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Correction published on 24 May 2021, see Int. J. Mol. Sci. 2021, 22(11), 5531.
Article

Genome-Wide Identification of M35 Family Metalloproteases in Rhizoctonia cerealis and Functional Analysis of RcMEP2 as a Virulence Factor during the Fungal Infection to Wheat

by 1,2,†, 2,†, 3,†, 1, 1 and 1,*
1
Institute of Crop Sciences, National Key Facility for Crop Gene Resources and Genetic Improvement, Chinese Academy of Agricultural Sciences, Beijing 100081, China
2
College of Agriculture, Hunan Agricultural University, Changsha 410128, China
3
College of Plant Protection, Shandong Agricultural University; Taian 271018, China
*
Author to whom correspondence should be addressed.
These authors contributed equally to this work.
Int. J. Mol. Sci. 2020, 21(8), 2984; https://doi.org/10.3390/ijms21082984
Received: 31 March 2020 / Revised: 18 April 2020 / Accepted: 20 April 2020 / Published: 23 April 2020
(This article belongs to the Section Molecular Biology)
Rhizoctonia cerealis is the causal pathogen of the devastating disease, sharp eyespot, of the important crop wheat (Triticum aestivum L.). In phytopathogenic fungi, several M36 metalloproteases have been implicated in virulence, but pathogenesis roles of M35 family metalloproteases are largely unknown. Here, we identified four M35 family metalloproteases from R. cerealis genome, designated RcMEP2–RcMEP5, measured their transcriptional profiles, and investigated RcMEP2 function. RcMEP2-RcMEP5 are predicted as secreted metalloproteases since each protein sequence contains a signal peptide and an M35 domain that includes two characteristic motifs HEXXE and GTXDXXYG. Transcription levels of RcMEP2-RcMEP5 markedly elevated during the fungus infection to wheat, among which RcMEP2 expressed with the highest level. Functional dissection indicated that RcMEP2 and its M35 domain could trigger H2O2 rapidly-excessive accumulation, induce cell death, and inhibit expression of host chitinases. This consequently enhanced the susceptibility of wheat to R. cerealis and the predicated signal peptide of RcMEP2 functions required for secretion and cell death-induction. These results demonstrate that RcMEP2 is a virulence factor and that its M35 domain and signal peptide are necessary for the virulence role of RcMEP2. This study facilitates a better understanding of the pathogenesis mechanism of metalloproteases in phytopathogens including R. cerealis. View Full-Text
Keywords: cell death; M35 metalloprotease; reactive oxygen species; Rhizoctonia cerealis; virulence; wheat (Triticum aestivum L.) cell death; M35 metalloprotease; reactive oxygen species; Rhizoctonia cerealis; virulence; wheat (Triticum aestivum L.)
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MDPI and ACS Style

Pan, L.; Wen, S.; Yu, J.; Lu, L.; Zhu, X.; Zhang, Z. Genome-Wide Identification of M35 Family Metalloproteases in Rhizoctonia cerealis and Functional Analysis of RcMEP2 as a Virulence Factor during the Fungal Infection to Wheat. Int. J. Mol. Sci. 2020, 21, 2984. https://doi.org/10.3390/ijms21082984

AMA Style

Pan L, Wen S, Yu J, Lu L, Zhu X, Zhang Z. Genome-Wide Identification of M35 Family Metalloproteases in Rhizoctonia cerealis and Functional Analysis of RcMEP2 as a Virulence Factor during the Fungal Infection to Wheat. International Journal of Molecular Sciences. 2020; 21(8):2984. https://doi.org/10.3390/ijms21082984

Chicago/Turabian Style

Pan, Lijun, Shengxian Wen, Jinfeng Yu, Lin Lu, Xiuliang Zhu, and Zengyan Zhang. 2020. "Genome-Wide Identification of M35 Family Metalloproteases in Rhizoctonia cerealis and Functional Analysis of RcMEP2 as a Virulence Factor during the Fungal Infection to Wheat" International Journal of Molecular Sciences 21, no. 8: 2984. https://doi.org/10.3390/ijms21082984

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