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J. Bacteriol., Dec 1995, 6937-6945, Vol 177, No. 23
J de la Cruz, JA Pintor-Toro, T Benitez, A Llobell and LC Romero
The mycoparasitic fungus Trichoderma harzianum CECT 2413 produces at least
three extracellular beta-1,3-glucanases. The most basic of these
extracellular enzymes, named BGN13.1, was expressed when either fungal cell
wall polymers or autoclaved mycelia from different fungi were used as the
carbon source. BGN13.1 was purified to electrophoretic homogeneity and was
biochemically characterized. The enzyme was specific for beta-1,3 linkages
and has an endolytic mode of action. A synthetic oligonucleotide primer
based on the sequence of an internal peptide was designed to clone the cDNA
corresponding to BGN13.1. The deduced amino acid sequence predicted a
molecular mass of 78 kDa for the mature protein. Analysis of the amino acid
sequence indicates that the enzyme contains three regions, one N-terminal
leader sequence; another, nondefined sequence; and one cysteine-rich
C-terminal sequence. Sequence comparison shows that this
beta-1,3-glucanase, first described for filamentous fungi, belongs to a
family different from that of its previously described bacterial, yeast,
and plant counterparts. Enzymatic-activity, protein, and mRNA data
indicated that bgn13.1 is repressed by glucose and induced by either fungal
cell wall polymers or autoclaved yeast cells and mycelia. Finally,
experimental evidence showed that the enzyme hydrolyzes yeast and fungal
cell walls.
Copyright © 1995, American Society for Microbiology
A novel endo-beta-1,3-glucanase, BGN13.1, involved in the mycoparasitism of Trichoderma harzianum
Instituto de Bioquimica Vegetal y Fotosintesis, Consejo Superior de Investigaciones Cientificas y Universidad de Sevilla, Spain.
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