Abstract
Replicative form DNA of bacteriophage f1 was found to be sensitive in vitro to restriction by endonuclease R-EcoRII if the DNA was isolated from an Escherichia coli strain deficient in cytosine methylase activity. A similar observation was previously made with DNA from the closely related bacteriophage fd (S. Schlagman, S. Hattman, M. S. May, and L. Berger, submitted for publication). The two DNA fragments produced by the endo R-EcoRII digestion of f1 DNA were localized on the f1 cleavage map and their genetic content was determined. The polypeptides synthesized in a "coupled" transcription-translation system under the direction of each RII fragment were examined. The results of such experiments allow the ordering of genes V and VII and indicate the location of a RNA promotor for gene VIII.
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- Arber W. Host specificity of DNA produced by Escherichia coli. 9. Host-controlled modification of bacteriophage fd. J Mol Biol. 1966 Oct;20(3):483–496. doi: 10.1016/0022-2836(66)90004-0. [DOI] [PubMed] [Google Scholar]
- BOYER H. GENETIC CONTROL OF RESTRICTION AND MODIFICATION IN ESCHERICHIA COLI. J Bacteriol. 1964 Dec;88:1652–1660. doi: 10.1128/jb.88.6.1652-1660.1964. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bannister D., Glover S. W. The isolation and properties of non-restricting mutants of two different host specificities associated with drug resistance factors. J Gen Microbiol. 1970 Apr;61(1):63–71. doi: 10.1099/00221287-61-1-63. [DOI] [PubMed] [Google Scholar]
- Boyer H. W., Chow L. T., Dugaiczyk A., Hedgpeth J., Goodman H. M. DNA substrate site for the EcoRII restriction endonuclease and modification methylase. Nat New Biol. 1973 Jul 11;244(132):40–43. doi: 10.1038/newbio244040a0. [DOI] [PubMed] [Google Scholar]
- Chang A. C., Cohen S. N. Genome construction between bacterial species in vitro: replication and expression of Staphylococcus plasmid genes in Escherichia coli. Proc Natl Acad Sci U S A. 1974 Apr;71(4):1030–1034. doi: 10.1073/pnas.71.4.1030. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Cohen S. N., Chang A. C., Boyer H. W., Helling R. B. Construction of biologically functional bacterial plasmids in vitro. Proc Natl Acad Sci U S A. 1973 Nov;70(11):3240–3244. doi: 10.1073/pnas.70.11.3240. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Edgell M. H., Hutchison C. A., 3rd, Sclair M. Specific endonuclease R fragments of bacteriophage phiX174 deoxyribonucleic acid. J Virol. 1972 Apr;9(4):574–582. doi: 10.1128/jvi.9.4.574-582.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hattman S. Plasmid-controlled variation in the content of methylated bases in single-stranded DNA bacteriophages M13 and fd. J Mol Biol. 1973 Mar 15;74(4):749–752. doi: 10.1016/0022-2836(73)90064-8. [DOI] [PubMed] [Google Scholar]
- Hattman S., Schlagman S., Cousens L. Isolation of a mutant of Escherichia coli defective in cytosine-specific deoxyribonucleic acid methylase activity and in partial protection of bacteriophage lambda against restriction by cells containing the N-3 drug-resistance factor. J Bacteriol. 1973 Sep;115(3):1103–1107. doi: 10.1128/jb.115.3.1103-1107.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Henry T. J., Pratt D. The proteins of bacteriophage M13. Proc Natl Acad Sci U S A. 1969 Mar;62(3):800–807. doi: 10.1073/pnas.62.3.800. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Horiuchi K., Vovis G. F., Zinder N. D. Effect of deoxyribonucleic acid length on the adenosine triphosphatase activity of Escherichia coli restriction endonuclease B. J Biol Chem. 1974 Jan 25;249(2):543–552. [PubMed] [Google Scholar]
- Hutchison C. A., 3rd, Edgell M. H. Genetic assay for small fragments of bacteriophage phi X174 deoxyribonucleic acid. J Virol. 1971 Aug;8(2):181–189. doi: 10.1128/jvi.8.2.181-189.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Konings R. N., Hulsebos T., Van den Hondel C. A. Identification and characterization of the in vitro synthesized gene products of bacteriophage M13. J Virol. 1975 Mar;15(3):570–584. doi: 10.1128/jvi.15.3.570-584.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lyons L. B., Zinder N. D. The genetic map of the filamentous bacteriophage f1. Virology. 1972 Jul;49(1):45–60. doi: 10.1016/s0042-6822(72)80006-0. [DOI] [PubMed] [Google Scholar]
