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. 1967 Jun;57(6):1857–1864. doi: 10.1073/pnas.57.6.1857

Chain initiation in a polycistronic message: sequential versus simultaneous derepression of the enzymes for histidine biosynthesis in Salmonella typhimurium.

M A Berberich, J S Kovach, R F Goldberger
PMCID: PMC224557  PMID: 5340637

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Selected References

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

  1. AMES B. N., GARRY B., HERZENBERG L. A. The genetic control of the enzymes of histidine biosynthesis in Salmonella typhimurium. J Gen Microbiol. 1960 Apr;22:369–378. doi: 10.1099/00221287-22-2-369. [DOI] [PubMed] [Google Scholar]
  2. AMES B. N., HARTMAN P. E., JACOB F. Chromosomal alterations affecting the regulation of histidine biosynthetic enzymes in Salmonella. J Mol Biol. 1963 Jul;7:23–42. doi: 10.1016/s0022-2836(63)80016-9. [DOI] [PubMed] [Google Scholar]
  3. AMES B. N., MARTIN R. G., GARRY B. J. The first step of histidine biosynthesis. J Biol Chem. 1961 Jul;236:2019–2026. [PubMed] [Google Scholar]
  4. Adams J. M., Capecchi M. R. N-formylmethionyl-sRNA as the initiator of protein synthesis. Proc Natl Acad Sci U S A. 1966 Jan;55(1):147–155. doi: 10.1073/pnas.55.1.147. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Alpers D. H., Tomkins G. M. Sequential transcription of the genes of the lactose operon and its regulation by protein synthesis. J Biol Chem. 1966 Oct 10;241(19):4434–4443. [PubMed] [Google Scholar]
  6. Ames B. N., Garry B. COORDINATE REPRESSION OF THE SYNTHESIS OF FOUR HISTIDINE BIOSYNTHETIC ENZYMES BY HISTIDINE. Proc Natl Acad Sci U S A. 1959 Oct;45(10):1453–1461. doi: 10.1073/pnas.45.10.1453. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. BYRNE R., LEVIN J. G., BLADEN H. A., NIRENBERG M. W. THE IN VITRO FORMATION OF A DNA-RIBOSOME COMPLEX. Proc Natl Acad Sci U S A. 1964 Jul;52:140–148. doi: 10.1073/pnas.52.1.140. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Berberich M. A., Venetianer P., Goldberger R. F. Alternative modes of derepression of the histidine operon observed in Salmonella typhimurium. J Biol Chem. 1966 Oct 10;241(19):4426–4433. [PubMed] [Google Scholar]
  9. Burchall J. J., Hitchings G. H. Inhibitor binding analysis of dihydrofolate reductases from various species. Mol Pharmacol. 1965 Sep;1(2):126–136. [PubMed] [Google Scholar]
  10. Eisenstadt J., Lengyel P. Formylmethionyl-tRNA dependence of amino acid incorporation in extracts of trimethoprim-treated Escherichia coli. Science. 1966 Oct 28;154(3748):524–527. [PubMed] [Google Scholar]
  11. FRIEDKIN M. ENZYMATIC ASPECTS OF FOLIC ACID. Annu Rev Biochem. 1963;32:185–214. doi: 10.1146/annurev.bi.32.070163.001153. [DOI] [PubMed] [Google Scholar]
  12. Goldberger R. F., Berberich M. A. Sequential repression and derepression of the enzymes for histidine biosynthesis in Salmonella typhimurium. Proc Natl Acad Sci U S A. 1965 Jul;54(1):279–286. doi: 10.1073/pnas.54.1.279. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  14. MARCKER K., SANGER F. N-FORMYL-METHIONYL-S-RNA. J Mol Biol. 1964 Jun;8:835–840. doi: 10.1016/s0022-2836(64)80164-9. [DOI] [PubMed] [Google Scholar]
