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Insights into the transcriptional and post-transcriptional regulation of the rice SUMOylation machinery and into the role of two rice SUMO proteases

2018-12-12Artigo científico Acesso aberto
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dc.contributor.authorRosa, Margarida T.G.
dc.contributor.authorAlmeida, Diego M.
dc.contributor.authorPires, Inês S.
dc.contributor.authorda Rosa Farias, Daniel
dc.contributor.authorMartins, Alice G.
dc.contributor.authorda Maia, Luciano Carlos
dc.contributor.authorde Oliveira, António Costa
dc.contributor.authorSaibo, Nelson J.M.
dc.contributor.authorOliveira, M. Margarida
dc.contributor.authorAbreu, Isabel A.
dc.contributor.institutionInstituto de Tecnologia Química e Biológica António Xavier (ITQB)
dc.contributor.institutionBioresources 4 Sustainability (GREEN-IT)
dc.contributor.pblBioMed Central (BMC)
dc.date.accessioned2019-05-03T22:15:57Z
dc.date.available2019-05-03T22:15:57Z
dc.date.issued2018-12-12
dc.description.abstractBackground: SUMOylation is an essential eukaryotic post-translation modification that, in plants, regulates numerous cellular processes, ranging from seed development to stress response. Using rice as a model crop plant, we searched for potential regulatory points that may influence the activity of the rice SUMOylation machinery genes. Results: We analyzed the presence of putative cis-acting regulatory elements (CREs) within the promoter regions of the rice SUMOylation machinery genes and found CREs related to different cellular processes, including hormone signaling. We confirmed that the transcript levels of genes involved in target-SUMOylation, containing ABA- and GA-related CREs, are responsive to treatments with these hormones. Transcriptional analysis in Nipponbare (spp. japonica) and LC-93-4 (spp. indica), showed that the transcript levels of all studied genes are maintained in the two subspecies, under normal growth. OsSUMO3 is an exceptional case since it is expressed at low levels or is not detectable at all in LC-93-4 roots and shoots, respectively. We revealed post-transcriptional regulation by alternative splicing (AS) for all genes studied, except for SUMO coding genes, OsSIZ2, OsOTS3, and OsELS2. Some AS forms have the potential to alter protein domains and catalytic centers. We also performed the molecular and phenotypic characterization of T-DNA insertion lines of some of the genes under study. Knockouts of OsFUG1 and OsELS1 showed increased SUMOylation levels and non-overlapping phenotypes. The fug1 line showed a dwarf phenotype, and significant defects in fertility, seed weight, and panicle architecture, while the els1 line showed early flowering and decreased plant height. We suggest that OsELS1 is an ortholog of AtEsd4, which was also supported by our phylogenetic analysis. Conclusions: Overall, we provide a comprehensive analysis of the rice SUMOylation machinery and discuss possible effects of the regulation of these genes at the transcriptional and post-transcriptional level. We also contribute to the characterization of two rice SUMO proteases, OsELS1 and OsFUG1.en
dc.description.versionpublishersversion
dc.description.versionpublished
dc.format.extent2567596
dc.identifier.doi10.1186/s12870-018-1547-3
dc.identifier.issn1471-2229
dc.identifier.otherPURE: 12440413
dc.identifier.otherPURE UUID: 04c3232b-a6ae-4180-8c7f-8470a819bb96
dc.identifier.otherScopus: 85058435629
dc.identifier.otherPubMed: 30541427
dc.identifier.urihttp://www.scopus.com/inward/record.url?scp=85058435629&partnerID=8YFLogxK
dc.identifier.urlhttps://www.scopus.com/pages/publications/85058435629
dc.language.isoeng
dc.peerreviewedyes
dc.subjectAlternative splicing
dc.subjectcis-elements
dc.subjectRice (Oryza sativa)
dc.subjectSUMO proteases
dc.subjectSUMOylation
dc.subjectT-DNA
dc.subjectPlant Science
dc.titleInsights into the transcriptional and post-transcriptional regulation of the rice SUMOylation machinery and into the role of two rice SUMO proteasesen
dc.typejournal article
degois.publication.issue1
degois.publication.titleBMC Plant Biology
degois.publication.volume18
dspace.entity.typePublication
rcaap.rightsopenAccess

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