Structural basis of host autophagy-related protein 8 (ATG8) binding by the Irish Potato Famine pathogen effector protein PexRD54

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Maqbool, Abbas, Hughes, Richard K., Dagdas, Yasin F., Tregidgo, Nicholas, Zess, Erin, Belhaj, Khaoula, Round, Adam, Bozkurt, Tolga O., Kamoun, Sophien ORCID: https://orcid.org/0000-0002-0290-0315 and Banfield, Mark J. (2016) Structural basis of host autophagy-related protein 8 (ATG8) binding by the Irish Potato Famine pathogen effector protein PexRD54. Journal of Biological Chemistry, 291 (38). pp. 20270-20282. ISSN 0021-9258

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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 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.

Item Type: Article
Additional Information: Author's Choice—Final version free via Creative Commons CC-BY license.
Uncontrolled Keywords: autophagy,host-pathogen interaction,plant molecular biology,protein structure,protein-protein interaction,effector protein,plant pathogen
Faculty \ School: Faculty of Science > The Sainsbury Laboratory
Faculty of Science > School of Biological Sciences
UEA Research Groups: Faculty of Science > Research Groups > Plant Sciences
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Depositing User: Pure Connector
Date Deposited: 12 Oct 2016 14:00
Last Modified: 03 Jul 2023 11:30
URI: https://ueaeprints.uea.ac.uk/id/eprint/60874
DOI: 10.1074/jbc.M116.744995

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