  15. MOAT A. G., FRIEDMAN H. The biosynthesis and interconversion of purines and their derivatives. Bacteriol Rev. 1960 Sep;24(3):309–339. doi: 10.1128/br.24.3.309-339.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. MOYED H. S., MAGASANIK B. The biosynthesis of the imidazole ring of histidine. J Biol Chem. 1960 Jan;235:149–153. [PubMed] [Google Scholar]
  17. Margolies M. N., Goldberger R. F. Isolation of the fourth (isomerase) of histidine biosynthesis from Salmonella typhimurium. J Biol Chem. 1966 Jul 25;241(14):3262–3269. [PubMed] [Google Scholar]
  18. Martin R. G., Silbert D. F., Smith W. E., Whitfield H. J., Jr Polarity in the histidine operon. J Mol Biol. 1966 Nov 14;21(2):357–369. doi: 10.1016/0022-2836(66)90104-5. [DOI] [PubMed] [Google Scholar]
  19. Martin R. G., Whitfield H. J., Jr, Berkowitz D. B., Voll M. J. A molecular model of the phenomenon of polarity. Cold Spring Harb Symp Quant Biol. 1966;31:215–220. doi: 10.1101/sqb.1966.031.01.029. [DOI] [PubMed] [Google Scholar]
  20. Roth J. R., Antón D. N., Hartman P. E. Histidine regulatory mutants in Salmonella typhimurium. I. Isolation and general properties. J Mol Biol. 1966 Dec 28;22(2):305–323. doi: 10.1016/0022-2836(66)90134-3. [DOI] [PubMed] [Google Scholar]
  21. SMITH D. W., AMES B. N. INTERMEDIATES IN THE EARLY STEPS OF HISTIDINE BIOSYNTHESIS. J Biol Chem. 1964 Jun;239:1848–1855. [PubMed] [Google Scholar]
  22. STENT G. S. THE OPERON: ON ITS THIRD ANNIVERSARY. MODULATION OF TRANSFER RNA SPECIES CAN PROVIDE A WORKABLE MODEL OF AN OPERATOR-LESS OPERON. Science. 1964 May 15;144(3620):816–820. doi: 10.1126/science.144.3620.816. [DOI] [PubMed] [Google Scholar]
  23. Shih A. Y., Eisenstadt J., Lengyel P. On the relation between ribonucleic acid synthesis and peptide chain initiation in E. coli. Proc Natl Acad Sci U S A. 1966 Nov;56(5):1599–1605. doi: 10.1073/pnas.56.5.1599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Thach R. E., Dewey K. F., Brown J. C., Doty P. Formylmethionine codon AUG as an initiator of polypeptide synthesis. Science. 1966 Jul 22;153(3734):416–418. doi: 10.1126/science.153.3734.416. [DOI] [PubMed] [Google Scholar]
  25. VOGEL H. J., BONNER D. M. Acetylornithinase of Escherichia coli: partial purification and some properties. J Biol Chem. 1956 Jan;218(1):97–106. [PubMed] [Google Scholar]
  26. Viñuela E., Salas M., Ochoa S. Translation of the genetic message, iii. Formylmethionine as initiator of proteins programed by polycistronic messenger RNA. Proc Natl Acad Sci U S A. 1967 Mar;57(3):729–734. doi: 10.1073/pnas.57.3.729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. WALLER J. P. THE NH2-TERMINAL RESIDUES OF THE PROTEINS FROM CELL-FREE EXTRACTS OF E. COLI. J Mol Biol. 1963 Nov;7:483–496. doi: 10.1016/s0022-2836(63)80096-0. [DOI] [PubMed] [Google Scholar]
  28. Webster R. E., Engelhardt D. L., Zinder N. D. In vitro protein synthesis: chain initiation. Proc Natl Acad Sci U S A. 1966 Jan;55(1):155–161. doi: 10.1073/pnas.55.1.155. [DOI] [PMC free article] [PubMed] [Google Scholar]

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