Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 38, Pages 20270-20282Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M116.744995
Keywords
autophagy; host-pathogen interaction; plant molecular biology; protein structure; protein-protein interaction; effector protein; plant pathogen
Categories
Funding
- European Research Council Proposal NGRB
- Biotechnology and Biological Sciences Research Council [BB/J00453, BB/M002462]
- John Innes Foundation
- Gatsby Charitable Foundation
- BBSRC [BBS/E/J/000C0624, BBS/E/J/000CA485, BB/M002462/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BBS/E/J/000CA485, BBS/E/J/000C0624, BB/M002462/1] Funding Source: researchfish
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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.
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