenesis. Nature. 1974 Sep 13;251(5471):112–119. doi: 10.1038/251112a0. [DOI] [PubMed] [Google Scholar]
  65. King J., Lenk E. V., Botstein D. Mechanism of head assembly and DNA encapsulation in Salmonella phage P22. II. Morphogenetic pathway. J Mol Biol. 1973 Nov 15;80(4):697–731. doi: 10.1016/0022-2836(73)90205-2. [DOI] [PubMed] [Google Scholar]
  66. Kleckner N., Chan R. K., Tye B. K., Botstein D. Mutagenesis by insertion of a drug-resistance element carrying an inverted repetition. J Mol Biol. 1975 Oct 5;97(4):561–575. doi: 10.1016/s0022-2836(75)80059-3. [DOI] [PubMed] [Google Scholar]
  67. Kleckner N. Translocatable elements in procaryotes. Cell. 1977 May;11(1):11–23. doi: 10.1016/0092-8674(77)90313-0. [DOI] [PubMed] [Google Scholar]
  68. LEVINE M., CURTISS R. Genetic fine structure of the C region and the linkage map of phage P22. Genetics. 1961 Dec;46:1573–1580. doi: 10.1093/genetics/46.12.1573. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. LEVINE M. Mutations in the temperate phage P22 and lysogeny in Salmonella. Virology. 1957 Feb;3(1):22–41. doi: 10.1016/0042-6822(57)90021-1. [DOI] [PubMed] [Google Scholar]
  70. LEVINE M., SMITH H. O. SEQUENTIAL GENE ACTION IN THE ESTABLISHMENT OF LYSOGENY. Science. 1964 Dec 18;146(3651):1581–1582. doi: 10.1126/science.146.3651.1581. [DOI] [PubMed] [Google Scholar]
  71. Lee F., Squires C. L., Squires C., Yanofsky C. Termination of transcription in vitro in the Escherichia coli tryptophan operon leader region. J Mol Biol. 1976 May 15;103(2):383–393. doi: 10.1016/0022-2836(76)90318-1. [DOI] [PubMed] [Google Scholar]
  72. Levine M., Schott C. Mutations of phage P22 affecting phage DNA synthesis and lysogenization. J Mol Biol. 1971 Nov 28;62(1):53–64. doi: 10.1016/0022-2836(71)90130-6. [DOI] [PubMed] [Google Scholar]
  73. Levine M., Truesdell S., Ramakrishnan T., Bronson M. J. Dual control of lysogeny by bacteriophage P22: an antirepressor locus and its controlling elements. J Mol Biol. 1975 Feb 5;91(4):421–438. doi: 10.1016/0022-2836(75)90270-3. [DOI] [PubMed] [Google Scholar]
  74. Lew K., Casjens S. Identification of early proteins coded by bacteriophage P22. Virology. 1975 Dec;68(2):525–533. doi: 10.1016/0042-6822(75)90292-5. [DOI] [PubMed] [Google Scholar]
  75. Oppenheim A. Suppression of a Pm mutant by the sar mutation for the synthesis of repressor by bacteriophage lambda. J Mol Biol. 1977 Mar 25;111(1):83–89. doi: 10.1016/s0022-2836(77)80134-4. [DOI] [PubMed] [Google Scholar]
  76. Ozeki H. Chromosome Fragments Participating in Transduction in Salmonella Typhimurium. Genetics. 1959 May;44(3):457–470. doi: 10.1093/genetics/44.3.457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  77. Pearce U., Stocker B. A. Variation in composition of chromosome fragments transduced by phage P22. Virology. 1965 Nov;27(3):290–296. doi: 10.1016/0042-6822(65)90108-x. [DOI] [PubMed] [Google Scholar]
  78. Pipas J. M., Reeves R. H. Patterns of transcription in bacteriophage P22-infected Salmonella typhimurium. J Virol. 1977 Feb;21(2):825–828. doi: 10.1128/jvi.21.2.825-828.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Poteete A. R., King J. Functions of two new genes in Salmonella phage P22 assembly. Virology. 1977 Feb;76(2):725–739. doi: 10.1016/0042-6822(77)90254-9. [DOI] [PubMed] [Google Scholar]
  80. Radding C. M., Szpirer J., Thomas R. THE STRUCTURAL GENE FOR lambda EXONUCLEASE. Proc Natl Acad Sci U S A. 1967 Feb;57(2):277–283. doi: 10.1073/pnas.57.2.277. [DOI] [PMC free article] [PubMed] [Google Scholar]
