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    Differential N-end rule degradation of RIN4/NOI fragments generated by the AvrRpt2 effector protease.


    Goslin, Kevin and Eschen-Lippold, Lennart and Naumann, Christin and Linster, Eric and Sorel, Maud and Klecker, Maria and de Marchi, Remi and Kind, Anne and Wirtz, Markus and Lee, Justin and Dissmeyer, Nico and Graciet, Emmanuelle (2019) Differential N-end rule degradation of RIN4/NOI fragments generated by the AvrRpt2 effector protease. Plant Physiology, 180. pp. 2272-2289. ISSN 1532-2548

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    Abstract

    In plants, the protein RPM1-INTERACTING PROTEIN4 (RIN4) is a central regulator of both pattern-triggered immunity and effector-triggered immunity. RIN4 is targeted by several effectors, including the Pseudomonas syringae protease effector AvrRpt2. Cleavage of RIN4 by AvrRpt2 generates potentially unstable RIN4 fragments, whose degradation leads to the activation of the resistance protein RESISTANT TO P. SYRINGAE2. Hence, identifying the determinants of RIN4 degradation is key to understanding RESISTANT TO P. SYRINGAE2–mediated effector-triggered immunity, as well as virulence functions of AvrRpt2. In addition to RIN4, AvrRpt2 cleaves host proteins from the nitrate-induced (NOI) domain family. Although cleavage of NOI domain proteins by AvrRpt2 may contribute to pattern-triggered immunity regulation, the (in)stability of these proteolytic fragments and the determinants regulating their stability remain unexamined. Notably, a common feature of RIN4, and of many NOI domain protein fragments generated by AvrRpt2 cleavage, is the exposure of a new N-terminal residue that is destabilizing according to the N-end rule. Using antibodies raised against endogenous RIN4, we show that the destabilization of AvrRpt2-cleaved RIN4 fragments is independent of the N-end rule pathway (recently renamed the N-degron pathway). By contrast, several NOI domain protein fragments are genuine substrates of the N-degron pathway. The discovery of this set of substrates considerably expands the number of known proteins targeted for degradation by this ubiquitin-dependent pathway in plants. These results advance our current understanding of the role of AvrRpt2 in promoting bacterial virulence.

    Item Type: Article
    Additional Information: This work was supported by the Science Foundation Ireland (grant no. 13/IA/1870 to E.G.), the Deutsche Forschungsgemeinschaft (DFG) (grant no. LE 2321/3–1 to J.L.), the ScienceCampus Halle – Plant-Based Bioeconomy and DFG (grant no. DI 1794/3–1 to N.D.), a Ph.D. fellowship from the Landesgraduiertenförderung Sachsen-Anhalt (to C.D.), the ERASMUS1 exchange program (to A.K.), and the research in the M.W. group was funded by the DFG via the Collaborative Research Centre (1036 TP 13) and the European Union by the ERA-CAPS (project KatNat). Cite as: Differential N-end Rule Degradation of RIN4/NOI Fragments Generated by the AvrRpt2 Effector Protease Kevin Goslin, Lennart Eschen-Lippold, Christin Naumann, Eric Linster, Maud Sorel, Maria Klecker, Rémi de Marchi, Anne Kind, Markus Wirtz, Justin Lee, Nico Dissmeyer, Emmanuelle Graciet Plant Physiology Aug 2019, 180 (4) 2272-2289; DOI: 10.1104/pp.19.00251
    Keywords: Differential N-end Rule Degradation; RIN4/NOI; Fragments Generated; AvrRpt2; Effector Protease;
    Academic Unit: Faculty of Science and Engineering > Biology
    Item ID: 13590
    Identification Number: https://doi.org/10.1104/pp.19.00251
    Depositing User: Emmanuelle Graciet
    Date Deposited: 19 Nov 2020 16:28
    Journal or Publication Title: Plant Physiology
    Publisher: American Society of Plant Biologists
    Refereed: Yes
    Funders: Science Foundation Ireland (SFI), Deutsche Forschungsgemeinschaft (DFG)
    URI:

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