Publication
Article Metrics
Citations
Online attention
Structural basis of host Autophagy-related protein 8 (ATG8) binding by the Irish potato famine pathogen effector protein PexRD54
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