Kinetic Analysis of Plant SUMO Conjugation Machinery

Castaño-Miquel, Laura; Lois, L. María

doi:10.1007/978-1-4939-3759-2_9

Cited by 2 publications

(1 citation statement)

References 25 publications

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“…CC-BY-NC-ND 4.0 International license made available under a (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is The copyright holder for this preprint this version posted October 5, 2020. ; https://doi.org/10.1101/2020.10.05.326249 doi: bioRxiv preprint SAE2 proteolytic processing analysis SAE2 UFDCt was cloned into cloned into pET28a (Novagene) to encode a N-terminal Histidine tag and produced as previously described 38 . 350g of freshly protein extracts from rosette and silique Col-0 plants were incubated with 10g of recombinant His:SAE2 UFDCt protein in the presence of the extraction buffer supplemented with ATP.…”

Section: Protein Extraction and Immunoblotmentioning

confidence: 99%

Evolution of molecular determinants for SUMO-activating enzyme subcellular localization in plants

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Castaño-Miquel

Carretero‐Paulet³

et al. 2020

Preprint

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Post-translational modification by Small Ubiquitin-related Modifier (SUMO) is an essential regulatory mechanism in eukaryotes. In the cell, SUMO conjugates are highly enriched in the nucleus and, consistently, SUMOylation machinery components are mainly nuclear. Nonetheless, cytosolic SUMO targets also exist and the mechanisms that facilitate SUMO conjugation in the cytosol are unknown. Here, we show that the nuclear localization of the Arabidopsis SUMO activating enzyme large subunit SAE2 is dependent on two nuclear localization signals, the canonical NLS1 and the non-canonical NLS2 identified and validated here. NLS2 is proteolytic processed from SAE2 during seed development, facilitating SAE2 enrichment in the cytosol. Results obtained using transgenic plants expressing different SAE2 proteoforms suggest that SAE2 cytosolic enrichment could constitute a rapid signal for growth arrest. Phylogenetic studies indicated that the Arabidopsis NLS1-NLS2 structural organization is conserved only in seed plants, providing a potential evolutionary role of cytosolic SUMOylation in seed appearance.

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Section: Protein Extraction and Immunoblotmentioning

confidence: 99%

Evolution of molecular determinants for SUMO-activating enzyme subcellular localization in plants

Más

Castaño-Miquel

Carretero‐Paulet³

et al. 2020

Preprint

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Proteomic analysis of SUMO1-SUMOylome changes during defense elicitation inArabidopsis

Ingole

Dahale

Bhattacharjee

2020

Preprint

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Rapid adaptation of plants to developmental or physiological cues is facilitated by specific receptors that transduce the signals mostly via post-translational modification (PTM) cascades of downstream partners. Reversible covalent attachment of SMALL UBIQUITIN-LIKE MODIFIER (SUMO), a process termed as SUMOylation, influence growth, development and adaptation of plants to various stresses. Strong regulatory mechanisms maintain the steady-state SUMOylome and mutants with SUMOylation disturbances display mis-primed immunity often with growth consequences. Identity of the SUMO-substrates undergoing SUMOylation changes during defences however remain largely unknown. Here we exploit either the auto-immune property of an Arabidopsis mutant or defense responses induced in wild-type plants against Pseudomonas syringae pv tomato (PstDC3000) to enrich and identify SUMO1-substrates. Our results demonstrate massive enhancement of SUMO1-conjugates due to increased SUMOylation efficiencies during defense responses. Of the 261 proteins we identify, 29 have been previously implicated in immune-associated processes. Role of others expand to diverse cellular roles indicating massive readjustments the SUMOylome alterations may cause during induction of immunity. Overall, our study highlights the complexities of a plant immune network and identifies multiple SUMO-substrates that may orchestrate the signalling.

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Kinetic Analysis of Plant SUMO Conjugation Machinery

Cited by 2 publications

References 25 publications

Evolution of molecular determinants for SUMO-activating enzyme subcellular localization in plants

Evolution of molecular determinants for SUMO-activating enzyme subcellular localization in plants

Proteomic analysis of SUMO1-SUMOylome changes during defense elicitation inArabidopsis

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