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. 1978 Sep;5(9):3141–3156. doi: 10.1093/nar/5.9.3141

Nucleotide sequence of the O gene and of the origin of replication in bacteriophage lambda DNA.

G Scherer
PMCID: PMC342237  PMID: 704348

Abstract

The nucleotide sequence of the O gene in bacteriophage lambda DNA is presented. According to two possible initiator codons, the primary structure of the O protein deduced from the DNA sequence consists of 278 or 299 amino acid residues. Structure and function of the O protein--one of the two phage initiator proteins for lambda DNA replication--are discussed in the light of a secondary structure model for the O protein. The central part of the O gene contains a cluster of symmetrical sequences extending over 160 base pairs. The point mutation of the cis-dominant replication mutant ti12 is located in this region.

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Selected References

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  1. Bickle T. A., Pirrotta V., Imber R. A simple, general procedure for purifying restriction endonucleases. Nucleic Acids Res. 1977 Aug;4(8):2561–2572. doi: 10.1093/nar/4.8.2561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Chou P. Y., Adler A. J., Fasman G. D. Conformational prediction and circular dichroism studies on the lac repressor. J Mol Biol. 1975 Jul 25;96(1):29–45. doi: 10.1016/0022-2836(75)90180-1. [DOI] [PubMed] [Google Scholar]
  3. Chou P. Y., Fasman G. D. Prediction of protein conformation. Biochemistry. 1974 Jan 15;13(2):222–245. doi: 10.1021/bi00699a002. [DOI] [PubMed] [Google Scholar]
  4. Denniston-Thompson K., Moore D. D., Kruger K. E., Furth M. E., Blattner F. R. Physical structure of the replication origin of bacteriophage lambda. Science. 1977 Dec 9;198(4321):1051–1056. doi: 10.1126/science.929187. [DOI] [PubMed] [Google Scholar]
  5. Eisen H. A., Fuerst C. R., Siminovitch L., Thomas R., Lambert L., Pereira da Silva L., Jacob F. Genetics and physiology of defective lysogeny in K12 (lambda): studies of early mutants. Virology. 1966 Oct;30(2):224–241. doi: 10.1016/0042-6822(66)90098-5. [DOI] [PubMed] [Google Scholar]
  6. Fiddes J. C., Barrell B. G., Godson G. N. Nucleotide sequences of the separate origins of synthesis of bacteriophage G4 viral and complementary DNA strands. Proc Natl Acad Sci U S A. 1978 Mar;75(3):1081–1085. doi: 10.1073/pnas.75.3.1081. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Furth M. E., Blattner F. R., McLeester C., Dove W. F. Genetic structure of the replication origin of bacteriophage lambda. Science. 1977 Dec 9;198(4321):1046–1051. doi: 10.1126/science.929186. [DOI] [PubMed] [Google Scholar]
  8. Hughes S. G. The sensitivity of bacteriophage lambda DNA to restriction endonuclease RII. J Mol Biol. 1975 Nov 5;98(3):645–647. doi: 10.1016/s0022-2836(75)80093-3. [DOI] [PubMed] [Google Scholar]
  9. Maxam A. M., Gilbert W. A new method for sequencing DNA. Proc Natl Acad Sci U S A. 1977 Feb;74(2):560–564. doi: 10.1073/pnas.74.2.560. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Ohmori H., Tomizawa J. I., Maxam A. M. Detection of 5-methylcytosine in DNA sequences. Nucleic Acids Res. 1978 May;5(5):1479–1485. doi: 10.1093/nar/5.5.1479. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Pirrotta V. The lambda repressor and its action. Curr Top Microbiol Immunol. 1976;74:21–54. doi: 10.1007/978-3-642-66336-9_2. [DOI] [PubMed] [Google Scholar]
