1887

Microbiology Society logo

Volume 140, Issue 9

Enzyme inactivation related to a hyperoxidant state during conidiation of Free

Abstract

The conidiation process of is characterized by three morphogenetic steps: hyphal adhesion, aerial hyphal formation, and production of conidia. Previous data indicated the occurrence of a hyperoxidant state at the onset of all three morphogenetic steps. Because glutamine synthetase (GS) and the biosynthetic glutamate dehydrogenase [GDH(NADP)] enzymes are susceptible to inactivation by reactive oxygen species, we followed these enzyme activities during conidiation and under different physiological conditions and related them to the hyperoxidant states and morphogenesis. Loss of GS activity occurred prior to all three morphogenetic steps, coinciding with an increase in total protein oxidation. Oxidized GS polypeptides were detected during hyphal adhesion. Loss of GDH(NADP) activity also occurred during hyphal adhesion and before aerial hyphal formation; the enzyme polypeptide and activity decreased in the adhered hyphae to low values and no GDH(NADP) was detected in aerial hyphae. The catabolic GDH [GDH(NAD)] behaved in an opposite manner, increasing its activity during hyphal adhesion and aerial hyphae development. These results are discussed with regard to cell differentiation and the conidiation process in .

  • Received:
  • Accepted:
  • Revised:
  • Published Online:
Keyword(s): glutamate dehydrogenase , glutamine synthetase , oxygen radicals , protein oxidation and sporulation
© Society for General Microbiology 1994
Loading

Article metrics loading...

/content/journal/micro/10.1099/13500872-140-9-2391
1994-09-01
2024-04-20
Loading full text...

Full text loading...

/deliver/fulltext/micro/140/9/mic-140-9-2391.html?itemId=/content/journal/micro/10.1099/13500872-140-9-2391&mimeType=html&fmt=ahah

References

  1. Aguirre J., Hansberg W. 1986; Oxidation of Neurospora crassa glutamine synthetase. J Bacteriol 166:1040–1045
     [Google Scholar]
  2. Aguirre J., Rodriguez R., Hansberg W. 1989; Oxidation of Neurospora crassa NADP-specific glutamate dehydrogenase by activated oxygen species. J Bacteriol 171:6243–6250
     [Google Scholar]
  3. Ahn B., Rhee S. G., Stadtman E. R. 1987; Use of fluorescein hydrazide and fluorescein thiocarbazide reagents for the fluoro-metric of protein carbonyl groups and for the detection of oxidized protein on polyacrylamide gels. Anal Biochem 161:245–257
     [Google Scholar]
  4. Cardenas M.E., Hansberg W. 1984; Glutamine metabolism during aerial mycelium growth of Neurospora crassa. J Gen Microbiol 130:1733–1744
     [Google Scholar]
  5. Ferguson A.R., Sims A. P. 1971; Inactivation in vivo of glutamine synthetase and NAD-specific glutamate dehydrogenase: its role in the regulation of glutamine synthesis in yeast. J Gen Microbiol 69:423–427
     [Google Scholar]
  6. Fincham J.R.S. 1957; A modified glutamic acid dehydrogenase as a result of gene mutation in Neurospora crassa. Biochem J 65:721–728
     [Google Scholar]
  7. Halliwell B., Gutteridge J. M. C. 1990; Role of free radicals and catalytic metal ions in human disease: an overview. Methods Enzymol 186:1–85
     [Google Scholar]
  8. Hansberg W., Aguirre J. 1990; Hyperoxidant states cause microbial cell differentiation by cell isolation from dioxygen. J Theor Biol 142:201–221
     [Google Scholar]
  9. Hansberg W., de Groot H., Sies H. 1993; Reactive oxygen species associated with cell differentiation in Neurospora crassa.. Free Rad Biol and Med 14:287–293
     [Google Scholar]
  10. Kinsey J.A., Hung B. T. 1981; Mutation at the am locus of Neurospora crassa.. Genetics 99:405–414
     [Google Scholar]
  11. Mora Y., Chavez O., Mora J. 1980; Regulation of Neurospora crassa glutamine synthetase by the carbon and nitrogen source. J Gen Microbiol 118:455–463
     [Google Scholar]
  12. O'Farrell P. H. 1975; High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250:4007–4021
     [Google Scholar]
  13. Sanchez F., Campomanes M., Quinto C., Hansberg W., Mora J., Palacios R. 1978; Nitrogen source regulates glutamine synthetase mRNA levels in Neurospora crassa. J Bacteriol 136:880–885
     [Google Scholar]
  14. Sanchez F., Calva E., Campomanes M., Blanco L, Guzman J., Saborio J. L., Palacios R. 1980; Heterogeneity of glutamine synthetase polypeptides in Neurospora crassa. J Biol Chem 255:2231–2234
     [Google Scholar]
  15. Sies H., Akerboom P. M. 1984; Glutathione disulfide (GSSG) efflux cells and tissues. Methods Ensymol 105:445–451
     [Google Scholar]
  16. Springer M.L., Yanofsky C. 1989; A morphological and genetic analysis of the conidiophore development in Neurospora crassa.. Genes Devel 3:559–571
     [Google Scholar]
  17. Toledo I., Hansberg W. 1990; Protein oxidation related to morphogenesis in Neurospora crassa. Exp Mycol 14:184–189
     [Google Scholar]
  18. Toledo I., Aguirre J., Hansberg W. 1986; Aerial growth in Neurospora crassa: characterization of an experimental model system.. Exp Mycol 10:114–125
     [Google Scholar]
  19. Toledo I., Noronha-Dutra A.A., Hansberg W. 1991; Loss of NAD(P)-reducing power and glutathione disulfide excretion at the start of induction of aerial growth in Neurospora crassa. J Bacteriol 173:3243–3249
     [Google Scholar]
  20. Vogel H.J. 1964; Distribution of lysine pathways among fungi: evolutionary implication. Am Nat 98:435–446
     [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/13500872-140-9-2391
Loading
Enzyme inactivation related to a hyperoxidant state during conidiation of Neurospora crassa
Microbiology 140, 2391 (1994); https://doi.org/10.1099/13500872-140-9-2391
/content/journal/micro/10.1099/13500872-140-9-2391
/content/journal/micro/10.1099/13500872-140-9-2391
Loading

Data & Media loading...

Most cited Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error