AUTHOR=Xu Yang , Li Xiaoxia , Liang Wenxing , Liu Mengjie 

TITLE=Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in the Phytopathogenic Fungus Botrytis cinerea

JOURNAL=Frontiers in Microbiology

VOLUME=11

YEAR=2020

URL=https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2020.585614

DOI=10.3389/fmicb.2020.585614

ISSN=1664-302X

ABSTRACT=<p>Posttranslational modifications (PTMs) of the whole proteome have become a hot topic in the research field of epigenetics, and an increasing number of PTM types have been identified and shown to play significant roles in different cellular processes. Protein lysine 2-hydroxyisobutyrylation (K<sub><italic>hib</italic></sub>) is a newly detected PTM, and the 2-hydroxyisobutyrylome has been identified in several species. <italic>Botrytis cinerea</italic> is recognized as one of the most destructive pathogens due to its broad host distribution and very large economic losses; thus the many aspects of its pathogenesis have been continuously studied. However, distribution and function of K<sub><italic>hib</italic></sub> in this phytopathogenic fungus are not clear. In this study, a proteome-wide analysis of K<sub><italic>hib</italic></sub> in <italic>B. cinerea</italic> was performed, and 5,398 K<sub><italic>hib</italic></sub> sites on 1,181 proteins were identified. Bioinformatics analysis showed that the 2-hydroxyisobutyrylome in <italic>B. cinerea</italic> contains both conserved proteins and novel proteins when compared with K<sub><italic>hib</italic></sub> proteins in other species. Functional classification, functional enrichment and protein interaction network analyses showed that K<sub><italic>hib</italic></sub> proteins are widely distributed in cellular compartments and involved in diverse cellular processes. Significantly, 37 proteins involved in different aspects of regulating the pathogenicity of <italic>B. cinerea</italic> were detected as K<sub><italic>hib</italic></sub> proteins. Our results provide a comprehensive view of the 2-hydroxyisobutyrylome and lay a foundation for further studying the regulatory mechanism of K<sub><italic>hib</italic></sub> in both <italic>B. cinerea</italic> and other plant pathogens.</p>