Journalartikel

Jahr der Veröffentlichung: 2021

Seiten: 4881-4895

Zeitschrift: Environmental Microbiology

Bandnummer: 23

Heftnummer: 9

ISSN: 1462-2912

eISSN: 1462-2920

DOI Link: https://doi.org/10.1111/1462-2920.15335

Verlag: Wiley

Abstract: 
ATP-dependent Lon proteases function in bacterial pathogenesis by regulating the expression of the Type III secretion system; however, little is known about how Lon proteases regulate fungal pathogenesis. We previously investigated Lon-binding proteins involved in fungal pathogenesis that interact with PrePL, the smallest Magnaporthe oryzae Lon-binding protein. Here, we show that Lon cleaves PrePL and produces Pc, an extracellular 11-kDa isoform with catalase and peroxidase activity. The Delta PrePL loss-of-function strain showed stronger sporulation and accelerated disease development, suggesting a temporally specific negative regulatory mechanism controlled by PrePL in disease progression. Neither the truncated Pc, nor the full-length PrePL missing the Lon cleavage site complemented the Delta PrePL phenotype, suggesting that full-length PrePL and Pc both function in fungal development. PrePL targeted to the mitochondria undergoes hydrolysis by Lon to produce Pc, which accumulates in the fungal apoplast. Importantly, recombinant Pc induced plant defence responses and cell death after being infiltrated into selected plant leaves, indicating that it functions as an avirulence factor. This work thus reveals a novel pathogenic factor in the fungal Lon-mediated pathway. Additionally, our results provide new insight into the functions of a full-length protein and its cleaved isoform in fungal pathogenesis.

Harvard-Zitierstil: Dang, Y., Wei, Y., Wang, Y., Liu, S., Julia, C. and Zhang, S. (2021) Cleavage of PrePL by Lon promotes growth and pathogenesis in Magnaporthe oryzae, Environmental Microbiology, 23(9), pp. 4881-4895. https://doi.org/10.1111/1462-2920.15335

APA-Zitierstil: Dang, Y., Wei, Y., Wang, Y., Liu, S., Julia, C., & Zhang, S. (2021). Cleavage of PrePL by Lon promotes growth and pathogenesis in Magnaporthe oryzae. Environmental Microbiology. 23(9), 4881-4895. https://doi.org/10.1111/1462-2920.15335