Abstract
Calpains are ubiquitous and well-conserved proteins that belong to the calcium-dependent, non-lysosomal cysteine protease family. In this study, 8 putative calpains were identified using Pfam domain analysis and BlastP searches in M. oryzae. Three single gene deletion mutants (ΔMocapn7, ΔMocapn9 and ΔMocapn14) and two double gene deletion mutants (ΔMocapn4ΔMocapn7 and ΔMocapn9ΔMocapn7) were obtained using the high-throughput gene knockout system. The calpain disruption mutants showed defects in colony characteristics, conidiation, sexual reproduction and cell wall integrity. The mycelia of the ΔMocapn7, ΔMocapn4ΔMocapn7 and ΔMocapn9ΔMocapn7 mutants showed reduced pathogenicity on rice and barley.
Highlights
Magnaporthe oryzae is considered an excellent model for studying the interactions between plants and fungi[17]
Ubiquitin-mediated proteolysis of target proteins plays an important role in nutrient assimilation, development and pathogenicity of M. oryzae[22,23,31]
We elucidate the pivotal functions of calpains, an overlooked protein degradation system in M. oryzae
Summary
Magnaporthe oryzae is considered an excellent model for studying the interactions between plants and fungi[17]. The ΔMocapn[9] and ΔMocapn[14] mutants were similar with the wild-type strain Guy[11] and developed multiple conidiophores with pyriform conidia sympodially arrayed at 24 h post-conidial induction (Fig. 3B). We crossed Guy[11] and the calpain gene deletion mutants with the 2539 strain (described in the Experimental procedures).
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