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爱尔兰马铃薯饥荒病原菌效应蛋白PexRD54与宿主自噬相关蛋白8（ATG8）结合的结构基础

Structural Basis of Host Autophagy-related Protein 8 (ATG8) Binding by the Irish Potato Famine Pathogen Effector Protein PexRD54.

作者信息

Maqbool Abbas, Hughes Richard K, Dagdas Yasin F, Tregidgo Nicholas, Zess Erin, Belhaj Khaoula, Round Adam, Bozkurt Tolga O, Kamoun Sophien, Banfield Mark J

机构信息

From the Department of Biological Chemistry, John Innes Centre, and.

the Sainsbury Laboratory, Norwich Research Park, Norwich NR4 7UH, United Kingdom.

出版信息

J Biol Chem. 2016 Sep 16;291(38):20270-20282. doi: 10.1074/jbc.M116.744995. Epub 2016 Jul 25.

DOI:10.1074/jbc.M116.744995
PMID:27458016
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5025708/
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.

摘要

丝状植物病原体向宿主细胞输送效应蛋白以促进感染。致病疫霉的RXLR型效应蛋白PexRD54通过其ATG8家族相互作用基序（AIM）与马铃薯ATG8结合，并扰乱宿主选择性自噬。然而，这种相互作用的结构基础仍然未知。在这里，我们确定了PexRD54的晶体结构，其具有模块化结构，包括五个串联重复结构域，AIM序列位于无序的C末端。为了确定PexRD54与ATG8之间的界面，我们解析了马铃薯ATG8CL与包含效应蛋白AIM序列的肽形成的复合物的晶体结构，并使用小角X射线散射建立了全长PexRD54-ATG8CL复合物的模型。对PexRD54串联结构域进行基于结构的缺失分析表明，在体外和植物体内该结构域仍保留与ATG8CL的结合。这项研究为卵菌RXLR效应蛋白的结构/功能关系以及这些蛋白如何与宿主细胞靶点相互作用以促进疾病提供了新的见解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/508305642586/zbc0401651880009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/6f311198f35e/zbc0401651880001.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/841d944386d8/zbc0401651880005.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/19eaf52b7d29/zbc0401651880007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/c096b81e1832/zbc0401651880008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/508305642586/zbc0401651880009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/6f311198f35e/zbc0401651880001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/cdc6d20f9617/zbc0401651880002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/a467fe2a230c/zbc0401651880003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/e653b1c4963a/zbc0401651880004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/841d944386d8/zbc0401651880005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/66bcf72128fa/zbc0401651880006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/19eaf52b7d29/zbc0401651880007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/c096b81e1832/zbc0401651880008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6d7/5025708/508305642586/zbc0401651880009.jpg

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