A splicing variant of EDS1 from Vitis vinifera forms homodimers but no heterodimers with PAD4.

ABSTRACT: Enhanced Disease Susceptibility 1 (EDS1), a key component of microbe-triggered immunity and effector-triggered immunity in most higher plants, forms functional heterodimeric complexes with its homologs Phytoalexin Deficient 4 (PAD4) or Senescence-associated Gene 101 (SAG101). Here, the crystal structure of VvEDS1^Nterm , the N-terminal domain of EDS1 from Vitis vinifera, is reported, representing the first structure of an EDS1 entity beyond the model plant Arabidopsis thaliana. VvEDS1^Nterm has an α/β-hydrolase fold, is similar to the N-terminal domain of A. thaliana EDS1 and forms stable homodimers in solution as well as in crystals. These VvEDS1^Nterm homodimers are spatially incompatible with heterodimers with PAD4 or SAG101, they explain why VvEDS1^Nte

SUBMITTER: Voss M 

PROVIDER: S-EPMC10044092 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature