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. 1971 Dec;69(4):409–433. doi: 10.1093/genetics/69.4.409

Polarity and Enzyme Functions in Mutants of the First Three Genes of the Tryptophan Operon of ESCHERICHIA COLI

Charles Yanofsky 1, Virginia Horn 1, Miriam Bonner 1, Susan Stasiowski 1
PMCID: PMC1224543  PMID: 4945859

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Selected References

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

  1. Balbinder E., Blume A. J., Weber A., Tamaki H. Polar and antipolar mutants in the tryptophan operon of Salmonella typhimurium. J Bacteriol. 1968 Jun;95(6):2217–2229. doi: 10.1128/jb.95.6.2217-2229.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bauerle R. H., Margolin P. A multifunctional enzyme complex in the tryptophan pathway of Salmonella typhimurium: comparison of polarity and pseudopolarity mutations. Cold Spring Harb Symp Quant Biol. 1966;31:203–214. doi: 10.1101/sqb.1966.031.01.028. [DOI] [PubMed] [Google Scholar]
  3. Blume A. J., Balbinder E. The tryptophan operon of Salmonella typhimurium. Fine structure analysis by deletion mapping and abortive transduction. Genetics. 1966 Mar;53(3):577–592. doi: 10.1093/genetics/53.3.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Blume A. J., Weber A., Balbinder E. Analysis of polar and nonpolar tryptophan mutants by derepression kinetics. J Bacteriol. 1968 Jun;95(6):2230–2241. doi: 10.1128/jb.95.6.2230-2241.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Contesse G., Naono S., Gros F. Effet des mutations polaires sur la transcription de l'opéron lactose chez Escherichia coli. C R Acad Sci Hebd Seances Acad Sci D. 1966 Oct 10;263(15):1007–1010. [PubMed] [Google Scholar]
  6. Coukell M. B., Yanofsky C. Influence of chromosome structure on the frequency of tonB trp deletions in Escherichia coli. J Bacteriol. 1971 Mar;105(3):864–872. doi: 10.1128/jb.105.3.864-872.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Crawford I. P., Sikes S. Mutants of Escherichia coli defective in the B protein of tryptophan synthetase. IV. Recombination map. Genetics. 1970 Dec;66(4):607–616. doi: 10.1093/genetics/66.4.607. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Creighton T. E. N-(5'-phosphoribosyl)anthranilate isomerase-indol-3-ylglycerol phosphate synthetase of tryptophan biosynthesis. Relationship between the two activities of the enzyme from Escherichia coli. Biochem J. 1970 Dec;120(4):699–707. doi: 10.1042/bj1200699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. FRANKLIN N. C., LURIA S. E. Transduction by bacteriophage P-1 and the properties of the lac genetic region in E. coli and S. dysenteriae. Virology. 1961 Nov;15:299–311. doi: 10.1016/0042-6822(61)90362-2. [DOI] [PubMed] [Google Scholar]
  10. Fink G. R., Martin R. G. Translation and polarity in the histidine operon. II. Polarity in the histidine operon. J Mol Biol. 1967 Nov 28;30(1):97–107. doi: 10.1016/0022-2836(67)90246-x. [DOI] [PubMed] [Google Scholar]
  11. Grodzicker T., Zipser D. A mutation which creates a new site for the re-initiation of polypeptide synthesis in the z gene of the lac operon of Escherichia coli. J Mol Biol. 1968 Dec;38(3):305–314. doi: 10.1016/0022-2836(68)90388-4. [DOI] [PubMed] [Google Scholar]
  12. Henderson E. J., Zalkin H., Hwang L. H. The anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase aggregate. Catalytic and regulatory properties of aggregated and unaggregated forms of anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase. J Biol Chem. 1970 Mar 25;245(6):1424–1431. [PubMed] [Google Scholar]
  13. Hwang L. H., Zalkin H. Multiple forms of anthranilate synthetase-anthranilate 5-phosphoribosylpyrophosphate phosphoribosyltransferase from Salmonella typhimurium. J Biol Chem. 1971 Apr 25;246(8):2338–2345. [PubMed] [Google Scholar]
  14. Imamoto F., Yanofsky C. Transcription of the tryptophan operon in polarity mutants of Escherichia coli. I. Characterization of the tryptophan messenger RNA of polar mutants. J Mol Biol. 1967 Aug 28;28(1):1–23. doi: 10.1016/s0022-2836(67)80073-1. [DOI] [PubMed] [Google Scholar]
  15. Ito J., Crawford I. P. Regulation of the enzymes of the tryptophan pathway in Escherichia coli. Genetics. 1965 Dec;52(6):1303–1316. doi: 10.1093/genetics/52.6.1303. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Ito J., Yanofsky C. The nature of the anthranilic acid synthetase complex of Escherichia coli. J Biol Chem. 1966 Sep 10;241(17):4112–4114. [PubMed] [Google Scholar]
  17. Jordan E., Saedler H. Polarity of amber mutations and suppressed amber mutations in the galactose operon of E. coli. Mol Gen Genet. 1967;100(3):283–295. doi: 10.1007/BF00381824. [DOI] [PubMed] [Google Scholar]
  18. Kuwano M., Schlessinger D., Morse D. E. Loss of dispensable endonuclease activity in relief of polarity by suA. Nat New Biol. 1971 Jun 16;231(24):214–217. doi: 10.1038/newbio231214a0. [DOI] [PubMed] [Google Scholar]
  19. Morse D. E., Yanofsky C. Polarity and the degradation of mRNA. Nature. 1969 Oct 25;224(5217):329–331. doi: 10.1038/224329a0. [DOI] [PubMed] [Google Scholar]
  20. Nagano H., Zalkin H., Henderson E. J. The anthranilate synthetase-anthranilate-5-phosphorribosylpyrophosphate phosphoribosyltransferase aggregate. On the reaction mechanism of anthranilate synthetase from Salmonella typhimurium. J Biol Chem. 1970 Aug 10;245(15):3810–3820. [PubMed] [Google Scholar]
  21. Nagano H., Zalkin H. Some physicochemical properties of anthranilate synthetase component I from Salmonella typhimurium. J Biol Chem. 1970 Jun;245(12):3097–3103. [PubMed] [Google Scholar]
  22. Norkin L. C. Marker-specific effects in genetic recombination. J Mol Biol. 1970 Aug;51(3):633–655. doi: 10.1016/0022-2836(70)90013-6. [DOI] [PubMed] [Google Scholar]
  23. Parmeggiani A., Luft J. H., Love D. S., Krebs E. G. Crystallization and properties of rabbit skeletal muscle phosphofructokinase. J Biol Chem. 1966 Oct 25;241(20):4625–4637. [PubMed] [Google Scholar]
  24. Smith O. H. Structure of the trpC cistron specifying indoleglycerol phosphate synthetase, and its localization in the tryptophan operon of Escherichia coli. Genetics. 1967 Sep;57(1):95–105. doi: 10.1093/genetics/57.1.95. [DOI] [PMC free article] [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. 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]
  27. Zipser D., Zabell S., Rothman J., Grodzicker T., Wenk M. Fine structure of the gradient of polarity in the z gene of the lac operon of Escherichia coli. J Mol Biol. 1970 Apr 14;49(1):251–254. doi: 10.1016/0022-2836(70)90392-x. [DOI] [PubMed] [Google Scholar]

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