INVESTIGADORES
DIAZ RICCI Juan Carlos
congresos y reuniones científicas
Título:
Heterologous expression of AsES, an elicitor subtilisin isolated from Acremonium strictum.
Autor/es:
CARO MA. DEL PILAR; MARTÍNEZ ZAMORA, MARTÍN G.; DÍAZ RICCI, JUAN C.
Lugar:
Rosario, Santa Fe.
Reunión:
Congreso; SAIB 51º Annual Meeting; 2014
Resumen:
AsES protein, a
subtilisin like serine protease isolated from the avirulent fungus Acremonium
strictum, induces plant defence response in strawberry and other species.
Sequence analysis reveals that AsES possesses a typical pre-pro-mature
organization that consists of a signal sequence, an inhibitor domain
(pro-peptide) in the N-terminal region with chaperone function and a mature
proteinase domain with catalytic activity. The aim of this work was to obtain
AsES protein by heterologous expression in order to assess its elicitor
activity. The coding sequence of AsES pro-protein was cloned and expressed in Escherichia
coli and then purified by affinity chromatography. Proteolytic activity was
evaluated in vitro by specific substrate hydrolysis and elicitor activity was
assessed through ROS formation and protection against Colletotrichum
acutatum, the causal agent of anthracnose disease. The results of this
study suggest that AsES mature protein of 34 kDa is formed by autolysis of the
pro-peptide (45 kDa) after its expression and it is functionally active. The
mature protein can protect plants against anthracnose and produces the
accumulation of ROS at 4 hpi. Direct application of AsES recombinant protein
could be used as a new strategy for diseases biocontrol helping to reduce
agrochemicals minimizing environmental impact.