Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1976 Aug;19(2):501–517. doi: 10.1128/jvi.19.2.501-517.1976

Analysis of gene function of bacteriophage phi 29 of Bacillus subtilis: identification of cistrons essential for viral assembly.

E W Hagen, B E Reilly, M E Tosi, D L Anderson
PMCID: PMC354888  PMID: 822175

Abstract

Restrictive infection of Bacillus subtilis by suppressor-sensitive (sus) mutants of phi 29 has been used to search for cistrons that function in viral assembly. The products of cistrons 7, 9, 10, and 16 are necessary for head morphogenesis. The neck upper collar protein P10 and the tail protein P9 must be present for DNA packaging to occur. The protein P7 must be present for phage-related particles to form. A prohead-like particle has been isolated during 16-restrictive infection. The particle is composed of the proteins Hd, P10, F, and P7. P16 must function for DNA-filled particles to accumulate. A DNA-containing particle produced in the absence of the cistron 11 product may be an intermediate in the phi 29 assembly pathway. The protein P13 interacts with P9 and P11 to form a stable DNA-filled particle. The products of cistrons 2 and 3 are essential for viral DNA synthesis, and in their absence virus-related particles are not detected.

Full text

PDF
502

Images in this article

507Image
on p.507
508Image
on p.508
509Image
on p.509
510Image
on p.510
511Image
on p.511
512Image
on p.512
513Image
on p.513
514Image
on p.514
515Image
on p.515
516Image
on p.516

Selected References

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

  1. Anderson D. L., Hickman D. D., Reilly B. E. Structure of Bacillus subtilis bacteriophage phi 29 and the length of phi 29 deoxyribonucleic acid. J Bacteriol. 1966 May;91(5):2081–2089. doi: 10.1128/jb.91.5.2081-2089.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Anderson D. L., Reilly B. E. Analysis of bacteriophage phi 29 gene function: protein synthesis in suppressor-sensitive mutant infection of Bacillus subtilis. J Virol. 1974 Jan;13(1):211–221. doi: 10.1128/jvi.13.1.211-221.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Carrascosa J. L., Camacho A., Viñuela E., Salas M. A precursor of the neck appendage protein of B. subtilis phage phi 29. FEBS Lett. 1974 Aug 30;44(3):317–321. [PubMed] [Google Scholar]
  4. Carrascosa J. L., Viñuela E., Salas M. Proteins induced in Bacillus subtilis infected with bacteriophage phi 29. Virology. 1973 Nov;56(1):291–299. [PubMed] [Google Scholar]
  5. 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]
  6. Hagen E. W., Anderson D. L. In situ lysis of phi29- and SPO1-infected Bacillus subtilis. J Virol. 1975 Jan;15(1):217–220. doi: 10.1128/jvi.15.1.217-220.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hawley L. A., Reilly B. E., Hagen E. W., Anderson D. L. Viral protein synthesis in bacteriophage phi 29-infected Bacillus subtilis. J Virol. 1973 Nov;12(5):1149–1159. doi: 10.1128/jvi.12.5.1149-1159.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Ivarie R. D., Pène J. J. DNA replication in bacteriophage ø29: the requirement of a viral-specfic product for association of ø29 DNA with the cell membrane of Bacillus amyloliquefaciens. Virology. 1973 Apr;52(2):351–362. doi: 10.1016/0042-6822(73)90330-9. [DOI] [PubMed] [Google Scholar]
  9. LUFT J. H. Improvements in epoxy resin embedding methods. J Biophys Biochem Cytol. 1961 Feb;9:409–414. doi: 10.1083/jcb.9.2.409. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Loskutoff D. J., Pène J. J., Andrews D. P. Gene expression during the development of Bacillus subtilis bacteriophage phi 29. I. Analysis of viral-specific transcription by deoxyribonucleic acid-ribonucleic acid competition hybridization. J Virol. 1973 Jan;11(1):78–86. doi: 10.1128/jvi.11.1.78-86.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Mellado R. P., Moreno F., Viñuela E., Salas M., Reilly B. E., Anderson D. L. Genetic analysis of bacteriophage phi 29 of Bacillus subtilis: integration and mapping of reference mutants of two collections. J Virol. 1976 Aug;19(2):495–500. doi: 10.1128/jvi.19.2.495-500.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Moreno F. Suppressor-sensitive mutants and genetic map of Bacillus subtilis bacteriophage phi 29. Virology. 1974 Nov;62(1):1–16. doi: 10.1016/0042-6822(74)90298-0. [DOI] [PubMed] [Google Scholar]
  13. Méndez E., Ramírez G., Salas M., Viñuela E. Structural proteins of bacteriophage phi 29. Virology. 1971 Sep;45(3):567–576. doi: 10.1016/0042-6822(71)90172-3. [DOI] [PubMed] [Google Scholar]
  14. Nelson R. A., Reilly B. E., Anderson D. L. Morphogenesis of bacteriophage phi 29 of Bacillus subtilis: preliminary isolation and characterization of intermediate particles of the assembly pathway. J Virol. 1976 Aug;19(2):518–532. doi: 10.1128/jvi.19.2.518-532.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Ortin J., Viñuela E., Salas M., Vasquez C. DNA-protein complex in circular DNA from phage phi-29. Nat New Biol. 1971 Dec 29;234(52):275–277. doi: 10.1038/newbio234275a0. [DOI] [PubMed] [Google Scholar]
  16. Péne J. J., Murr P. C., Barrow-Carraway J. Synthesis of bacteriophage phi 29 proteins in Bacillus subtilis. J Virol. 1973 Jul;12(1):61–67. doi: 10.1128/jvi.12.1.61-67.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. REILLY B. E., SPIZIZEN J. BACTERIOPHAGE DEOXYRIBONUCLEATE INFECTION OF COMPETENT BACILLUS SUBTILIS. J Bacteriol. 1965 Mar;89:782–790. doi: 10.1128/jb.89.3.782-790.1965. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. REYNOLDS E. S. The use of lead citrate at high pH as an electron-opaque stain in electron microscopy. J Cell Biol. 1963 Apr;17:208–212. doi: 10.1083/jcb.17.1.208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Reilly B. E., Tosi M. E., Anderson D. L. Genetic analysis of bacteriophage phi29 of Bacillus subtilis: mapping of the cistrons coding for structural proteins. J Virol. 1975 Oct;16(4):1010–1016. doi: 10.1128/jvi.16.4.1010-1016.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Reilly B. E., Zeece V. M., Anderson D. L. Genetic study of suppressor-sensitive mutants of the Bacillus subtilis bacteriophage phi 29. J Virol. 1973 May;11(5):756–760. doi: 10.1128/jvi.11.5.756-760.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Schachtele C. F., Reilly B. E., De Sain C. V., Whittington M. O., Anderson D. L. Selective replication of bacteriophage phi29 deoxyribonucleic acid in 6-(p-hydroxyphenylazo)-uracil-treated Bacillus subtilis. J Virol. 1973 Jan;11(1):153–155. doi: 10.1128/jvi.11.1.153-155.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Tosi M. E., Reilly B. E., Anderson D. L. Morphogenesis of bacteriophage phi29 of Bacillus subtilis: cleavage and assembly of the neck appendage protein. J Virol. 1975 Nov;16(5):1282–1295. doi: 10.1128/jvi.16.5.1282-1295.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Tosi M., Anderson D. L. Antigenic properties of bacteriophage phi 29 structural proteins. J Virol. 1973 Dec;12(6):1548–1559. doi: 10.1128/jvi.12.6.1548-1559.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES