Dataset Information

Proteomic analyses of lysine 2-hydroxyisobutyrylation in Fusarium graminearum in response to tebuconazole and carbendazim

ABSTRACT: Lysine 2-hydroxyisobutyrylation (Khib) is a newly discovered post-translational modification in some prokaryotic and eukaryotic organisms. Here, we carried out proteome-wide analysis of Khib in Fusarium graminearum, identifying the reshaping of lysine 2-hydroxyisobutyrylome by tebuconazole or carbendazim, using the most recently-developed high-resolution LC-MS/MS in combination with high-specific affinity enrichment. In total, 3035 quantifiable Khib sites on 937 proteins were identified. With the criteria of fold changes over 1.3, normalized with total proteins, 1083 Khib sites of 509 proteins were considered as significantly affected by tebuconazole treatment, while 344 Khib sites of 227 proteins were significantly affacted by carbendazim. Furthermore, bioinformatics analysis were conducted.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Gibberella Zeae (strain Ph-1 / Atcc Mya-4620 / Fgsc 9075 / Nrrl 31084) (wheat Head Blight Fungus) (fusarium Graminearum)

SUBMITTER: Yanxiang Zhao

LAB HEAD: Jinguang Huang

PROVIDER: PXD022499 | Pride | 2022-04-04

REPOSITORIES: Pride

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Publications

Quantitative multiplexed proteomics analysis reveals reshaping of the lysine 2-hydroxyisobutyrylome in Fusarium graminearum by tebuconazole.

Zhao Yanxiang Y Zhang Limin L Ju Chao C Zhang Xiaoyan X Huang Jinguang J

BMC genomics 20220218 1

<h4>Backgrounds</h4>Lysine 2-hydroxyisobutyrylation (Khib) is a newly discovered posttranslational modification (PTM) and has been identified in several prokaryotic and eukaryotic organisms. Fusarium graminearum, a major pathogen of Fusarium head blight (FHB) in cereal crops, can cause considerable yield loss and produce various mycotoxins that threaten human health. The application of chemical fungicides such as tebuconazole (TEC) remains the major method to control this pathogen. However, the ...[more]

PMID: 35180840

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Project description:N-glycosylation is an important posttranslational modification in all eukaryotes, but little is known about the N-glycoproteomes in microalgal systems. Here, N-glycoproteome of the model diatom Phaeodactylum tricornutum was unveiled. Totally, 893 different N-glycosylated sites from 649 proteins were identified from P. tricornutum. The new synthesized N-glycans were principally transferred to asparagine residues within the conserved N-X-S/T (where X is a residue other than proline) sequence of nascent polypeptide chains. Functional annotation of N-glycosylated proteins showed that 70% N-glycoproteins were involved in vesicular transport and posttranslational modification, protein turnover, chaperones, indicating the N-glycosylation was important for these functions. Of the all identified N-glycoproteins 45.3% were predicted to localize on chloroplast, which implied the widespread regulatory role of N-glycosylation in chloroplast. Furthermore, the enrichment results of N-glycoproteins indicated that compared to ‘Cellular component’ and ‘Biological process’ categories proteins related with the ‘Molecular function’ category were more prone to be N-glycosylated. And it was speculated that N-glycosylation played a vital regulatory role in catalytic activity of enzymes and metabolism processes of many small molecules. 47% of all enriched proteins were related with metabolic pathways. The functional annotation and enrichment of N-glycoproteins suggested that N-glycoproteins participated in a variety of important metabolic pathways and perform different functions in P. tricornutum. 12 proteins involved in the ER quality control mechanism and ER- associated degradation pathway were identified as N-glycosylated proteins, indicating that the N-glycosylated modification was important for their functions in the protein N-glycosylation pathway. Additionally, some interacted glycoproteins were classified from this study, which provided valuable information for studying the functions of these glycoproteins. In the study, the identification of N-glycosylation on nascent proteins expands our understanding of this PTM at a proteomics scale and may facilitate the elucidation of the precise function of proteins in this model diatom.

Dataset Information

Proteomic analyses of lysine 2-hydroxyisobutyrylation in Fusarium graminearum in response to tebuconazole and carbendazim

Publications

Quantitative multiplexed proteomics analysis reveals reshaping of the lysine 2-hydroxyisobutyrylome in Fusarium graminearum by tebuconazole.

Similar Datasets

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