Comprehensive identification of lysine 2‐hydroxyisobutyrylated proteins in <i>Ustilaginoidea virens</i> reveals the involvement of lysine 2‐hydroxyisobutyrylation in fungal virulence

Chen, Xiaoyang; Li, Xiabing; Li, Pingping; Líu, Hao; Huang, Junbin; Luo, Chaoxi; Hsiang, Tom; Zheng, Lu

doi:10.1111/jipb.13066

Cited by 27 publications

(33 citation statements)

References 54 publications

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“…Khib has recently been reported in F. oxysporum , B. cinerea , and U. virens . In U. virens , disruption of 2-hydroxyisobutyrylation in the MAPK pathway kinase UvSlt2 by mutation decreases fungal virulence ( Chen et al, 2021 ). In the comprehensive analysis of F. oxysporum , critical proteins for virulence – FoFmk1, FoHog1 and two MAP kinase signaling proteins – have been identified ( Qian et al, 2021 ); For B. cinerea , many 2-hydroxyisobutyrylated proteins are involved in substance synthesis and metabolism, redox and autophagy, kinase and protease, and are associated with the pathogenicity of B. cinerea ( Xu et al, 2020 ).…”

Section: Discussionmentioning

confidence: 99%

“…Large amounts of Khib have been reported in plants, such as developing rice seeds ( Meng et al, 2017 ), common wheat ( Bo et al, 2021 ; Zhang et al, 2021 ) and Physcomitrella patens ( Yu et al, 2017 ); Histone H4K8 2-hydroxyisobutyrylation (H4K8 hib) has been identified as an evolutionarily conserved modification in Saccharomyces cerevisiae ( Huang et al, 2017 ). Some reports have described Khib in biological pathogens, such as the animal pathogens Proteus mirabilis , Toxoplasma gondii , and Candida albicans ( Dong et al, 2018 ; Yin et al, 2019 ; Zheng et al, 2021 ), Khib in plant pathogens has also been reported, such as Fusarium oxysporum , Botrytis cinerea , and Ustilaginoidea virens ( Xu et al, 2020 ; Chen et al, 2021 ; Qian et al, 2021 ). Reports on these three pathogens have revealed that Khib is widely distributed in cellular compartments and is involved in diverse cellular processes, including regulation of pathogenicity and virulence.…”

Section: Introductionmentioning

confidence: 99%

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

Xu¹,

Zhang²,

Yu³

et al. 2021

Front. Microbiol.

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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.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Xu¹,

Zhang²,

Yu³

et al. 2021

Front. Microbiol.

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“…In Escherichia coli, CobB serves as a K hib deacylase (Dong et al, 2019). UvRpd3 was recently reported to function as the main enzyme that removes K hib in Ustilaginoidea virens (Chen et al, 2021). However, the key regulatory enzymes involved in K hib homeostasis in rice have not been identified.…”

Section: Introductionmentioning

confidence: 99%

Ustilaginoidea virens modulates lysine 2‐hydroxyisobutyrylation in rice flowers during infection

Chen

Duan

et al. 2021

JIPB

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The post-translational modification lysine 2hydroxyisobutyrylation (K hib ) plays an important role in gene transcription, metabolism, and enzymatic activity. K hib sites have been identified in rice (Oryza sativa). However, the K hib status of proteins in rice flowers during pathogen infection remains unclear. Here, we report a comprehensive identification of K hib -modified proteins in rice flowers, and the changes in these proteins during infection with the fungal pathogen Ustilaginoidea virens. By using a tandem mass tag-based quantitative proteomics approach, we identified 2,891 K hib sites on 964 proteins in rice flowers. Our data demonstrated that 2-hydroxyisobutyrylated proteins are involved in diverse biological processes. K hib levels were substantially reduced upon infection with U. virens. Chromatin immunoprecipitation polymerase chain reaction (PCR) and reverse transcription quantitative PCR analyses revealed that histone K hib is involved in the expression of disease-resistance genes. More importantly, most quantified sites on core histones H3 were downregulated upon U. virens infection. In addition, the histone deacetylases HDA705, HDA716, SRT1, and SRT2 are involved in the removal of K hib marks in rice. HDA705 was further confirmed to negatively regulate rice disease resistance to pathogens U. virens, Magnaporthe oryzae, and Xanthomonas oryzae pv. oryzae (Xoo). Our data suggest that U. virens could modulate K hib in rice flowers during infection.

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“…However, there was evidence that K hib modification may introduce the conformational changes of Enolase1 and alter the substrate binding [ 148 ]. K hib increased the hydrophobic solvent-accessible surface area and decreased the enzymatic activity of UvSlt2 [ 149 ].…”

Section: Starch Biosynthesis-related Proteins Targeted By Ptmsmentioning

confidence: 99%

Proteomics and Post-Translational Modifications of Starch Biosynthesis-Related Proteins in Developing Seeds of Rice

Tappiban

Bao

2021

IJMS

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Rice (Oryza sativa L.) is a foremost staple food for approximately half the world’s population. The components of rice starch, amylose, and amylopectin are synthesized by a series of enzymes, which are responsible for rice starch properties and functionality, and then affect rice cooking and eating quality. Recently, proteomics technology has been applied to the establishment of the differentially expressed starch biosynthesis-related proteins and the identification of posttranslational modifications (PTMs) target starch biosynthesis proteins as well. It is necessary to summarize the recent studies in proteomics and PTMs in rice endosperm to deepen our understanding of starch biosynthesis protein expression and regulation, which will provide useful information to rice breeding programs and industrial starch applications. The review provides a comprehensive summary of proteins and PTMs involved in starch biosynthesis based on proteomic studies of rice developing seeds. Starch biosynthesis proteins in rice seeds were differentially expressed in the developing seeds at different developmental stages. All the proteins involving in starch biosynthesis were identified using proteomics methods. Most starch biosynthesis-related proteins are basically increased at 6–20 days after flowering (DAF) and decreased upon the high-temperature conditions. A total of 10, 14, 2, 17, and 7 starch biosynthesis related proteins were identified to be targeted by phosphorylation, lysine acetylation, succinylation, lysine 2-hydroxyisobutyrylation, and malonylation, respectively. The phosphoglucomutase is commonly targeted by five PTMs types. Research on the function of phosphorylation in multiple enzyme complex formation in endosperm starch biosynthesis is underway, while the functions of other PTMs in starch biosynthesis are necessary to be conducted in the near future.

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Comprehensive identification of lysine 2‐hydroxyisobutyrylated proteins in Ustilaginoidea virens reveals the involvement of lysine 2‐hydroxyisobutyrylation in fungal virulence

Cited by 27 publications

References 54 publications

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

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

Ustilaginoidea virens modulates lysine 2‐hydroxyisobutyrylation in rice flowers during infection

Proteomics and Post-Translational Modifications of Starch Biosynthesis-Related Proteins in Developing Seeds of Rice

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