AHL13 is a chromatin-associated DNA-binding protein involved in plant immune responses. Key characteristics include:
Domains: Contains two AT-hook motifs for DNA binding and a plant-prokaryote conserved (PPC) domain for nuclear localization and protein-protein interactions .
Function: Regulates jasmonic acid (JA) biosynthesis, defense gene expression, and resistance to pathogens like Pseudomonas syringae and Botrytis cinerea .
Phosphorylation: Targeted by MAPKs (MPK3, MPK4, MPK6), with phosphorylation at residues S109 and S376 stabilizing the protein and enhancing its immune regulatory functions .
While the provided sources do not explicitly describe commercial AHL13 antibodies, studies infer their use through methodologies such as:
Immunoblotting: Detecting AHL13-GFP fusion proteins in transgenic Arabidopsis lines (e.g., ahl13-1 Pro35S::AHL13-GFP) .
Phosphoproteomics: Identifying MAPK-dependent phosphorylation sites on AHL13 .
Mutant Analysis: Validating AHL13 knockout (ahl13-1) and overexpression phenotypes .
Pathogen Resistance:
Transcriptional Regulation: AHL13 modulates promoters of JA-related genes (AOC1, LOX2, LOX4) and MYB transcription factors linked to ROS homeostasis .
MAPK Substrate: Phosphorylation by MPK3/4/6 stabilizes AHL13, preventing proteasomal degradation .
Structural Impact: Phosphorylation at S109/S376 alters surface charge, potentially enhancing DNA binding or protein interactions .
Mutant Lines:
Transcriptome Data: RNA-seq revealed AHL13’s role in suppressing JA biosynthesis under non-stress conditions, balancing growth and defense .
AHL13 bridges MAPK signaling to chromatin-level immune regulation. Its phosphorylation status determines: