Estudo funcional do gene gluc31 que codifica uma β-1,3-glucanase da família GH16 de Trichoderma harzianum

• Autor(a) principal: Ribeiro, Marcela Suriani
• Data de Publicação: 2017
• Tipo de documento: Tese
• Idioma: por
• Título da fonte: Repositório Institucional da UFG
• dARK ID: ark:/38995/0013000006wwq
• Texto Completo: http://repositorio.bc.ufg.br/tede/handle/tede/7346
• topic: Deleção de genes; Fungos filamentosos; Parede celular; Glicosil hidrolases; Gene deletion; Filamentous fungi; Cell wall; Glycosyl hydrolase; CIENCIAS BIOLOGICAS::GENETICA

The genus Trichoderma includes species that have the ability to antagonize plant pathogens in a complex process ranging from antibiosis, competition for nutrients, mycoparasitism and induction of defense mechanisms in plants or a combination of these. Trichoderma species are known for their ability to produce lytic enzymes such as exoglucanases, endoglucanases, chitinases, and proteases that is essential for phytopathogen cell wall degradation. In the development and differentiation processes of Trichoderma, β-glucanases contributes significantly to the morphogenetic-morphological process that lead to the presence of β-glucans as the main component of fungi wall. In this work, we studied the functional role of the gluc31 gene that encodes an endo β-1,3-glucanase of the GH16 family of Trichoderma harzianum ALL42 through the deletion of this gene. This study demonstrated that the absence of Δgluc31 gene did not affect the in vivo mycoparasitism ability of the mutant T. harzianum ALL42, however the involvement of this gene in cell wall remodeling and synthesis were demonstrated. In the absence of the gluc31 gene, a higher deposition of chitin polymers on the cell wall of the mutant hyphae was observed. The absence of the gluc31 gene in T. harzianum also demonstrated an effect on the expression of other genes belonging to the family 16 of glycosyl hydrolases, due to the function redundancy found among the glucanases.