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Structural basis of host Autophagy-related protein 8 (ATG8) binding by the Irish potato famine pathogen effector protein PexRD54

DOI: 10.1074/jbc.M116.744995 DOI Help

Authors: Abbas Maqbool (John Innes Centre) , Richard Hughes (John Innes Centre) , Yasin F Dagdas (The Sainsbury Laboratory) , Nicholas Tregidgo (John Innes Centre) , Erin Zess (The Sainsbury Laboratory) , Khaoula Belhaj (The Sainsbury Laboratory) , Adam Round (EMBL Grenoble, Keele University) , Tolga O Bozkurt (Imperial College) , Sophien Kamoun (The Sainsbury Laboratory) , Mark Banfield (John Innes Centre)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Biological Chemistry

State: Published (Approved)
Published: July 2016
Diamond Proposal Number(s): 7641

Abstract: 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 comprises 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 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.

Journal Keywords: effector protein ; plant pathogen ; plant molecular biology; host - pathogen interaction ; protein structure ; protein - protein interaction; autophagy

Subject Areas: Biology and Bio-materials


Instruments: B21-High Throughput SAXS , I02-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength)

Other Facilities: ESRF beamline BM29

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