Do proteolytic cascades exist in plants?

Paulus, Judith K; Hoorn, Renier A. L. van der

doi:10.1093/jxb/erz016

Cited by 16 publications

(18 citation statements)

References 47 publications

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“…These proteolytic cascades offer irreversible, fast, nontranscriptional regulatory pathways that can quickly propagate and amplify a signal. Although proteases are equally numerous in plants, proteolytic cascades have not yet been reported in this kingdom, but there are several indications that they probably occur (38). Our results demonstrate that immune protease Rcr3 is released from its inactive proRcr3 precursor by P69B and other SBTs, describing a robust extracellular proteolytic cascade acting in plant immunity in solanaceous plants.…”

Section: Discussionmentioning

confidence: 67%

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Extracellular proteolytic cascade in tomato activates immune protease Rcr3

Paulus

Kourelis

Ramasubramanian

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

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Proteolytic cascades regulate immunity and development in animals, but these cascades in plants have not yet been reported. Here we report that the extracellular immune protease Rcr3 of tomato is activated by P69B and other subtilases (SBTs), revealing a proteolytic cascade regulating extracellular immunity in solanaceous plants. Rcr3 is a secreted papain-like Cys protease (PLCP) of tomato that acts both in basal resistance against late blight disease (Phytophthora infestans) and in gene-for-gene resistance against the fungal pathogen Cladosporium fulvum (syn. Passalora fulva). Despite the prevalent model that Rcr3-like proteases can activate themselves at low pH, we found that catalytically inactive proRcr3 mutant precursors are still processed into mature mRcr3 isoforms. ProRcr3 is processed by secreted P69B and other Asp-selective SBTs in solanaceous plants, providing robust immunity through SBT redundancy. The apoplastic effector EPI1 of P. infestans can block Rcr3 activation by inhibiting SBTs, suggesting that this effector promotes virulence indirectly by preventing the activation of Rcr3(-like) immune proteases. Rcr3 activation in Nicotiana benthamiana requires a SBT from a different subfamily, indicating that extracellular proteolytic cascades have evolved convergently in solanaceous plants or are very ancient in the plant kingdom. The frequent incidence of Asp residues in the cleavage region of Rcr3-like proteases in solanaceous plants indicates that activation of immune proteases by SBTs is a general mechanism, illuminating a proteolytic cascade that provides robust apoplastic immunity.

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Section: Discussionmentioning

confidence: 67%

“…Proteolytic cascades involve different proteases that consecutively activate one another (38). Several proteolytic cascades have been described for metazoans (39).…”

Section: Discussionmentioning

confidence: 99%

Extracellular proteolytic cascade in tomato activates immune protease Rcr3

Paulus

Kourelis

Ramasubramanian

et al. 2020

Proc. Natl. Acad. Sci. U.S.A.

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“…The Arabidopsis genome codes for over 800 proteases with distinct temporal and tissue expression profiles (van der Hoorn, 2008;Tsiatsiani et al, 2012) but our knowledge on plant proteolytic cascades is still fragmentary (Paulus and Van der Hoorn, 2019). Understanding the regulation of the gluconeogenic pathway during seed germination is of critical importance, as seedling establishment has a direct impact on plant fitness and productivity (Graham, 2008).…”

Section: Discussionmentioning

confidence: 99%

Proteolytic cleavage ofArabidopsis thalianaphosphoenolpyruvate carboxykinase-1 modifies its allosteric regulation

Rojas

Hartman

Figueroa

et al. 2020

Preprint

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Phosphoenolpyruvate carboxykinase (PEPCK) plays a crucial role in gluconeogenesis. In this work, we analyze the proteolysis of Arabidopsis thaliana PEPCK1 (AthPEPCK1) in germinating seedlings. We found that expression of AthPEPCK1 peaks at 24-48 hours post-imbibition. Concomitantly, we observed shorter versions of AthPEPCK1, putatively generated by metacaspase-9 (AthMC9). To study the impact of AthMC9 cleavage on the kinetic and regulatory properties of AthPEPCK1, we produced truncated mutants based on the reported AthMC9 cleavage sites. The Δ19 and Δ101 truncated mutants of AthPEPCK1 showed similar kinetic parameters and the same quaternary structure than the WT. However, activation by malate and inhibition by glucose 6-phosphate were abolished in the Δ101 mutant. We propose that proteolysis of AthPEPCK1 in germinating seedlings operates as a mechanism to adapt the sensitivity to allosteric regulation during the sink-to-source transition.HighlightThis paper describes the effects of the N-terminal proteolytic cleavage on the kinetic and regulatory properties of Arabidopsis thaliana phosphoenolpyruvate carboxykinase-1.

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“…Plants contain hundreds of proteases with mostly unknown substrates and function (van der Hoorn, 2008; Demir et al , 2018; Paulus and van der Hoorn, 2019). In a pioneering study, COFRADIC was used for complementary in vitro and in vivo approaches to identify physiological substrates of Arabidopsis metacaspase 9 (MC9) (Tsiatsiani et al , 2013).…”

Section: N-terminomics For Unbiased Identification Of Plant Protease mentioning

confidence: 99%