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. 1969 Sep;4(3):252–255. doi: 10.1128/jvi.4.3.252-255.1969

Phenotypic Suppression by Streptomycin of Amber Mutants in the Ribonucleic Acid Bacteriophage Coat Protein Cistron

Michihiko Kuwano 1,1, Hideya Endo 1
PMCID: PMC375866  PMID: 16789101

Abstract

After mutagenesis with nitrosoguanidine or ultraviolet light, 298 streptomycin high-resistant and 98 streptomycin high-dependent mutants were isolated from HfrC Su−. They were tested for their ability to phenotypically suppress five different amber ribonucleic acid (RNA) bacteriophage mutants in the presence of streptomycin. The phage mutants are all in the coat protein, which is 129 amino acids long; the uracil-adenine-guanine codons were at the following positions: sus3 and amB2, 6; amB11, 50; amB21, 54; sus11, 70. Only sus3 and amB2 could be phenotypically suppressed by streptomycin; this was clearly demonstrated in nine mutant strains, seven str-HR and two str-HD. The suppression was always dependent upon added streptomycin and was dose-dependent in all cases. None of the mutants showed measurable suppression in absence of the drug. Among revertants to streptomycin independence from streptomycin-dependent strains that could show phenotypic suppression, most of those that were still resistant to streptomycin (10 μg or more) retained the capacity to show phenotypic suppression; whereas among those revertants sensitive to 10 μg of streptomycin or less, none retained the capacity. Eight different amber polar mutants (strong and weak) in gene 34 of phage T4 were also tested for pleiotypic suppression by streptomycin in all the streptomycin-resistant and -dependent strains isolated. No suppression was found in any of the 396 strains tested.

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Selected References

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

  1. Apirion D., Schlessinger D. Reversion from streptomycin dependence in Escherichia coli by a further change in the ribosome. J Bacteriol. 1967 Oct;94(4):1275–1276. doi: 10.1128/jb.94.4.1275-1276.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Apirion D., Schlessinger D. The loss of phenotypic suppression in streptomycin-resistant mutants. Proc Natl Acad Sci U S A. 1967 Jul;58(1):206–212. doi: 10.1073/pnas.58.1.206. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. CLARK A. J., MARGULIES A. D. ISOLATION AND CHARACTERIZATION OF RECOMBINATION-DEFICIENT MUTANTS OF ESCHERICHIA COLI K12. Proc Natl Acad Sci U S A. 1965 Feb;53:451–459. doi: 10.1073/pnas.53.2.451. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Freda C. E., Cohen S. S. Streptomycin and infection of Escherichia coli by T6r+ bacteriophage. J Bacteriol. 1966 Dec;92(6):1670–1679. doi: 10.1128/jb.92.6.1670-1679.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. GORINI L., KATAJA E. PHENOTYPIC REPAIR BY STREPTOMYCIN OF DEFECTIVE GENOTYPES IN E. COLI. Proc Natl Acad Sci U S A. 1964 Mar;51:487–493. doi: 10.1073/pnas.51.3.487. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Kuwano M., Endo H., Ohnishi Y. Mutations to spectinomycin resistance which alleviate the restriction of an amber suppressor by streptomycin resistance. J Bacteriol. 1969 Feb;97(2):940–943. doi: 10.1128/jb.97.2.940-943.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Lodish H. F., Zinder N. D. Mutants of the bacteriophage f2. 8. Control mechanisms for phage-specific syntheses. J Mol Biol. 1966 Aug;19(2):333–348. doi: 10.1016/s0022-2836(66)80008-6. [DOI] [PubMed] [Google Scholar]
  8. Luzzatto L., Apirion D., Schlessinger D. Mechanism of action of streptomycin in E. coli: interruption of the ribosome cycle at the initiation of protein synthesis. Proc Natl Acad Sci U S A. 1968 Jul;60(3):873–880. doi: 10.1073/pnas.60.3.873. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Luzzatto L., Schlessinger D., Apirion D. Escherichia coli: high resistance or dependence on streptomycin produced by the same allele. Science. 1968 Aug 2;161(3840):478–479. doi: 10.1126/science.161.3840.478. [DOI] [PubMed] [Google Scholar]
  10. Mayuga C., Meier D., Wang T. Escherichia coli: the K 12 ribosomal protein and the streptomycin region of the chromosome. Biochem Biophys Res Commun. 1968 Oct 24;33(2):203–206. doi: 10.1016/0006-291x(68)90768-7. [DOI] [PubMed] [Google Scholar]
  11. Nakata A., Stahl F. W. Further evidence for polarity mutations in bacteriophage T4. Genetics. 1967 Mar;55(3):585–590. doi: 10.1093/genetics/55.3.585. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Tooze J., Weber K. Isolation and characterization of amber mutants of bacteriophage R17. J Mol Biol. 1967 Sep 14;28(2):311–330. doi: 10.1016/s0022-2836(67)80012-3. [DOI] [PubMed] [Google Scholar]
  13. Weber K., Notani G., Wikler M., Konigsberg W. Amino acid sequence of the f2 coat protein. J Mol Biol. 1966 Sep;20(2):423–425. doi: 10.1016/0022-2836(66)90073-8. [DOI] [PubMed] [Google Scholar]
  14. Whitfield H. J., Jr, Martin R. G., Ames B. N. Classification of aminotransferase (C gene) mutants in the histidine operon. J Mol Biol. 1966 Nov 14;21(2):335–355. doi: 10.1016/0022-2836(66)90103-3. [DOI] [PubMed] [Google Scholar]

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