Rxivist logo

Rxivist combines preprints from bioRxiv with data from Twitter to help you find the papers being discussed in your field. Currently indexing 67,118 bioRxiv papers from 295,271 authors.

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

By Kevin Goslin, Lennart Eschen-Lippold, Christin Naumann, Eric Linster, Maud Sorel, Maria Klecker, RĂ©mi de Marchi, Anne Kind, Markus Wirtz, Justin Lee, Nico Dissmeyer, Emmanuelle Graciet

Posted 20 Mar 2019
bioRxiv DOI: 10.1101/583054 (published DOI: 10.1104/pp.19.00251)

The protein RPM1-INTERACTING PROTEIN4 (RIN4) is a central regulator of both layers of plant immunity systems, the so-called pattern-triggered immunity (PTI) and effector-triggered immunity (ETI). RIN4 is targeted by several effectors, including the Pseudomonas syringae protease effector AvrRpt2. Cleavage of RIN4 by AvrRpt2 generates unstable RIN4 fragments, whose degradation leads to the activation of the resistance protein RPS2 (RESISTANT TO P. SYRINGAE2). Hence, identifying the determinants of RIN4 degradation is key to understanding RPS2-mediated ETI, 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 PTI regulation, the (in)stability of these proteolytic fragments and the determinants that regulate their stability have not been examined. 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 N-degron pathway). By contrast, several NOI-domain protein fragments are bona fide substrates of the N-degron pathway. The discovery of this novel set of substrates considerably expands the number of proteins targeted for degradation by this ubiquitin-dependent pathway, for which very few physiological substrates are known in plants. Our results also open new avenues of research to understand the role of AvrRpt2 in promoting bacterial virulence.

Download data

  • Downloaded 234 times
  • Download rankings, all-time:
    • Site-wide: 43,690 out of 67,121
    • In plant biology: 1,261 out of 1,947
  • Year to date:
    • Site-wide: 20,695 out of 67,121
  • Since beginning of last month:
    • Site-wide: 37,055 out of 67,121

Altmetric data


Downloads over time

Distribution of downloads per paper, site-wide


Sign up for the Rxivist weekly newsletter! (Click here for more details.)


News