Abstract
Due to their sessile nature, plants are constantly subjected to various environmental stresses such as drought, salinity, and pathogen infections. Post-translational modifications (PTMs), like SUMOylation, play a vital role in the regulation of plant responses to their environment. The process of SUMOylation typically involves an enzymatic cascade containing the activation, (E1), conjugation (E2), and ligation (E3) of SUMO to a target protein. Additionally, it also requires a class of SUMO proteases that generate mature SUMO from its precursor and cleave it off the target protein, a process termed deSUMOylation. It is now clear that SUMOylation in plants is key to a plethora of adaptive responses. How this is achieved with an extremely limited set of machinery components is still unclear. One possibility is that novel SUMO components are yet to be discovered. However, current knowledge indicates that only a small set of enzymes seem to be responsible for the modification of a large number of SUMO substrates. It is yet unknown where the specificity lies within the SUMO system. Although this seems to be a crucial question in the field of SUMOylation studies, not much is known about the factors that provide specificity. In this review, we highlight the role of the localisation of SUMO components as an important factor that can play a vital role in contributing to the specificity within the process. This will introduce a new facet to our understanding of the mechanisms underlying such a dynamic process.
Highlights
Post-translational modifications of proteins play a crucial role in many cellular processes through their unique ability to alter rapidly and reversibly the function, stability, and locations of pre-existing proteins
Ubiquitin is generally regarded as targeting a protein for degradation, SUMOylation can rapidly change the overall fate of target proteins by altering their stability or interaction with partner proteins or DNA
In the final step, activated SUMO is transferred to an active site cysteine of E2, a conjugation enzyme, forming a SUMO-E2 thioester intermediate that promotes the transfer of SUMO to a lysine residue in the target protein, mediated directly or indirectly by an E3 ligase [28,39]
Summary
Post-translational modifications of proteins play a crucial role in many cellular processes through their unique ability to alter rapidly and reversibly the function, stability, and locations of pre-existing proteins. Protein modifications include chemical modifications such as acetylation and phosphorylation and the conjugation of proteins to target substrates like ubiquitination and SUMOylation. Both ubiquitination and SUMOylation involve the covalent attachment of ubiquitin and SUMO Four SUMO proteins have been identified in animals: cerevisiae [15]. SUMO2 and 3 from human and animals share 87–95% protein sequence identity and 4. This is followed by forming a thioester bond, consuming ATP in the process [28,29,30] This is followed by SUMObeing being transferred anotherunique uniqueE2-conjugating. The charged-E2 (E2~ SUMO thioester) can either transfer SUMO directly directly to one or more lysines in the target substrate by mono-, multi-, and poly-SUMOylation [31–.
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