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Global analysis of lysine 2-hydroxyisobutyrylation during Fusarium graminearum infection in maize

Proteins post-translational modification (PTMs) is necessary in the whole life process of organisms. Among them, lysine 2-hydroxyisobutyrylation (Khib) plays an important role in protein synthesis, transcriptional regulation, and cell metabolism. Khib is a newly identified PTM in several plant speci...

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Autores principales: Zhang, Kang, Cao, Hongzhe, Ma, Yuxin, Si, Helong, Zang, Jinping, Bai, Hua, Yu, Lu, Pang, Xi, Zhou, Fan, Xing, Jihong, Dong, Jingao
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9521605/
https://www.ncbi.nlm.nih.gov/pubmed/36186065
http://dx.doi.org/10.3389/fpls.2022.1000039
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author Zhang, Kang
Cao, Hongzhe
Ma, Yuxin
Si, Helong
Zang, Jinping
Bai, Hua
Yu, Lu
Pang, Xi
Zhou, Fan
Xing, Jihong
Dong, Jingao
author_facet Zhang, Kang
Cao, Hongzhe
Ma, Yuxin
Si, Helong
Zang, Jinping
Bai, Hua
Yu, Lu
Pang, Xi
Zhou, Fan
Xing, Jihong
Dong, Jingao
author_sort Zhang, Kang
collection PubMed
description Proteins post-translational modification (PTMs) is necessary in the whole life process of organisms. Among them, lysine 2-hydroxyisobutyrylation (Khib) plays an important role in protein synthesis, transcriptional regulation, and cell metabolism. Khib is a newly identified PTM in several plant species. However, the function of Khib in maize was unclear. In this study, western blotting results showed that Khib modification level increased significantly after Fusarium graminearum infection, and 2,066 Khib modified sites on 728 proteins were identified in maize, among which 24 Khib sites occurred on core histones. Subcellular localization results showed that these Khib modified proteins were localized in cytoplasm, chloroplast, and nucleus. Then, comparative proteomic analysis of the defense response to F. graminearum infection showed that Khib modification participated in plant resistance to pathogen infection by regulating glycolysis, TCA cycle, protein synthesis, peroxisome, and secondary metabolic processes, such as benzoxazinoid biosynthesis, phenylpropanoid biosynthesis, jasmonic acid synthesis, and tyrosine and tryptophan biosynthesis. In addition, we also demonstrated that lysine 2-hydroxyisobutyrylation sites on histones were involved in the gene expression of pathogenesis-related proteins. Our results provide a new perspective for the study of plant disease resistance, and had directive significance of maize disease resistance for molecular breeding.
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spelling pubmed-95216052022-09-30 Global analysis of lysine 2-hydroxyisobutyrylation during Fusarium graminearum infection in maize Zhang, Kang Cao, Hongzhe Ma, Yuxin Si, Helong Zang, Jinping Bai, Hua Yu, Lu Pang, Xi Zhou, Fan Xing, Jihong Dong, Jingao Front Plant Sci Plant Science Proteins post-translational modification (PTMs) is necessary in the whole life process of organisms. Among them, lysine 2-hydroxyisobutyrylation (Khib) plays an important role in protein synthesis, transcriptional regulation, and cell metabolism. Khib is a newly identified PTM in several plant species. However, the function of Khib in maize was unclear. In this study, western blotting results showed that Khib modification level increased significantly after Fusarium graminearum infection, and 2,066 Khib modified sites on 728 proteins were identified in maize, among which 24 Khib sites occurred on core histones. Subcellular localization results showed that these Khib modified proteins were localized in cytoplasm, chloroplast, and nucleus. Then, comparative proteomic analysis of the defense response to F. graminearum infection showed that Khib modification participated in plant resistance to pathogen infection by regulating glycolysis, TCA cycle, protein synthesis, peroxisome, and secondary metabolic processes, such as benzoxazinoid biosynthesis, phenylpropanoid biosynthesis, jasmonic acid synthesis, and tyrosine and tryptophan biosynthesis. In addition, we also demonstrated that lysine 2-hydroxyisobutyrylation sites on histones were involved in the gene expression of pathogenesis-related proteins. Our results provide a new perspective for the study of plant disease resistance, and had directive significance of maize disease resistance for molecular breeding. Frontiers Media S.A. 2022-09-15 /pmc/articles/PMC9521605/ /pubmed/36186065 http://dx.doi.org/10.3389/fpls.2022.1000039 Text en Copyright © 2022 Zhang, Cao, Ma, Si, Zang, Bai, Yu, Pang, Zhou, Xing and Dong. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Plant Science
Zhang, Kang
Cao, Hongzhe
Ma, Yuxin
Si, Helong
Zang, Jinping
Bai, Hua
Yu, Lu
Pang, Xi
Zhou, Fan
Xing, Jihong
Dong, Jingao
Global analysis of lysine 2-hydroxyisobutyrylation during Fusarium graminearum infection in maize
title Global analysis of lysine 2-hydroxyisobutyrylation during Fusarium graminearum infection in maize
title_full Global analysis of lysine 2-hydroxyisobutyrylation during Fusarium graminearum infection in maize
title_fullStr Global analysis of lysine 2-hydroxyisobutyrylation during Fusarium graminearum infection in maize
title_full_unstemmed Global analysis of lysine 2-hydroxyisobutyrylation during Fusarium graminearum infection in maize
title_short Global analysis of lysine 2-hydroxyisobutyrylation during Fusarium graminearum infection in maize
title_sort global analysis of lysine 2-hydroxyisobutyrylation during fusarium graminearum infection in maize
topic Plant Science
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9521605/
https://www.ncbi.nlm.nih.gov/pubmed/36186065
http://dx.doi.org/10.3389/fpls.2022.1000039
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