Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54.
Abbas MaqboolRichard K HughesYasin F DagdasNicholas TregidgoErin ZessKhaoula BelhajAdam R RoundTolga Osman BozkurtSophien KamounMark J BanfieldPublished in: The Journal of biological chemistry (2016)
Filamentous plant pathogens deliver effector proteins to host cells to promote infection. The Phytophthora infestans RXLR-type effector PexRD54 binds potato ATG8 via its ATG8 family-interacting motif (AIM) and perturbs host-selective autophagy. However, the structural basis of this interaction remains unknown. Here, we define the crystal structure of PexRD54, which includes a modular architecture, including five tandem repeat domains, with the AIM sequence presented at the disordered C terminus. To determine the interface between PexRD54 and ATG8, we solved the crystal structure of potato ATG8CL in complex with a peptide comprising the effector's AIM sequence, and we established a model of the full-length PexRD54-ATG8CL complex using small angle x-ray scattering. Structure-informed deletion of the PexRD54 tandem domains reveals retention of ATG8CL binding in vitro and in planta This study offers new insights into structure/function relationships of oomycete RXLR effectors and how these proteins engage with host cell targets to promote disease.
Keyphrases
- structural basis
- type iii
- regulatory t cells
- dendritic cells
- cell death
- high resolution
- induced apoptosis
- signaling pathway
- endoplasmic reticulum stress
- stem cells
- primary care
- cell therapy
- amino acid
- computed tomography
- mass spectrometry
- dna binding
- magnetic resonance
- gram negative
- cell cycle arrest
- pi k akt
- protein kinase
- protein protein