PopP2 interacts with PAD4 in an acetyltransferase activity-dependent manner and affects plant immunity. (2nd December 2021)

• Record Type: Journal Article
• Authors: Huh, Sung Un
• Is Part Of: Plant signaling & behavior. Volume 16:Number 12(2021)
• Publication Date: 2021-12-02
• Subjects: Lipase like protein -- PAD4 -- EDS1 -- ralstonia effector -- PopP2 -- acetylation; Plant ecophysiology -- Periodicals; Plant cellular signal transduction -- Periodicals; Plant cellular signal transduction; Plant ecophysiology; Periodicals; Electronic journals; 581
• DOI: 10.1080/15592324.2021.2017631
• Languages: English
• ISSNs: 1559-2316

Abstract

ABSTRACT: Plant pathogenic bacteria inject many of the effector proteins into host cell to manipulate host protein and promote pathogen development. Only a few effectors can be recognized by plant immune receptors called nucleotide‐binding domain and leucine‐rich repeat‐containing proteins (NLRs). Enhanced disease susceptibility1 (EDS1) is an important regulator of plant basal and NLR receptor-triggered immunity. EDS1/PAD4 or EDS1/SAG101 heterodimers are recruited by Toll-interleukin1-receptor domain NLRs (TNLs) to transcriptionally mobilize resistance pathways. Type III effector PopP2 contributes to Ralstonia solanacearum virulence. PopP2 has an acetyltransferase activity and is recognized by Arabidopsis NLR pair RPS4/RRS1-R. On the other hand, PopP2 avirulence function is dependent on its enzymatic activity but target proteins in the host cell are still largely unknown. In this study, we found EDS1 and PAD4 are new host targets of PopP2 effector. Arabidopsis PAD4 lipase-like domain protein physically associates with enzymatic active PopP2 protein but not inactive PopP2 C321A . PAD4-PopP2 interaction is disrupted by EDS1 immune regulator but not SAG101. We propose that acetyltransferase activity of PopP2 might confer specificity to PAD4 to manipulate plant immunity. As a counter strategy, EDS1 associates with PAD4 to form heterodimeric immune regulator complexes for activating basal resistance and interfering PopP2 physical interaction.