  81. Raj A. S., Raj A. Y., Schmieger H. Phage genes involved in the formation generalized transducing particles in Salmonella--Phage P22. Mol Gen Genet. 1974;135(2):175–184. doi: 10.1007/BF00264784. [DOI] [PubMed] [Google Scholar]
  82. Rao G. R., Burma D. P. Purification and properties of phage P22-induced lysozyme. J Biol Chem. 1971 Nov;246(21):6474–6479. [PubMed] [Google Scholar]
  83. Rao R. N. Bacteriophage P22 controlled exclusion in Salmonella typhimurium. J Mol Biol. 1968 Aug 14;35(3):607–622. doi: 10.1016/s0022-2836(68)80017-8. [DOI] [PubMed] [Google Scholar]
  84. Rao R. N., Smith H. O. Phage P22 lysogens of a Salmonella typhimurium mutant deleted at the normal prophage attachment site. Virology. 1968 Oct;36(2):328–330. doi: 10.1016/0042-6822(68)90157-8. [DOI] [PubMed] [Google Scholar]
  85. Reichardt L., Kaiser A. D. Control of lambda repressor synthesis. Proc Natl Acad Sci U S A. 1971 Sep;68(9):2185–2189. doi: 10.1073/pnas.68.9.2185. [DOI] [PMC free article] [PubMed] [Google Scholar]
  86. Rhoades M., MacHattie L. A., Thomas C. A., Jr The P22 bacteriophage DNA molecule. I. The mature form. J Mol Biol. 1968 Oct 14;37(1):21–40. doi: 10.1016/0022-2836(68)90071-5. [DOI] [PubMed] [Google Scholar]
  87. Rhoades M., Thomas C. A., Jr The P22 bacteriophage DNA molecule. II. Circular intracellular forms. J Mol Biol. 1968 Oct 14;37(1):41–61. doi: 10.1016/0022-2836(68)90072-7. [DOI] [PubMed] [Google Scholar]
  88. Roberts J. W., Roberts C. W. Proteolytic cleavage of bacteriophage lambda repressor in induction. Proc Natl Acad Sci U S A. 1975 Jan;72(1):147–151. doi: 10.1073/pnas.72.1.147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  89. Roberts J. W. Transcription termination and late control in phage lambda. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3300–3304. doi: 10.1073/pnas.72.9.3300. [DOI] [PMC free article] [PubMed] [Google Scholar]
  90. Roth J. R., Hartman P. E. Heterogeneity in P22 transducing particles. Virology. 1965 Nov;27(3):297–307. doi: 10.1016/0042-6822(65)90109-1. [DOI] [PubMed] [Google Scholar]
  91. SMITH H. O., LEVINE M. TWO SEQUENTIAL REPRESSIONS OF DNA SYNTHESIS IN THE ESTABLISHMENT OF LYSOGENY BY PHAGE P22 AND ITS MUTANTS. Proc Natl Acad Sci U S A. 1964 Aug;52:356–363. doi: 10.1073/pnas.52.2.356. [DOI] [PMC free article] [PubMed] [Google Scholar]
  92. STOCKER B. A. Transduction of flagellar characters in Salmonella. J Gen Microbiol. 1953 Dec;9(3):410–433. doi: 10.1099/00221287-9-3-410. [DOI] [PubMed] [Google Scholar]
  93. STREISINGER G., EDGAR R. S., DENHARDT G. H. CHROMOSOME STRUCTURE IN PHAGE T4. I. CIRCULARITY OF THE LINKAGE MAP. Proc Natl Acad Sci U S A. 1964 May;51:775–779. doi: 10.1073/pnas.51.5.775. [DOI] [PMC free article] [PubMed] [Google Scholar]
  94. Schmieger H., Backhaus H. Altered cotransduction frequencies exhibited by HT-mutants of Salmonella-phage P22. Mol Gen Genet. 1976 Feb 2;143(3):307–309. doi: 10.1007/BF00269408. [DOI] [PubMed] [Google Scholar]
  95. Schmieger H. The molecular structure of the transducing particles of Salmonella phage P22. II. Density gradient analysis of DNA. Mol Gen Genet. 1970;109(4):323–337. doi: 10.1007/BF00267702. [DOI] [PubMed] [Google Scholar]
  96. Schumann W., Lindenblatt E., Bade E. G. Bacteriophage-specific DNA-binding proteins in P22-lysogenic and in P22-infected Salmonella typhimurium. J Virol. 1976 Oct;20(1):334–338. doi: 10.1128/jvi.20.1.334-338.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  97. Skalka S. A., Hanson P. Comparisons of the distribution of nucleotides and common sequences in deoxyribonucleic acid from selected bacteriophages. J Virol. 1972 Apr;9(4):583–593. doi: 10.1128/jvi.9.4.583-593.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  98. Smith-Keary P. F. Restricted trandsuction by bacteriophage P22 in Salmonella typhimurium. Genet Res. 1966 Aug;8(1):73–82. doi: 10.1017/s0016672300009927. [DOI] [PubMed] [Google Scholar]
