Sir2‐mediated cytoplasmic deacetylation facilitates pathogenic fungi infection in host plants

Author:

Zhang Ning1ORCID,Hu Jicheng1,Liu Zhishan1,Liang Wenxing1ORCID,Song Limin1

Affiliation:

1. College of Plant Health and Medicine, Engineering Research Center for Precision Pest Management for Fruits and Vegetables of Qingdao, Shandong Engineering Research Center for Environment‐Friendly Agricultural Pest Management, Shandong Province Key Laboratory of Applied Mycology Qingdao Agricultural University Qingdao 266109 China

Abstract

Summary Lysine acetylation is an evolutionarily conserved and widespread post‐translational modification implicated in the regulation of multiple metabolic processes, but its function remains largely unknown in plant pathogenic fungi. A comprehensive analysis combined with proteomic, molecular and cellular approaches was presented to explore the roles of cytoplasmic acetylation in Fusarium oxsysporum f.sp. lycopersici (Fol). The divergent cytoplasmic deacetylase FolSir2 was biochemically characterized, which is contributing to fungal virulence. Based on this, a total of 1752 acetylated sites in 897 proteins were identified in Fol via LC–MS/MS analysis. Further analyses of the quantitative acetylome revealed that 115 proteins representing two major pathways, translational and ribosome biogenesis, were hyperacetylated in the ∆Folsir2 strain. We experimentally examined the regulatory roles of FolSir2 on K271 deacetylation of FolGsk3, a serine/tyrosine kinase implicated in a variety of cellular functions, which was found to be crucial for the activation of FolGsk3 and thus modulated Fol pathogenicity. Cytoplasmic deacetylation by FolSir2 homologues has a similar function in Botrytis cinerea and likely other fungal pathogens. These findings reveal a conserved mechanism of silent information regulator 2‐mediated cytoplasmic deacetylation that is involved in plant‐fungal pathogenicity, providing a candidate target for designing broad‐spectrum fungicides to control plant diseases.

Funder

National Natural Science Foundation of China

Publisher

Wiley

Subject

Plant Science,Physiology

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