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. 2021 Nov 17;11(1):22383.
doi: 10.1038/s41598-021-01956-2.

Tandem Mass Tag labelling quantitative acetylome analysis of differentially modified proteins during mycoparasitism of Clonostachys chloroleuca 67-1

Na Jiang #  1 , Binna Lv #  1 , Haixia Wu  1 , Shidong Li  1 , Manhong Sun  2
Affiliations

Tandem Mass Tag labelling quantitative acetylome analysis of differentially modified proteins during mycoparasitism of Clonostachys chloroleuca 67-1

Na Jiang et al. Sci Rep. .

Abstract

Lysine acetylation (Kac) is an important post-translational modification (PTM) of proteins in all organisms, but its functions have not been extensively explored in filamentous fungi. In this study, a Tandem Mass Tag (TMT) labelling lysine acetylome was constructed, and differentially modified Kac proteins were quantified during mycoparasitism and vegetative growth in the biocontrol fungus Clonostachys chloroleuca 67-1, using liquid chromatography-tandem mass spectrometry (LC-MS/MS). A total of 1448 Kac sites were detected on 740 Kac proteins, among which 126 sites on 103 proteins were differentially regulated. Systematic bioinformatics analyses indicate that the modified Kac proteins were from multiple subcellular localizations and involved in diverse functions including chromatin assembly, glycometabolism and redox activities. All Kac sites were characterized by 10 motifs, including the novel CxxKac motif. The results suggest that Kac proteins may have effects of broadly regulating protein interaction networks during C. chloroleuca parasitism to Sclerotinia sclerotiorum sclerotia. This is the first report of a correlation between Kac events and the biocontrol activity of C. chloroleuca. Our findings provide insight into the molecular mechanisms underlying C. chloroleuca control of plant fungal pathogens regulated by Kac proteins.

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Conflict of interest statement

The authors declare no competing interests.

Figures

Figure 1
Figure 1
Properties of the identified peptides in C. chloroleuca 67–1. (A) Distribution of peptide mass errors. (B) Distribution of lysine acetylation (Kac) sites. (C) Length of Kac peptides.
Figure 2
Figure 2
Motif analysis of identified Kac sites in C. chloroleuca 67–1. (A) Kac motifs and conservation of Kac sites. The size of each letter corresponds to the frequency of the amino acid residues in a given position. (B) Heatmap of the amino acid composition of Kac sites.
Figure 3
Figure 3
Volcano plot of differentially modified Kac sites in C. chloroleuca 67–1.
Figure 4
Figure 4
GO functional distribution and subcellular localization of differentially regulated Kac proteins in C. chloroleuca 67–1. (A) Biological process classification. (B) Cellular component classification. (C) Molecular function classification. (D) Subcellular localization.
Figure 5
Figure 5
KOG functional classification of differentially regulated Kac proteins in C. chloroleuca 67–1.
Figure 6
Figure 6
Enrichment analysis of up-regulated Kac proteins in C. chloroleuca 67–1. (A) GO-based enrichment analysis. (B) KEGG pathway-based enrichment analysis.
Figure 7
Figure 7
Domain-based enrichment analysis of all differentially regulated Kac proteins in C. chloroleuca 67–1.
Figure 8
Figure 8
Protein–protein interaction network of differentially regulated modification sites in C. chloroleuca 67–1.
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