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Hybrid B heme peroxidases are recently discovered unique oxidoreductases present solely in the fungal kingdom. We have investigated two typical representatives from <i>Magnaporthe oryzae</i>—one of the most dangerous phytopathogens known as a causal agent of the rice blast disease. First, we focused on native expression of two detected <i>hyBpox</i> paralogs by the means of reverse-transcription quantitative real-time PCR. Our results indicate a 7-fold induction of the <i>MohyBpox1</i> transcript in a medium with H₂O₂ and a 3-fold induction in a medium with peroxyacetic acid. For the <i>MohyBpox2</i> paralog the induction patterns were up to 12-fold and 6.7-fold, respectively. We have successfully expressed the shorter gene, <i>MohyBpox1</i>, heterologously in <i>Pichia pastoris</i> for detailed characterization. Observed biochemical and biophysical properties of the highly purified protein reveal that a typical HyBPOX is significantly different from previously investigated APx-CcP hybrids. This newly discovered secretory peroxidase reveals a Soret maximum at 407 nm, Q bands at 532 and 568 nm, CT band at 625 nm and a purity number of 1.48. Electron paramagnetic resonance (EPR) analysis suggests a mixture of high and low spin species in the ferric state dependent on calcium contents. Steady-state kinetic data reveal the highest peroxidase activity with ABTS, 5-aminosalycilate and efficient oxidation of tyrosine. MoHyBPOX1 as a fusion protein consists of two domains. The longer conserved N-terminal peroxidase domain is connected with a shorter C-terminal domain containing a carbohydrate binding motif of type CBM21. We demonstrate the capacity of MoHyBPOX1 to bind soluble starch efficiently. Potential involvement of hybrid peroxidases in the pathogenicity of <i>M. oryzae</i> is discussed.