Abstract:SIZ1 is a small ubiquitin‐related modifier (SUMO) E3 ligase that mediates post‐translational SUMO modification of target proteins and thereby regulates developmental processes and hormonal and environmental stress responses in Arabidopsis. However, the role of SUMO E3 ligases in crop plants is largely unknown. Here, we identified and characterized two Glycine max (soybean) SUMO E3 ligases, GmSIZ1a and GmSIZ1b. Expression of GmSIZ1a and GmSIZ1b was induced in response to salicylic acid (SA), heat, and dehydrati… Show more
“…Small ubiquitin‐related modifier conjugation was lower in siz1 mutants than in wild‐type Arabidopsis plants, even under heat stress . Conversely, heat‐induced sumoylation of target proteins was observed in several previous studies . In addition, rice E3 SUMO ligases OsSIZ1 and OsSIZ2 were involved in sumoylation of target proteins under heat stress , and transgenic Arabidopsis overexpressing tomato E3 SUMO ligase SISIZ1 also accumulated SUMO conjugates in response to heat stress .…”
Section: Discussionmentioning
confidence: 61%
“…Numerous proteins are conjugated to SUMO in response to heat stress, suggesting that sumoylation contributes to heat tolerance . Here, AtSIZ1 was polyubiquitinated rather than sumoylated under heat stress conditions (Fig.…”
Section: Resultsmentioning
confidence: 79%
“…Previous research showed that numerous proteins were modified by SUMO under conditions of heat stress . However, it is unclear whether E3 SUMO ligase is itself regulated by sumoylation or other protein modifications in response to stresses such as heat.…”
Section: Resultsmentioning
confidence: 99%
“…Cold, heat, and drought stresses stimulate the conjugation of SUMO to a range of target proteins . This suggested that the stability and activity of E3 SUMO ligase might also be post‐translationally modulated by stress.…”
Sumoylation regulates numerous cellular functions in plants as well as in other eukaryotic systems. However, the regulatory mechanisms controlling E3 small ubiquitin‐related modifier (SUMO) ligase are not well understood. Here, post‐translational modification of the Arabidopsis E3 SUMO ligase AtSIZ1 was shown to be specifically controlled by abiotic stresses. AtSIZ1 ubiquitination was induced by exposure to heat stress in transgenic plants overexpressing the E3 ubiquitin ligase COP1. In addition, AtSIZ1 ubiquitination was strongly enhanced in transgenic plants overexpressing SUMO isopeptidase ESD4 under heat stress. By contrast, drought stress induced sumoylation rather than ubiquitination of AtSIZ1 and sumoylated forms of AtSIZ1 accumulated in esd4 and cop1–4 mutants. Moreover, siz1 mutants were found to be tolerant to heat and drought stresses. Taken together, these results indicate that ubiquitination and sumoylation of AtSIZ1 in response to abiotic stresses depend on the activities of COP1 and ESD4 and that the activity and stability of AtSIZ1 can be specifically controlled by different abiotic stresses.
“…Small ubiquitin‐related modifier conjugation was lower in siz1 mutants than in wild‐type Arabidopsis plants, even under heat stress . Conversely, heat‐induced sumoylation of target proteins was observed in several previous studies . In addition, rice E3 SUMO ligases OsSIZ1 and OsSIZ2 were involved in sumoylation of target proteins under heat stress , and transgenic Arabidopsis overexpressing tomato E3 SUMO ligase SISIZ1 also accumulated SUMO conjugates in response to heat stress .…”
Section: Discussionmentioning
confidence: 61%
“…Numerous proteins are conjugated to SUMO in response to heat stress, suggesting that sumoylation contributes to heat tolerance . Here, AtSIZ1 was polyubiquitinated rather than sumoylated under heat stress conditions (Fig.…”
Section: Resultsmentioning
confidence: 79%
“…Previous research showed that numerous proteins were modified by SUMO under conditions of heat stress . However, it is unclear whether E3 SUMO ligase is itself regulated by sumoylation or other protein modifications in response to stresses such as heat.…”
Section: Resultsmentioning
confidence: 99%
“…Cold, heat, and drought stresses stimulate the conjugation of SUMO to a range of target proteins . This suggested that the stability and activity of E3 SUMO ligase might also be post‐translationally modulated by stress.…”
Sumoylation regulates numerous cellular functions in plants as well as in other eukaryotic systems. However, the regulatory mechanisms controlling E3 small ubiquitin‐related modifier (SUMO) ligase are not well understood. Here, post‐translational modification of the Arabidopsis E3 SUMO ligase AtSIZ1 was shown to be specifically controlled by abiotic stresses. AtSIZ1 ubiquitination was induced by exposure to heat stress in transgenic plants overexpressing the E3 ubiquitin ligase COP1. In addition, AtSIZ1 ubiquitination was strongly enhanced in transgenic plants overexpressing SUMO isopeptidase ESD4 under heat stress. By contrast, drought stress induced sumoylation rather than ubiquitination of AtSIZ1 and sumoylated forms of AtSIZ1 accumulated in esd4 and cop1–4 mutants. Moreover, siz1 mutants were found to be tolerant to heat and drought stresses. Taken together, these results indicate that ubiquitination and sumoylation of AtSIZ1 in response to abiotic stresses depend on the activities of COP1 and ESD4 and that the activity and stability of AtSIZ1 can be specifically controlled by different abiotic stresses.
“…Studies in A. thaliana have shown that the SUMOylation pathway is mainly mediated by the SUMO E3 ligase SIZ1. Currently, SIZ1 genes have been isolated from plants such as rice (PARK et al 2010), Dendrobium nobile (Liu et al 2015), apple (Zhang et al 2016), soybean (Cai et al 2017) and tomato (Zhang et al 2017), but no study on cloning the gene SIZ1 and its interaction with ICE1 in forest trees. The coding sequence of EcaSIZ1 , which was isolated in this study, is similar to the cloned SIZ1 protein in the above plants, and also has similar protein secondary domains such as MIZ1/SP zinc finger domain, SAP domain, PINIT domain, SXS domain and PHD domain.…”
SUMOylation in plants is associated with biotic and abiotic stress responses, flowering and other aspects of development, and ICE1 protein SUMOylation by SUMO E3 ligase SIZ1 plays important roles in plant cold tolerance. Here, we reported the subcellular localization of EcaICE1 and its interaction with EcaSIZ1 in Eucalyptus camaldulensis. The genes EcaICE1 and EcaSIZ1 were isolated by homologous cloning. The subcellular localization analysis showed that EcaICE1 was located in nucleus. Bimolecular fluorescence complementation (BiFC) analysis revealed that EcaICE1 could interact with EcaSIZ1 in the nucleus of Nicotiana benthamiana leaves. Moreover, yeast two-hybrid assay confirmed that the amino acid region from position 84 to 126 in EcaICE1 was critical for the strong transactivation activity of EcaICE1 and that the C terminal region from position 361 to 557 in EcaICE1 was the key region for its interaction with EcaSIZ1 by using different truncated lengths of non-transactivation activity of EcaICE1 as the bait protein. Collectively, our results showed that EcaICE1 may have a SUMOylation pathway similar to Arabidopsis thaliana.
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