Proteomic analysis of ubiquitinated proteins in rice (Oryza sativa) after treatment with pathogen-associated molecular pattern (PAMP) elicitors

Xiao Lin Chen, Xin Xie, Liye Wu, Caiyun Liu, Lirong Zeng, Xueping Zhou, Feng Luo, Guo Liang Wang, Wende Liu

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Reversible protein ubiquitination plays essential roles in regulating cellular processes. Although many reports have described the functions of ubiquitination in plant defense responses, few have focused on global changes in the ubiquitome. To better understand the regulatory roles of ubiquitination in rice pattern-triggered immunity (PTI), we investigated the ubiquitome of rice seedlings after treatment with two pathogen-associated molecular patterns, the fungal-derived chitin or the bacterial-derived flg22, using label-free quantitative proteomics. In chitin-treated samples, 144 and 167 lysine-ubiquitination sites in 121 and 162 proteins showed increased and decreased ubiquitination, respectively. In flg22-treated samples, 151 and 179 lysine-ubiquitination sites in 118 and 166 proteins showed increased and decreased ubiquitination, respectively. Bioinformatic analyses indicated diverse regulatory roles of these proteins. The ubiquitination levels of many proteins involved in the ubiquitination system, protein transportation, ligand recognition, membrane trafficking, and redox reactions were significantly changed in response to the elicitor treatments. Notably, the ubiquitination levels of many enzymes in the phenylpropanoid metabolic pathway were up-regulated, indicating that this pathway is tightly regulated by ubiquitination during rice PTI. Additionally, the ubiquitination levels of some key components in plant hormone signaling pathways were up-or down-regulated, suggesting that ubiquitination may fine-tune hormone pathways for defense responses. Our results demonstrated that ubiquitination, by targeting a wide range of proteins for degradation or stabilization, has a widespread role in modulating PTI in rice. The large pool of ubiquitination targets will serve as a valuable resource for understanding how the ubiquitination system regulates defense responses to pathogen attack.

Original languageEnglish (US)
Article number1064
JournalFrontiers in Plant Science
Volume9
DOIs
StatePublished - Jul 23 2018

Fingerprint

rice protein
proteomics
Oryza sativa
pathogens
rice
proteins
ubiquitination
elicitors
immunity
chitin
lysine
redox reactions
phenylpropanoids
protein degradation
global change

Keywords

  • Elicitors
  • Hormone signaling
  • Phenylpropanoid pathway
  • Plant defense
  • Quantitative proteomics
  • Ubiquitination

ASJC Scopus subject areas

  • Plant Science

Cite this

Proteomic analysis of ubiquitinated proteins in rice (Oryza sativa) after treatment with pathogen-associated molecular pattern (PAMP) elicitors. / Chen, Xiao Lin; Xie, Xin; Wu, Liye; Liu, Caiyun; Zeng, Lirong; Zhou, Xueping; Luo, Feng; Wang, Guo Liang; Liu, Wende.

In: Frontiers in Plant Science, Vol. 9, 1064, 23.07.2018.

Research output: Contribution to journalArticle

Chen, Xiao Lin ; Xie, Xin ; Wu, Liye ; Liu, Caiyun ; Zeng, Lirong ; Zhou, Xueping ; Luo, Feng ; Wang, Guo Liang ; Liu, Wende. / Proteomic analysis of ubiquitinated proteins in rice (Oryza sativa) after treatment with pathogen-associated molecular pattern (PAMP) elicitors. In: Frontiers in Plant Science. 2018 ; Vol. 9.
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abstract = "Reversible protein ubiquitination plays essential roles in regulating cellular processes. Although many reports have described the functions of ubiquitination in plant defense responses, few have focused on global changes in the ubiquitome. To better understand the regulatory roles of ubiquitination in rice pattern-triggered immunity (PTI), we investigated the ubiquitome of rice seedlings after treatment with two pathogen-associated molecular patterns, the fungal-derived chitin or the bacterial-derived flg22, using label-free quantitative proteomics. In chitin-treated samples, 144 and 167 lysine-ubiquitination sites in 121 and 162 proteins showed increased and decreased ubiquitination, respectively. In flg22-treated samples, 151 and 179 lysine-ubiquitination sites in 118 and 166 proteins showed increased and decreased ubiquitination, respectively. Bioinformatic analyses indicated diverse regulatory roles of these proteins. The ubiquitination levels of many proteins involved in the ubiquitination system, protein transportation, ligand recognition, membrane trafficking, and redox reactions were significantly changed in response to the elicitor treatments. Notably, the ubiquitination levels of many enzymes in the phenylpropanoid metabolic pathway were up-regulated, indicating that this pathway is tightly regulated by ubiquitination during rice PTI. Additionally, the ubiquitination levels of some key components in plant hormone signaling pathways were up-or down-regulated, suggesting that ubiquitination may fine-tune hormone pathways for defense responses. Our results demonstrated that ubiquitination, by targeting a wide range of proteins for degradation or stabilization, has a widespread role in modulating PTI in rice. The large pool of ubiquitination targets will serve as a valuable resource for understanding how the ubiquitination system regulates defense responses to pathogen attack.",
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