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The intrinsically disordered structural platform of the plant defence hub protein RPM 1‐interacting protein 4 provides insights into its mode of action in the host‐pathogen interface and evolution of the nitrate‐induced domain protein family
Author(s) -
Sun Xiaolin,
Greenwood David R.,
Templeton Matthew D.,
Libich David S.,
McGhie Tony K.,
Xue Bin,
Yoon Minsoo,
Cui Wei,
Kirk Christopher A.,
Jones William T.,
Uversky Vladimir N.,
Rikkerink Erik H. A.
Publication year - 2014
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12937
Subject(s) - effector , arabidopsis , intrinsically disordered proteins , arabidopsis thaliana , biology , protein–protein interaction , computational biology , plasma protein binding , genetics , chemistry , biochemistry , microbiology and biotechnology , biophysics , mutant , gene
Arabidopsis thaliana (At) RPM 1‐interacting protein 4 ( RIN 4), targeted by many defence‐suppressing bacterial type III effectors and monitored by several resistance proteins, regulates plant immune responses to pathogen‐associated molecular patterns and type III effectors. Little is known about the overall protein structure of At RIN 4, especially in its unbound form, and the relevance of structure to its diverse biological functions. At RIN 4 contains two nitrate‐induced ( NOI ) domains and is a member of the NOI family. Using experimental and bioinformatic approaches, we demonstrate that the unbound At RIN 4 is intrinsically disordered under physiological conditions. The intrinsically disordered polypeptide chain of At RIN 4 is interspersed with molecular recognition features (Mo RF s) and anchor ‐identified long‐binding regions, potentially allowing it to undergo disorder‐to‐order transitions upon binding to partner(s). A poly‐ l ‐proline II structure, often responsible for protein recognition, is also identified in At RIN 4. By performing bioinformatics analyses on RIN 4 homologues from different plant species and the NOI proteins from Arabidopsis , we infer the conservation of intrinsic disorder, Mo RF s and long‐binding regions of At RIN 4 in other plant species and the NOI family. Intrinsic disorder and Mo RF s could provide RIN 4 proteins with the binding promiscuity and plasticity required to act as hubs in a pivotal position within plant defence signalling cascades.