  99. Smith H. O. Defective phage formation by lysogens of integration deficient phage P22 mutants. Virology. 1968 Feb;34(2):203–223. doi: 10.1016/0042-6822(68)90231-6. [DOI] [PubMed] [Google Scholar]
  100. Smith H. O., Levine M. A phage P22 gene controlling integration of prophage. Virology. 1967 Feb;31(2):207–216. doi: 10.1016/0042-6822(67)90164-x. [DOI] [PubMed] [Google Scholar]
  101. Smith H. O., Levine M. Gene order in prophage P22. Virology. 1965 Oct;27(2):229–231. doi: 10.1016/0042-6822(65)90166-2. [DOI] [PubMed] [Google Scholar]
  102. Streisinger G., Emrich J., Stahl M. M. Chromosome structure in phage t4, iii. Terminal redundancy and length determination. Proc Natl Acad Sci U S A. 1967 Feb;57(2):292–295. doi: 10.1073/pnas.57.2.292. [DOI] [PMC free article] [PubMed] [Google Scholar]
  103. Susskind M. M., Botstein D. Mechanism of action of Salmonella phage P22 antirepressor. J Mol Biol. 1975 Oct 25;98(2):413–424. doi: 10.1016/s0022-2836(75)80127-6. [DOI] [PubMed] [Google Scholar]
  104. Susskind M. M., Botstein D., Wright A. Superinfection exclusion by P22 prophage in lysogens of Salmonella typhimurium. III. Failure of superinfecting phage DNA to enter sieA+ lysogens. Virology. 1974 Dec;62(2):350–366. doi: 10.1016/0042-6822(74)90398-5. [DOI] [PubMed] [Google Scholar]
  105. Susskind M. M., Wright A., Botstein D. Superinfection exclusion by P22 prophage in lysogens of Salmonella typhimurium. II. Genetic evidence for two exclusion systems. Virology. 1971 Sep;45(3):638–652. doi: 10.1016/0042-6822(71)90178-4. [DOI] [PubMed] [Google Scholar]
  106. Susskind M. M., Wright A., Botstein D. Superinfection exclusion by P22 prophage in lysogens of Salmonella typhimurium. IV. Genetics and physiology of sieB exclusion. Virology. 1974 Dec;62(2):367–384. doi: 10.1016/0042-6822(74)90399-7. [DOI] [PubMed] [Google Scholar]
  107. Szpirer J., Thomas R., Radding C. M. Hybrids of bacteriophages lambda and phi 80: a study of nonvegetative functions. Virology. 1969 Apr;37(4):585–596. doi: 10.1016/0042-6822(69)90276-1. [DOI] [PubMed] [Google Scholar]
  108. Séchaud J., Streisinger G., Emrich J., Newton J., Lanford H., Reinhold H., Stahl M. M. Chromosome structure in phage T4, II. Terminal redundancy and heterozygosis. Proc Natl Acad Sci U S A. 1965 Nov;54(5):1333–1339. doi: 10.1073/pnas.54.5.1333. [DOI] [PMC free article] [PubMed] [Google Scholar]
  109. 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]
  110. Tokuno S. I., Goldschmidt E. P., Gough M. Mutant of Salmonella typhimurium that channels infecting bacteriophage P22 toward lysogenization. J Bacteriol. 1974 Aug;119(2):508–513. doi: 10.1128/jb.119.2.508-513.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  111. Tokuno S. I., Gough M. Regulation of Bacteriophage P22 DNA synthesis and repressor levels in P22cly infections. J Virol. 1977 Mar;21(3):956–964. doi: 10.1128/jvi.21.3.956-964.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  112. Tokuno S., Gough M. Site c27 in phage P22 and control of the pathway to lysogeny. Mol Gen Genet. 1976 Mar 22;144(2):199–204. doi: 10.1007/BF02428109. [DOI] [PubMed] [Google Scholar]
  113. Tye B. K. A mutant of phage P22 with randomly permuted DNA. J Mol Biol. 1976 Jan 25;100(3):421–426. doi: 10.1016/s0022-2836(76)80073-3. [DOI] [PubMed] [Google Scholar]
