This review uncovers lysine acetylation's role in plant immunity, highlighting mechanisms involving non-histone proteins and acetyltransferases.
Plant immunity is regulated by numerous transcriptional and posttranslational mechanisms. Among these, lysine acetylation, which is controlled by lysine acetyltransferases (KATs) and lysine deacetylases (KDACs), has been extensively studied, particularly in the context of epigenetic regulation through histone acetylation. However, advances in proteomics have revealed that non‐histone proteins also undergo lysine acetylation, prompting increasing efforts to elucidate the underlying mechanisms and functions of this posttranslational modifications. This review provides a comprehensive analysis of acetyl‐lysine proteome (acetylome) studies during plant interaction with pathogens (including fungi, bacteria and viruses). By highlighting the significance of lysine acetylation in non‐histone proteins, these studies offer valuable insights into potential new targets for lysine acetylation in plant immunity. We further examine the roles of plant KATs and KDACs, as well as pathogen‐derived KATs, emphasizing the different types of lysine acetylation in non‐histone proteins. In particular, we explore how bacterial effectors, which mimic KAT activity, acetylate lysine residues in non‐histone proteins to modulate plant immunity. Additionally, we discuss on emerging molecular mechanisms involving plant KATs and KDACs that finely regulate immune responses, particularly within the jasmonic acid signalling pathway. These findings open new perspectives for future research on this posttranslational regulation within the context of plant immunity.
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Villette et al. (2025) studied this question.
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