  12. Pirrotta V. Two restriction endonucleases from Bacillus globiggi. Nucleic Acids Res. 1976 Jul;3(7):1747–1760. doi: 10.1093/nar/3.7.1747. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Polisky B., Greene P., Garfin D. E., McCarthy B. J., Goodman H. M., Boyer H. W. Specificity of substrate recognition by the EcoRI restriction endonuclease. Proc Natl Acad Sci U S A. 1975 Sep;72(9):3310–3314. doi: 10.1073/pnas.72.9.3310. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Raab C., Klein A., Kluding H., Hirth P., Fuchs E. Cell free synthesis of bacteriophage lambda replication proteins. FEBS Lett. 1977 Aug 15;80(2):275–278. doi: 10.1016/0014-5793(77)80456-0. [DOI] [PubMed] [Google Scholar]
  15. Rambach A. Replicator mutants of bacteriophage lambda: characterization of two subclasses. Virology. 1973 Jul;54(1):270–277. doi: 10.1016/0042-6822(73)90136-0. [DOI] [PubMed] [Google Scholar]
  16. Scherer G., Hobom G., Kössel H. DNA base sequence of the po promoter region of phage lamdba. Nature. 1977 Jan 13;265(5590):117–121. doi: 10.1038/265117a0. [DOI] [PubMed] [Google Scholar]
  17. Schnös M., Inman R. B. Position of branch points in replicating lambda DNA. J Mol Biol. 1970 Jul 14;51(1):61–73. doi: 10.1016/0022-2836(70)90270-6. [DOI] [PubMed] [Google Scholar]
  18. Schwarz E., Scherer G., Hobom G., Kössel H. Nucleotide sequence of cro, cII and part of the O gene in phage lambda DNA. Nature. 1978 Mar 30;272(5652):410–414. doi: 10.1038/272410a0. [DOI] [PubMed] [Google Scholar]
  19. Shine J., Dalgarno L. The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1342–1346. doi: 10.1073/pnas.71.4.1342. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Skalka A. M. DNA replication--bacteriophage lambda. Curr Top Microbiol Immunol. 1977;78:201–237. [PubMed] [Google Scholar]
  21. 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]
  22. Steitz J. A., Jakes K. How ribosomes select initiator regions in mRNA: base pair formation between the 3' terminus of 16S rRNA and the mRNA during initiation of protein synthesis in Escherichia coli. Proc Natl Acad Sci U S A. 1975 Dec;72(12):4734–4738. doi: 10.1073/pnas.72.12.4734. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Streeck R. E., Hobom G. Mapping of cleavage sites for restriction endonucleases in lambdadv plasmids. Eur J Biochem. 1975 Sep 15;57(2):595–606. doi: 10.1111/j.1432-1033.1975.tb02335.x. [DOI] [PubMed] [Google Scholar]
  24. THOMAS R., BERTANI L. E. ON THE CONTROL OF THE REPLICATION OF TEMPERATE BACTERIOPHAGES SUPERINFECTING IMMUNE HOSTS. Virology. 1964 Nov;24:241–253. doi: 10.1016/0042-6822(64)90163-1. [DOI] [PubMed] [Google Scholar]
  25. Thomas M., Davis R. W. Studies on the cleavage of bacteriophage lambda DNA with EcoRI Restriction endonuclease. J Mol Biol. 1975 Jan 25;91(3):315–328. doi: 10.1016/0022-2836(75)90383-6. [DOI] [PubMed] [Google Scholar]
  26. Wyatt W. M., Inokuchi H. Stability of lambda O and P replication functions. Virology. 1974 Mar;58(1):313–315. doi: 10.1016/0042-6822(74)90168-8. [DOI] [PubMed] [Google Scholar]
  27. Yates J. L., Gette W. R., Furth M. E., Nomura M. Effects of ribosomal mutations on the read-through of a chain termination signal: studies on the synthesis of bacteriophage lambda O gene protein in vitro. Proc Natl Acad Sci U S A. 1977 Feb;74(2):689–693. doi: 10.1073/pnas.74.2.689. [DOI] [PMC free article] [PubMed] [Google Scholar]

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