  114. Tye B. K., Chan R. K., Botstein D. Packaging of an oversize transducing genome by Salmonella phage P22. J Mol Biol. 1974 Jan 5;85(4):485–500. doi: 10.1016/0022-2836(74)90311-8. [DOI] [PubMed] [Google Scholar]
  115. Tye B. K., Huberman J. A., Botstein D. Non-random circular permutation of phage P22 DNA. J Mol Biol. 1974 Jan 5;85(4):501–528. doi: 10.1016/0022-2836(74)90312-x. [DOI] [PubMed] [Google Scholar]
  116. Walsh J., Meynell G. G. The isolation of non-excluding mutants of phage P22. J Gen Virol. 1967 Oct;1(4):581–582. doi: 10.1099/0022-1317-1-4-581. [DOI] [PubMed] [Google Scholar]
  117. Watanabe T., Ogata Y., Chan R. K., Botstein D. Specialized transduction of tetracycline resistance by phage P22 in Salmonella typhimurium. I. Transduction of R factor 222 by phage P22. Virology. 1972 Dec;50(3):874–882. doi: 10.1016/0042-6822(72)90441-2. [DOI] [PubMed] [Google Scholar]
  118. Weaver S., Levine M. Recombinational circularization of Salmonella phage P22 DNA. Virology. 1977 Jan;76(1):29–38. doi: 10.1016/0042-6822(77)90278-1. [DOI] [PubMed] [Google Scholar]
  119. Weaver S., Levine M. Replication in situ and DNA encapsulation following induction of an excision-defective lysogen of Salmonella bacteriophage P22. J Mol Biol. 1978 Jan 25;118(3):389–411. doi: 10.1016/0022-2836(78)90235-8. [DOI] [PubMed] [Google Scholar]
  120. Weaver S., Levine M. The timing of erf-mediated recombination in replication, lysogenization, and the formation of recombinant progeny by Salmonella phage P22. Virology. 1977 Jan;76(1):19–28. doi: 10.1016/0042-6822(77)90277-x. [DOI] [PubMed] [Google Scholar]
  121. Weil J., Cunningham R., Martin R., 3rd, Mitchell E., Bolling B. Characteristics of lambda p4, a lambda derivative containing 9 per cent excess DNA. Virology. 1972 Nov;50(2):373–380. doi: 10.1016/0042-6822(72)90388-1. [DOI] [PubMed] [Google Scholar]
  122. Westmoreland B. C., Szybalski W., Ris H. Mapping of deletions and substitutions in heteroduplex DNA molecules of bacteriophage lambda by electron microscopy. Science. 1969 Mar 21;163(3873):1343–1348. doi: 10.1126/science.163.3873.1343. [DOI] [PubMed] [Google Scholar]
  123. Wilgus G. S., Mural R. J., Friedman D. I., Fiandt M., Szybalski W. Lambda imm lambda-434: a phage with a hybrid immunity region. Virology. 1973 Nov;56(1):46–53. doi: 10.1016/0042-6822(73)90286-9. [DOI] [PubMed] [Google Scholar]
  124. Wing J. P. Integration and induction of phage P22 in a recombination-deficient mutant of Salmonella typhimurium. J Virol. 1968 Jul;2(7):702–709. doi: 10.1128/jvi.2.7.702-709.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  125. Wright A., Kanegasaki S. Molecular aspects of lipopolysaccharides. Physiol Rev. 1971 Oct;51(4):748–784. doi: 10.1152/physrev.1971.51.4.748. [DOI] [PubMed] [Google Scholar]
  126. Yamagami H., Yamamoto N. Contribution of the bacterial recombination function to replication of bacteriophage P2. J Mol Biol. 1970 Oct 28;53(2):281–285. doi: 10.1016/0022-2836(70)90300-1. [DOI] [PubMed] [Google Scholar]
  127. ZINDER N. D. Bacterial transduction. J Cell Physiol Suppl. 1955 May;45(Suppl 2):23–49. doi: 10.1002/jcp.1030450504. [DOI] [PubMed] [Google Scholar]
  128. ZINDER N. D., LEDERBERG J. Genetic exchange in Salmonella. J Bacteriol. 1952 Nov;64(5):679–699. doi: 10.1128/jb.64.5.679-699.1952. [DOI] [PMC free article] [PubMed] [Google Scholar]
  129. ZINDER N. D. Lysogenization and superinfection immunity in Salmonella. Virology. 1958 Apr;5(2):291–326. doi: 10.1016/0042-6822(58)90025-4. [DOI] [PubMed] [Google Scholar]

Articles from Microbiological Reviews are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES