Proteome-Wide Analysis of Lysine 2-Hydroxyisobutyrylation in Aspergillus niger in Peanuts.

Manlin Xu,Xia Zhang,Kang He,Ying Li,Zhiqing Guo,Jing Yu,Yucheng Chi,Xinying Song,Guowei Li

doi:10.3389/fmicb.2021.719337

Abstract

Aspergillus niger is a very destructive pathogen causing severe peanut root rot, especially in the seeding stage of peanuts (Arachis hypogaea), and often leading to the death of the plant. Protein lysine 2-hydroxyisobutyrylation (Khib) is a newly detected post-translational modification identified in several species. In this study, we identified 5041 Khib sites on 1,453 modified proteins in A. niger. Compared with five other species, A. niger has conserved and novel proteins. Bioinformatics analysis showed that Khib proteins are widely distributed in A. niger and are involved in many biological processes. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses revealed that Khib proteins were significantly enriched in many cellular compartments and pathways, such as ribosomes and proteasome subunits. A total of 223 Khib proteins were part of the PPI network, thus, suggesting that Khib proteins are associated with a large range of protein interactions and diverse pathways in the life processes of A. niger. Several identified proteins are involved in pathogenesis regulation. Our research provides the first comprehensive report of Khib and an extensive database for potential functional studies on Khib proteins in this economically important fungus.

Highlights

Protein post-translational modifications (PTMs) are important regulatory mechanisms that introduce new functionalities and dynamically control protein activity by modulating intra- and intermolecular interactions, enhancing protein capabilities
In the experimental procedures (Supplementary Figure 1A) used to identify Khib proteins and Khib sites in A. niger, three biological repeats were examined under the same experimental conditions
A total of 64,059 secondary mass spectrograms were obtained by mass spectrometry analysis

Summary

Introduction

Protein post-translational modifications (PTMs) are important regulatory mechanisms that introduce new functionalities and dynamically control protein activity by modulating intra- and intermolecular interactions, enhancing protein capabilities. With the development of highthroughput technologies such as mass spectrometry (MS), increasing numbers of modifications have been identified and functionally analyzed (Yuan et al, 2014), including ubiquitylation, phosphorylation, lysine acylation, crotonylation, succinylation, malonylation, β-hydroxybutyrylation, and 2hydroxyisobutyrylation (Allfrey et al, 1964; Tan et al, 2011; Xie et al, 2012, 2016; Medina and Avila, 2015; Meyer et al, 2016; Nandakumar et al, 2021). These studies have revealed that newly identified modifications have specific effects on cell growth, differentiation, metabolism, and other life processes

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Conclusion