- Marvin D. A., Hohn B. Filamentous bacterial viruses. Bacteriol Rev. 1969 Jun;33(2):172–209. doi: 10.1128/br.33.2.172-209.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Model P., Zinder N. D. In vitro synthesis of bacteriophage f1 proteins. J Mol Biol. 1974 Feb 25;83(2):231–251. doi: 10.1016/0022-2836(74)90389-1. [DOI] [PubMed] [Google Scholar]
- Morrow J. F., Cohen S. N., Chang A. C., Boyer H. W., Goodman H. M., Helling R. B. Replication and transcription of eukaryotic DNA in Escherichia coli. Proc Natl Acad Sci U S A. 1974 May;71(5):1743–1747. doi: 10.1073/pnas.71.5.1743. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Murray N. E., Murray K. Manipulation of restriction targets in phage lambda to form receptor chromosomes for DNA fragments. Nature. 1974 Oct 11;251(5475):476–481. doi: 10.1038/251476a0. [DOI] [PubMed] [Google Scholar]
- Pratt D., Tzagoloff H., Beaudoin J. Conditional lethal mutants of the small filamentous coliphage M13. II. Two genes for coat proteins. Virology. 1969 Sep;39(1):42–53. doi: 10.1016/0042-6822(69)90346-8. [DOI] [PubMed] [Google Scholar]
- Pratt D., Tzagoloff H., Erdahl W. S. Conditional lethal mutants of the small filamentous coliphage M13. I. Isolation, complementation, cell killing, time of cistron action. Virology. 1966 Nov;30(3):397–410. doi: 10.1016/0042-6822(66)90118-8. [DOI] [PubMed] [Google Scholar]
- Schlagman S., Hattman S. Mutants of the N-3 R-factor conditionally defective in hspII modification and deoxyribonucleic acid-cytosine methylase activity. J Bacteriol. 1974 Oct;120(1):234–239. doi: 10.1128/jb.120.1.234-239.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Smith H. O., Nathans D. Letter: A suggested nomenclature for bacterial host modification and restriction systems and their enzymes. J Mol Biol. 1973 Dec 15;81(3):419–423. doi: 10.1016/0022-2836(73)90152-6. [DOI] [PubMed] [Google Scholar]
- 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]
- Studier F. W. Analysis of bacteriophage T7 early RNAs and proteins on slab gels. J Mol Biol. 1973 Sep 15;79(2):237–248. doi: 10.1016/0022-2836(73)90003-x. [DOI] [PubMed] [Google Scholar]
- Takanami M., Okamoto T. Physical mapping of transcribing regions on coliphage fd DNA by the use of restriction endonucleases. Basic Life Sci. 1974;3:145–155. doi: 10.1007/978-1-4613-4529-9_12. [DOI] [PubMed] [Google Scholar]
- Takano T., Watanabe T., Fukasawa T. Mechanism of host-controlled restriction of bacteriophage lambda by R factors in Escherichia coli K12. Virology. 1968 Feb;34(2):290–302. doi: 10.1016/0042-6822(68)90239-0. [DOI] [PubMed] [Google Scholar]
- Taketo A. Sensitivity of Escherichia coli to viral nucleic acid. V. Competence of calcium-treated cells. J Biochem. 1972 Oct;72(4):973–979. doi: 10.1093/oxfordjournals.jbchem.a129988. [DOI] [PubMed] [Google Scholar]
- Watanabe T., Takano T., Arai T., Nishida H., Sato S. Episome-mediated Transfer of Drug Resistance in Enterobacteriaceae X. Restriction and Modification of Phages by fi R Factors. J Bacteriol. 1966 Aug;92(2):477–486. doi: 10.1128/jb.92.2.477-486.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yamamoto K. R., Alberts B. M., Benzinger R., Lawhorne L., Treiber G. Rapid bacteriophage sedimentation in the presence of polyethylene glycol and its application to large-scale virus purification. Virology. 1970 Mar;40(3):734–744. doi: 10.1016/0042-6822(70)90218-7. [DOI] [PubMed] [Google Scholar]
- Yoshimori R., Roulland-Dussoix D., Boyer H. W. R factor-controlled restriction and modification of deoxyribonucleic acid: restriction mutants. J Bacteriol. 1972 Dec;112(3):1275–1279. doi: 10.1128/jb.112.3.1275-1279.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]