INVESTIGADORES
CASTRILLO Maria lorena
congresos y reuniones científicas
Título:
In silico analysis of the regulatory regions of genes encoding chitinases involved in the mycoparasitism of Trichoderma koningiopsis POS7.
Autor/es:
AMERIO, NS; CASTRILLO, ML; BARENGO, MP; BICH, GA; ZAPATA, PD; VILLALBA, LL
Lugar:
Modalidad virtual
Reunión:
Congreso; 1st Latin American Congress of Women in Bioinformatics and Data Science 2020; 2020
Resumen:
Chitinolytic enzymes of Trichoderma are stable macromolecules compatible with the development of applicable enzyme cocktails for the control of a wide range of phytopathogenic fungi. To study the mechanisms of induction or repression of these enzymes is necessary to know the regulatory regions of the genes that encode them. Our objective was to predict in silico the potential regulatory motives involved in the activation of the synthesis of these enzymes with biocontrol ability, in T. koningiopsis POS7 genome. From the seven characterized genes encoding chitinases from the T. koningiopsis POS7 isolate, the response elements were located using the Geneious 9.1.5 bioinformatics software. It was possible to identify many response elements in the regulatory region of all the genes encoding chitinases. The regions related to catabolic repression by carbon (Cre1 / CreA) and those related to catabolic repression by nitrogen (AreA) predominated in relation to their presence and copy numbers (between two and eight) in all the genes characterized. The elements of physiological stress response (STRE) and binding sites for the pH regulatory protein (PacC) predominated for this set of genes also, appearing in most of them in a number of one or two copies per gene. The analysis carried out highlights that the expression of the genes encoding chitinases of the T. koningiopsis POS7 genome could be related to catabolic repression by carbon and nitrogen sources, in addition to stress and pH conditions. This knowledge will be a favorable and innovative impulse to increase the production of those target enzymes at a technological level.