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Updated: Jul 28, 2026

Detection of Histone Modifications in Plant Leaves
Published on: September 23, 2011
Multiple environmental signals determine the transcriptional activation of the mycoparasitism related gene prb1 in
V Olmedo-Monfil1, A Mendoza-Mendoza, I Gómez
1Department of Plant Genetic Engineering, Centro de Investigación y Estudios Avanzados, Unidad Irapuato, Apartado Postal 629, 36500 Irapuato, Gto., México.
Abstract:
Trichoderma atroviride parasitizes a large variety of phytopathogenic fungi. This characteristic has allowed its use as a biological control agent. The production of hydrolytic enzymes appears to be a key element in the parasitic process. Among the enzymes released by Trichoderma, the proteinase Prb1 plays a major role. We show here that the corresponding gene ( prb1) is subject to nitrogen catabolite repression. Accordingly, induction of prb1 transcription by Rhizoctonia solani cell walls and by osmotic stress requires release from a repressed condition, which is determined by nitrogen availability. Furthermore, the transcription pattern of the prb1 gene was not affected when an inhibitor of p38-Hog1, a regulator of the response to osmotic shock, was used. In contrast, a MEK1/2 (MAPK/ERK) inhibitor blocked prb1 transcription in response to nitrogen limitation, indicating that the pathway employed in the nitrogen response involves proteins similar to p42-p44. Fusion of the prb1 promoter to the gfp reporter gene allowed the detection of a novel regulatory element, providing an initial insight into the nature of the sites that control prb1 expression.
Insights
Trichoderma atroviride uses proteinase Prb1 for fungal control. Its gene expression is regulated by nitrogen availability and involves MAPK/ERK signaling pathways, not p38-Hog1.
Area of Science:
- * Mycology
- * Biocontrol
- * Molecular Biology
Background:
- * *Trichoderma atroviride* is a mycoparasitic fungus utilized as a biological control agent against plant pathogens.
- * Hydrolytic enzymes, particularly proteinase Prb1, are crucial for its parasitic activity.
- * Understanding the regulation of these enzymes is key to optimizing biocontrol strategies.
Purpose of the Study:
- * To investigate the regulatory mechanisms controlling the expression of the *prb1* gene in *T. atroviride*.
- * To determine the role of nitrogen availability and osmotic stress in *prb1* gene induction.
- * To elucidate the signaling pathways involved in *prb1* gene regulation.
Main Methods:
- * Analysis of *prb1* gene transcription under varying nitrogen conditions and osmotic stress.
- * Use of specific inhibitors for p38-Hog1 and MEK1/2 (MAPK/ERK) signaling pathways.
- * Construction of a *prb1* promoter-GFP reporter fusion to identify regulatory elements.
Main Results:
- * *prb1* gene expression is subject to nitrogen catabolite repression, requiring derepression for induction.
- * Induction of *prb1* by fungal cell walls and osmotic stress is dependent on nitrogen availability.
- * MEK1/2 (MAPK/ERK) pathway, but not p38-Hog1, is involved in the nitrogen-dependent regulation of *prb1* transcription.
- * A novel regulatory element controlling *prb1* expression was identified using a GFP reporter system.
Conclusions:
- * Nitrogen availability is a critical factor regulating the expression of the key enzyme *prb1* in *T. atroviride*.
- * The MAPK/ERK pathway plays a significant role in mediating the response to nitrogen limitation affecting *prb1* transcription.
- * The discovery of a novel regulatory element provides insights into the complex transcriptional control of *prb1* for enhanced biocontrol applications.
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