Molecular characterization of a novel β-1,3-exoglucanase related to mycoparasitism of Trichoderma harzianum

Rachel Cohen-Kupiec*, Karen E. Broglie, Dana Friesem, Richard M. Broglie, Ilan Chet

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

93 Scopus citations

Abstract

Trichoderma harzianum, a soil-borne filamentous fungus, is capable of parasitizing several plant pathogenic fungi secretion of lytic enzymes, mainly glucanases and chitinases, is considered the most crucial step of the mycoparasitic process. The lytic enzymes degrade the cell walls of the pathogenic fungi, enabling Trichoderma to utilize both their cell walls and cellular contents for nutrition. We have purified a 110 kDa novel extracellular β-1,3-exoglucanase from T. harzianum, grown with taminarin or in dual cultures with host fungi. The corresponding gene, lam1.3, and its cDNA were isolated and their nucleotide sequences determined. The deduced amino-acid sequence predicted a molecular mass of 110.7 kDa of a mature protein excluding a signal peptide. LAM1.3 showed high homology to EXG, a β- 1,3-exoglucanase of the phytopathogenic fungus Cochliobolus carbonum, and a lower homology to BGN13.1, a β-1,3-endoglucanase: isolated from T. harzianum. However, it contains a unique C-terminal embodying cysteine motifs. The expression of lam1.3 in growth with laminarin, but not with glucose, was found to be a result of differential accumulation of the corresponding mRNA.

Original languageEnglish
Pages (from-to)147-154
Number of pages8
JournalGene
Volume226
Issue number2
DOIs
StatePublished - 21 Jan 1999

Keywords

  • Antagonism
  • Cell wall
  • Laminarin
  • Lytic enzymes

Fingerprint

Dive into the research topics of 'Molecular characterization of a novel β-1,3-exoglucanase related to mycoparasitism of Trichoderma harzianum'. Together they form a unique fingerprint.

Cite this