Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1967 Dec;94(6):1896–1907. doi: 10.1128/jb.94.6.1896-1907.1967

Organization of the Tryptophan Pathway: a Phylogenetic Study of the Fungi

R Hütter a,1, J A DeMoss a
PMCID: PMC276919  PMID: 4864405

Abstract

The enzymes involved in tryptophan biosynthesis have been analyzed in a variety of fungal strains and a few other microorganisms. The same five biosynthetic reactions occur in all organisms tested, but differences have been found in the stability requirements for the enzymes, in their differential precipitation with ammonium sulfate, and in their sedimentation pattern after zone centrifugation. Based on the sedimentation behavior of anthranilate synthetase, phosphoribosyl-transferase, N-(5′-phosphoribosyl)-anthranilate isomerase, and indole-3-glycerophosphate synthetase, five different patterns of enzyme association could be recognized. The distribution of these patterns was used to evaluate several specific features of proposed phylogenetic relationships in the fungi. A closer relationship between Chytridiales and Aspergillales is postulated, eliminating the Zygomycetes and the Endomycetales as probable intermediates; the latter groups are considered to be sidelines. The data support the idea of a polyphyletic origin of the phycomycetes and suggest that anascosporogenous yeasts tested are related to the heterobasidiomycetes rather than to the Endomycetales. A possible sequence of changes leading to the various patterns of organization of the tryptophan pathway during the course of evolution is also proposed.

Full text

PDF
1896

Selected References

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

  1. BALBINDER E. The fine structure of the loci tryC and tryD of Salmonella typhimurium. I. Determination of the order of mutational sites by three-point transduction tests. Genetics. 1962 Apr;47:469–482. doi: 10.1093/genetics/47.4.469. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BARRATT R. W., NEWMEYER D., PERKINS D. D., GARNJOBST L. Map construction in Neurospora crassa. Adv Genet. 1954;6:1–93. doi: 10.1016/s0065-2660(08)60127-3. [DOI] [PubMed] [Google Scholar]
  3. 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]
  4. Bauerle R. H., Margolin P. The functional organization of the tryptophan gene cluster in Salmonella typhimurium. Proc Natl Acad Sci U S A. 1966 Jul;56(1):111–118. doi: 10.1073/pnas.56.1.111. [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. Crawford I. P., Yanofsky C. ON THE SEPARATION OF THE TRYPTOPHAN SYNTHETASE OF ESCHERICHIA COLI INTO TWO PROTEIN COMPONENTS. Proc Natl Acad Sci U S A. 1958 Dec 15;44(12):1161–1170. doi: 10.1073/pnas.44.12.1161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Creighton T. E., Yanofsky C. Indole-3-glycerol phosphate synthetase of Escherichia coli, an enzyme of the tryptophan operon. J Biol Chem. 1966 Oct 25;241(20):4616–4624. [PubMed] [Google Scholar]
  8. DANIEL J. W., RUSCH H. P. The pure culture of Physarum polycephalum on a partially defined soluble medium. J Gen Microbiol. 1961 May;25:47–59. doi: 10.1099/00221287-25-1-47. [DOI] [PubMed] [Google Scholar]
  9. DEMOSS J. A. THE CONVERSION OF SHIKIMIC ACID TO ANTHRANILIC ACID BY EXTRACTS OF NEUROSPORA CRASSA. J Biol Chem. 1965 Mar;240:1231–1235. [PubMed] [Google Scholar]
  10. DeMoss J. A., Wegman J. An enzyme aggregate in the tryptophan pathway of Neurospora crassa. Proc Natl Acad Sci U S A. 1965 Jul;54(1):241–247. doi: 10.1073/pnas.54.1.241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Hütter R., DeMoss J. A. Enzyme analysis of the tryptophan pathway in Aspergillus nidulans. Genetics. 1967 Feb;55(2):241–247. doi: 10.1093/genetics/55.2.241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. 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]
  14. 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]
  15. 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]
  16. Mortimer R. K., Hawthorne D. C. Genetic mapping in Saccharomyces. Genetics. 1966 Jan;53(1):165–173. doi: 10.1093/genetics/53.1.165. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Roberts C. F. Complementation analysis of the tryptophan pathway in Aspergillus nidulans. Genetics. 1967 Feb;55(2):233–239. doi: 10.1093/genetics/55.2.233. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. SANDERSON K. E., DEMEREC M. THE LINKAGE MAP OF SALMONELLA TYPHIMURIUM. Genetics. 1965 Jun;51:897–913. doi: 10.1093/genetics/51.6.897. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. 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]
  20. Wegman J., DeMoss J. A. The enzymatic conversion of anthranilate to indolylglycerol phosphate in Neurospora crassa. J Biol Chem. 1965 Oct;240(10):3781–3788. [PubMed] [Google Scholar]
  21. 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]
  22. YANOFSKY C. The tryptophan synthetase system. Bacteriol Rev. 1960 Jun;24(2):221–245. doi: 10.1128/br.24.2.221-245.1960. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES