A comprehensive dynamic immune acetylproteomics profiling induced by Puccinia polysora in maize

Area of Science:

• Plant Biology
• Molecular Biology
• Biochemistry

Background:

• Lysine-ε-acetylation (Kac) is a critical post-translational modification in plant-pathogen interactions.
• Pathogens can manipulate host acetylation through effectors, but the functional roles of these modified host proteins in defense are largely unknown.

Purpose of the Study:

• To investigate dynamic changes in protein abundance and lysine acetylation in maize during infection by Puccinia polysora.
• To identify host proteins and pathways regulated by acetylation during fungal invasion.

Main Methods:

• High-resolution tandem mass spectrometry was used to analyze protein acetylation and abundance in maize at multiple time points post-infection.
• Bioinformatic analysis was performed to identify Kac sites, motifs, and enriched pathways.

Main Results:

• A total of 7412 Kac sites across 4697 proteins were identified, with 1732 sites quantified.
• Lysine acetylation was found to be ubiquitous, targeting specific motifs and enriching proteins in metabolism and defense pathways.
• Acetylation patterns of defense-related proteins varied across signaling, defense response, cell wall fortification, ROS scavenging, redox, and proteostasis pathways.

Conclusions:

• Maize dynamically regulates cellular processes via altered acetylation of histones and non-histones in response to P. polysora infection.
• This study provides a comprehensive resource for understanding the dynamic roles of lysine acetylation in plant immune responses and host-pathogen interactions.