Skip to main content
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1978 May;134(2):470–475. doi: 10.1128/jb.134.2.470-475.1978

Localization of beta-(1,3)-glucanase in the mycelium of Sclerotium rolfsii.

G Kritzman, I Chet, Y Henis
PMCID: PMC222275  PMID: 350824

Abstract

The role of the lytic enzyme beta-(1,3)-glucanase in cell wall synthesis and its distribution in the mycelium of the fungus Sclerotium rolfsii were studied. Enzyme activity was determined after enzyme extraction with Triton X-100 from a cell wall preparation. Specific zones of immunofluorescence appeared in the hyphal tips, clamp connections, new septa, and lateral branching when a specific antiserum was used with the indirect method of the fluorescent antibody staining. Enzymatic activity in the cell wall preparation was inactivated by diethylpyrocarbonate. However, 69% of the total enzymatic activity was present in a latent form which was not affected by the ester. This result suggests that most of the beta-(1,3)-glucanase was present along the hyphal cell walls in a "masked" form. An active enzyme appeared only in those regions which showed immunofluorescence. The activity of glucan synthetase, an enzyme essential for wall formation, was higher in the branching funus grown on L-threonine-supplemented synthetic medium than in the synthetic medium-grown fungus.

Full text

PDF
475

Images in this article

Selected References

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

  1. Chet I., Henis Y., Mitchell R. Chemical composition of hyphal and sclerotial walls of Sclerotium rolfsii Sacc. Can J Microbiol. 1967 Feb;13(2):137–141. doi: 10.1139/m67-019. [DOI] [PubMed] [Google Scholar]
  2. Comp P. C., Lester G. Properties of an extracellular -galactosidase secreted by Neurospora crassa. J Bacteriol. 1971 Jul;107(1):162–167. doi: 10.1128/jb.107.1.162-167.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Friebe B., Holldorf A. W. Control of Extracellular beta-1,3-glucanase activity in a basidiomycete species. J Bacteriol. 1975 Jun;122(3):818–825. doi: 10.1128/jb.122.3.818-825.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Goldberg E. Lactic and Malic Dehydrogenases in Human Spermatozoa. Science. 1963 Feb 15;139(3555):602–603. doi: 10.1126/science.139.3555.602. [DOI] [PubMed] [Google Scholar]
  5. Grove S. N., Bracker C. E. Protoplasmic organization of hyphal tips among fungi: vesicles and Spitzenkörper. J Bacteriol. 1970 Nov;104(2):989–1009. doi: 10.1128/jb.104.2.989-1009.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Higgins M. L., Shockman G. D. Procaryotic cell division with respect to wall and membranes. CRC Crit Rev Microbiol. 1971 May;1(1):29–72. doi: 10.3109/10408417109104477. [DOI] [PubMed] [Google Scholar]
  7. Jones D., Gordon A. H., Bacon J. S. Co-operative action by endo- and exo-beta-(1 leads to 3)-glucanases from parasitic fungi in the degradation of cell-wall glucans of Sclerotinia sclerotiorum (Lib.) de Bary. Biochem J. 1974 Apr;140(1):47–55. doi: 10.1042/bj1400047. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Kritzman G., Chet I., Henis Y. The relationship between rhythmic hyphal growth and circadian formation of sclerotia in Sclerotium rolfsii Sacc. Can J Microbiol. 1977 Aug;23(8):959–963. doi: 10.1139/m77-143. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. Ne'eman Z., Kahane I., Razin S. Characterization of the mycoplasma membrane proteins. II. Solubilization and enzymic activities of Acholeplasma laidlawii membrane proteins. Biochim Biophys Acta. 1971 Oct 12;249(1):169–176. doi: 10.1016/0005-2736(71)90093-9. [DOI] [PubMed] [Google Scholar]
  11. REESE E. T., MANDELS M. Beta-D-1, 3 Glucanases in fungi. Can J Microbiol. 1959 Apr;5(2):173–185. doi: 10.1139/m59-022. [DOI] [PubMed] [Google Scholar]
  12. Solymosy F., Fedorcsák I., Gulyás A., Farkas G. L., Ehrenberg L. A new method based on the use of diethyl pyrocarbonate as a nuclease inhibitor for the extraction of undegraded nucleic acid from plant tissues. Eur J Biochem. 1968 Sep 24;5(4):520–527. doi: 10.1111/j.1432-1033.1968.tb00401.x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES