Abstract
Steady-state SUMOylome of a plant is adjusted locally during developmental transitions and more globally during stress exposures. We recently reported that basal immunity in Arabidopsis thaliana against Pseudomonas syringae pv tomato strain DC3000 (PstDC3000) is associated with strong enhancements in the net SUMOylome. Transcriptional upregulations of SUMO conjugases, suppression of protease, and increased SUMO translations accounted for this enhanced SUMOylation. Antagonistic roles of SUMO1/2 and SUMO3 isoforms further fine-tuned the SUMOylome adjustments, thus impacting defense amplitudes and immune outcomes. Loss of function of SUPPRESSOR OF rps4-RLD1 (SRFR1), a previously reported negative regulator of basal defenses, also caused constitutive increments in global SUMO-conjugates through similar modes. These suggest that SRFR1 plays a pivotal role in maintenance of SUMOylation homeostasis and its dynamic changes during immune elicitations. Here, we demonstrate that SRFR1 degradation kinetically precedes and likely provides the salicylic acid (SA) elevations necessary for the SUMOylome increments in basal defenses. We show that SRFR1 not only is a SUMOylation substrate but also interacts in planta with both SUMO1 and SUMO3. In sum1 or sum3 mutants, SRFR1 stabilities are reduced albeit by different modes. Whereas a srfr1 sum1 combination is lethal, the srfr1 sum3 plants retain developmental defects and enhanced immunity of the srfr1 parent. Together with increasing evidence of SUMOs self-regulating biochemical efficiencies of SUMOylation-machinery, we present their impositions on SRFR1 expression that in turn counter-modulates the SUMOylome. Overall, our investigations reveal multifaceted dynamics of regulated SUMOylome changes via SRFR1 in defense-developmental balance.
Highlights
In higher eukaryotes, pivotal roles of post-translational modifications (PTMs) balance protein expressions, activities, interacting partners, localization, and proteostasis (Walsh et al, 2005; Millar et al, 2019)
HA-SUPPRESSOR OF rps4-RLD1 (SRFR1) plants were challenged with PstDC3000, and tissue extracts from progressive time points were immuno-probed with anti-HA antibodies
We first demonstrated the role of a negative immune regulator SRFR1 in maintenance of host SUMOylome homeostasis (Ingole et al, 2021a)
Summary
Pivotal roles of post-translational modifications (PTMs) balance protein expressions, activities, interacting partners, localization, and proteostasis (Walsh et al, 2005; Millar et al, 2019). SUMOylation requires the availability of processed SUMOs, with exposed diglycine (GG) residues at their C-terminus. SCE is capable of direct SUMOylation, its binding to SUMO E3 ligases, which simultaneously interact with targeted substrates, augments the process and imparts specificity (Gareau and Lima, 2010). SUMOs are self-SUMOylated at internal lysines forming poly-SUMO chains. These are catalyzed by SUMO E4 ligases that belong to the PIAL (protein inhibitor of activated stat-like) class of proteins (Tomanov et al, 2014). Some SUMO proteases remove SUMOs from SUMOylated substrates or disintegrate polySUMO chains, recycling free SUMOs (Chosed et al, 2006; Colby et al, 2006; Morrell and Sadanandom, 2019)
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