Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1968 Mar;59(3):792–799. doi: 10.1073/pnas.59.3.792

Suppressor gene Su3+ of E. coli, a structural gene for tyrosine TRNA.

T Andoh, H Ozeki
PMCID: PMC224745  PMID: 4868217

Full text

PDF
792

Selected References

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

  1. Capecchi M. R., Gussin G. N. Suppression in vitro: Identification of a Serine-sRNA as a "Nonsense" Suppressor. Science. 1965 Jul 23;149(3682):417–422. doi: 10.1126/science.149.3682.417. [DOI] [PubMed] [Google Scholar]
  2. Engelhardt D. L., Webster R. E., Wilhelm R. C., Zinder N. In vitro studies on the mechanism of suppression of a nonsense mutation. Proc Natl Acad Sci U S A. 1965 Dec;54(6):1791–1797. doi: 10.1073/pnas.54.6.1791. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. FRANKEL F. R. An unusual DNA extracted from bacteria infected with phage T2. Proc Natl Acad Sci U S A. 1963 Mar 15;49:366–372. doi: 10.1073/pnas.49.3.366. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. GAREN A., GAREN S. Complementation in vivo between structural mutants of alkaline phosphatase from E. coli. J Mol Biol. 1963 Jul;7:13–22. doi: 10.1016/s0022-2836(63)80015-7. [DOI] [PubMed] [Google Scholar]
  5. Gallucci E., Garen A. Suppressor genes for nonsense mutations. II. The su-4 and su-5 suppressor genes of Escherichia coli. J Mol Biol. 1966 Jan;15(1):193–200. doi: 10.1016/s0022-2836(66)80220-6. [DOI] [PubMed] [Google Scholar]
  6. Garen A., Garen S., Wilhelm R. C. Suppressor genes for nonsense mutations. I. The Su-1, Su-2 and Su-3 genes of Escherichia coli. J Mol Biol. 1965 Nov;14(1):167–178. doi: 10.1016/s0022-2836(65)80238-8. [DOI] [PubMed] [Google Scholar]
  7. Gillespie D., Spiegelman S. A quantitative assay for DNA-RNA hybrids with DNA immobilized on a membrane. J Mol Biol. 1965 Jul;12(3):829–842. doi: 10.1016/s0022-2836(65)80331-x. [DOI] [PubMed] [Google Scholar]
  8. Gorini L., Beckwith J. R. Suppression. Annu Rev Microbiol. 1966;20:401–422. doi: 10.1146/annurev.mi.20.100166.002153. [DOI] [PubMed] [Google Scholar]
  9. Igarashi K., Hiraga S., Yura T. A deoxythymidine kinase deficient mutant of Escherichia coli. II. Mapping and transduction studies with phage phi 80. Genetics. 1967 Nov;57(3):643–654. doi: 10.1093/genetics/57.3.643. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. KELLENBERGER G., ZICHICHI M. L., WEIGLE J. A mutation affecting the DNA content of bacteriophage lambda and its lysogenizing properties. J Mol Biol. 1961 Aug;3:399–408. doi: 10.1016/s0022-2836(61)80053-3. [DOI] [PubMed] [Google Scholar]
  11. Kaplan S., Stretton A. O., Brenner S. Amber suppressors: efficiency of chain propagation and suppressor specific amino acids. J Mol Biol. 1965 Dec;14(2):528–533. doi: 10.1016/s0022-2836(65)80202-9. [DOI] [PubMed] [Google Scholar]
  12. MATSUSHIRO A. Specialized transduction of tryptophan markers in Escherichia coli K12 by bacteriophage phi-80. Virology. 1963 Apr;19:475–482. doi: 10.1016/0042-6822(63)90041-2. [DOI] [PubMed] [Google Scholar]
  13. NATHANS D., NOTANI G., SCHWARTZ J. H., ZINDER N. D. Biosynthesis of the coat protein of coliphage f2 by E. coli extracts. Proc Natl Acad Sci U S A. 1962 Aug;48:1424–1431. doi: 10.1073/pnas.48.8.1424. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. NOTANI G. W., ENGELHARDT D. L., KONIGSBERG W., ZINDER N. D. SUPPRESSION OF A COAT PROTEIN MUTANT OF THE BACTERIOPHAGE F2. J Mol Biol. 1965 Jun;12:439–447. doi: 10.1016/s0022-2836(65)80266-2. [DOI] [PubMed] [Google Scholar]
  15. Nishimura S., Harada F., Narushima U., Seno T. Purification of methionine-, valine-, phenylalanine- and tyrosine-specific tRNA from Escherichia coli. Biochim Biophys Acta. 1967 Jun 20;142(1):133–148. doi: 10.1016/0005-2787(67)90522-9. [DOI] [PubMed] [Google Scholar]
  16. SARABHAI A. S., STRETTON A. O., BRENNER S., BOLLE A. CO-LINEARITY OF THE GENE WITH THE POLYPEPTIDE CHAIN. Nature. 1964 Jan 4;201:13–17. doi: 10.1038/201013a0. [DOI] [PubMed] [Google Scholar]
  17. Smith J. D., Abelson J. N., Clark B. F., Goodman H. M., Brenner S. Studies on amber suppressor tRNA. Cold Spring Harb Symp Quant Biol. 1966;31:479–485. doi: 10.1101/sqb.1966.031.01.062. [DOI] [PubMed] [Google Scholar]
  18. Weigert M. G., Garen A. Base composition of nonsense codons in E. coli. Evidence from amino-acid substitutions at a tryptophan site in alkaline phosphatase. Nature. 1965 Jun 5;206(988):992–994. doi: 10.1038/206992a0. [DOI] [PubMed] [Google Scholar]
  19. Weigert M. G., Lanka E., Garen A. Amino acid substitutions resulting from suppression of nonsense mutations. II. Glutamine insertion by the Su-2 gene; tyrosine insertion by the Su-3 gene. J Mol Biol. 1965 Dec;14(2):522–527. doi: 10.1016/s0022-2836(65)80201-7. [DOI] [PubMed] [Google Scholar]
  20. Weigert M. G., Lanka E., Garen A. Base composition of nonsense codons in Escherichia coli II. The N2 codon UAA. J Mol Biol. 1967 Feb 14;23(3):391–400. doi: 10.1016/s0022-2836(67)80113-x. [DOI] [PubMed] [Google Scholar]
  21. Yamagishi H., Yoshizako F. Characteristics of DNA molecules extracted from bacteriophages phi-80 and phi-80-pt. Virology. 1966 Sep;30(1):29–35. doi: 10.1016/s0042-6822(66)81006-1. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES