Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1972 Nov;112(2):797–805. doi: 10.1128/jb.112.2.797-805.1972

Mapping of the Tryptophan Genes of Acinetobacter calcoaceticus by Transformation

R V Sawula 1, Irving P Crawford 1
PMCID: PMC251489  PMID: 5086660

Abstract

Auxotrophs of Acinetobacter calcoaceticus blocked in each reaction of the synthetic pathway from chorismic acid to tryptophan were obtained after N-methyl-N′-nitro-N-nitrosoguanidine mutagenesis. One novel class was found to be blocked in both anthranilate and p-aminobenzoate synthesis; these mutants (trpG) require p-aminobenzoate or folate as well as tryptophan (or anthranilate) for growth. The loci of six other auxotrophic classes requiring only tryptophan were defined by growth, accumulation, and enzymatic analysis where appropriate. The trp mutations map in three chromosomal locations. One group contains trpC and trpD (indoleglycerol phosphate synthetase and phosphoribosyl transferase) in addition to trpG mutations; this group is closely linked to a locus conferring a glutamate requirement. Another cluster contains trpA and trpB, coding for the two tryptophan synthetase (EC 4.2.1.20) subunits, along with trpF (phosphoribosylanthranilate isomerase); this group is weakly linked to a his marker. The trpE gene, coding for the large subunit of anthranilate synthetase, is unlinked to any of the above. This chromosomal distribution of the trp genes has not been observed in other organisms.

Full text

PDF
801

Selected References

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

  1. 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]
  2. Baumann P., Doudoroff M., Stanier R. Y. A study of the Moraxella group. II. Oxidative-negative species (genus Acinetobacter). J Bacteriol. 1968 May;95(5):1520–1541. doi: 10.1128/jb.95.5.1520-1541.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Baumann P., Doudoroff M., Stanier R. Y. Study of the Moraxella group. I. Genus Moraxella and the Neisseria catarrhalis group. J Bacteriol. 1968 Jan;95(1):58–73. doi: 10.1128/jb.95.1.58-73.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Baumann P. Isolation of Acinetobacter from soil and water. J Bacteriol. 1968 Jul;96(1):39–42. doi: 10.1128/jb.96.1.39-42.1968. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. Carlton B. C., Whitt D. D. The isolation and genetic characterization of mutants of the tryptophan system of Bacillus subtilis. Genetics. 1969 Jul;62(3):445–460. doi: 10.1093/genetics/62.3.445. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Crawford I. P., Yanofsky C. Pseudomonas putida tryptophan synthetase: partial sequence of the subunit. J Bacteriol. 1971 Oct;108(1):248–253. doi: 10.1128/jb.108.1.248-253.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gibson F. Chorismic acid: purification and some chemical and physical studies. Biochem J. 1964 Feb;90(2):256–261. doi: 10.1042/bj0900256. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gunsalus C., Gunsalus C. F., Chakrabarty A. M., Sikes S., Crawford I. P. Fine structure mapping of the tryptophan genes in Pseudomonas putida. Genetics. 1968 Nov;60(3):419–435. doi: 10.1093/genetics/60.3.419. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hoch S. O., Anagnostopoulos C., Crawford I. P. Enzymes of the tryptophan operon of Bacillus subtilis. Biochem Biophys Res Commun. 1969 Jun 27;35(6):838–844. doi: 10.1016/0006-291x(69)90700-1. [DOI] [PubMed] [Google Scholar]
  11. Huang M., Gibson F. Biosynthesis of 4-aminobenzoate in Escherichia coli. J Bacteriol. 1970 Jun;102(3):767–773. doi: 10.1128/jb.102.3.767-773.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Hutchinson M. A., Belser W. L. Enzymes of tryptophan biosynthesis in Serratia marcescens. J Bacteriol. 1969 Apr;98(1):109–115. doi: 10.1128/jb.98.1.109-115.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Hütter R., DeMoss J. A. Organization of the tryptophan pathway: a phylogenetic study of the fungi. J Bacteriol. 1967 Dec;94(6):1896–1907. doi: 10.1128/jb.94.6.1896-1907.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. 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]
  15. Juni E., Janik A. Transformation of Acinetobacter calco-aceticus (Bacterium anitratum). J Bacteriol. 1969 Apr;98(1):281–288. doi: 10.1128/jb.98.1.281-288.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Kane J. F., Holmes W. M., Jensen R. A. Metabolic interlock. The dual function of a folate pathway gene as an extra-operonic gene of tryptophan biosynthesis. J Biol Chem. 1972 Mar 10;247(5):1587–1596. [PubMed] [Google Scholar]
  17. Kane J. F., Jensen R. A. The molecular aggregation of anthranilate synthase in Bacillus subtilis. Biochem Biophys Res Commun. 1970 Oct 23;41(2):328–333. doi: 10.1016/0006-291x(70)90507-3. [DOI] [PubMed] [Google Scholar]
  18. Kloos W. E., Rose N. E. Transformation mapping of tryptophan loci in Micrococcus luteus. Genetics. 1970 Dec;66(4):595–605. doi: 10.1093/genetics/66.4.595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. LENNOX E. S. Transduction of linked genetic characters of the host by bacteriophage P1. Virology. 1955 Jul;1(2):190–206. doi: 10.1016/0042-6822(55)90016-7. [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. Proctor A. R., Kloos W. E. The tryptophan gene cluster of Staphylococcus aureus. J Gen Microbiol. 1970 Dec;64(3):319–327. doi: 10.1099/00221287-64-3-319. [DOI] [PubMed] [Google Scholar]
  22. Queener S. F., Gunsalus I. C. Anthranilate synthase enzyme system and complementation in Pseudomonas species. Proc Natl Acad Sci U S A. 1970 Nov;67(3):1225–1232. doi: 10.1073/pnas.67.3.1225. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. 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]
  24. TAYLOR W. H., JUNI E. Pathways for biosynthesis of a bacterial capsular polysaccharide. I. Characterization of the organism and polysaccharide. J Bacteriol. 1961 May;81:688–693. doi: 10.1128/jb.81.5.688-693.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Twarog R., Liggins G. L. Enzymes of the tryptophan pathway in Acinetobacter calco-aceticus. J Bacteriol. 1970 Oct;104(1):254–263. doi: 10.1128/jb.104.1.254-263.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. 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]
  27. YANOFSKY C., LENNOX E. S. Transduction and recombination study of linkage relationships among the genes controlling tryptophan synthesis in Escherichia coli. Virology. 1959 Aug;8:425–447. doi: 10.1016/0042-6822(59)90046-7. [DOI] [PubMed] [Google Scholar]
  28. Yanofsky C., Horn V., Bonner M., Stasiowski S. Polarity and enzyme functions in mutants of the first three genes of the tryptophan operon of Escherichia coli. Genetics. 1971 Dec;69(4):409–433. doi: 10.1093/genetics/69.4.409. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES