Insights into a key sulfite scavenger enzyme sulfite oxidase (SOX) gene in plants

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dc.contributor.authorFiliz, Ertuğrul
dc.contributor.authorVatansever, Recep
dc.contributor.authorÖzyiğit, İbrahim İlker
dc.date.accessioned2020-04-30T23:18:31Z
dc.date.available2020-04-30T23:18:31Z
dc.date.issued2017
dc.departmentDÜ, Çilimli Meslek Yüksekokulu, Bitkisel ve Hayvansal Üretim Bölümüen_US
dc.descriptionFiliz, Ertugrul/0000-0001-9636-6389; Ozyigit, Ibrahim Ilker/0000-0002-0825-5951en_US
dc.descriptionWOS: 000399687900012en_US
dc.descriptionPubMed: 28461726en_US
dc.description.abstractSulfite oxidase (SOX) is a crucial molybdenum cofactor-containing enzyme in plants that re-oxidizes the sulfite back to sulfate in sulfite assimilation pathway. However, studies of this crucial enzyme are quite limited hence this work was attempted to understand the SOXs in four plant species namely, Arabidopsis thaliana, Solanum lycopersicum, Populus trichocarpa and Brachypodium distachyon. Herein studied SOX enzyme was characterized with both oxidoreductase molybdopterin binding and Mo-co oxidoreductase dimerization domains. The alignment and motif analyses revealed the highly conserved primary structure of SOXs. The phylogeny constructed with additional species demonstrated a clear divergence of monocots, dicots and lower plants. In addition, to further understand the phylogenetic relationship and make a functional inference, a structure-based phylogeny was constructed using normalized RMSD values in five superposed models from four modelled plant SOXs herein and one previously characterized chicken SOX structure. The plant and animal SOXs showed a clear divergence and also implicated their functional divergences. Based on tree topology, monocot B. distachyon appeared to be diverged from other dicots, pointing out a possible monocot-dicot split. The expression patterns of sulfite scavengers including SOX were differentially modulated under cold, heat, salt and high light stresses. Particularly, they tend to be up-regulated under high light and heat while being down-regulated under cold and salt stresses. The presence of cis-regulatory motifs associated with different stresses in upstream regions of SOX genes was thus justified. The protein-protein interaction network of AtSOX and network enrichment with gene ontology (GO) terms showed that most predicted proteins, including sulfite reductase, ATP sulfurylases and APS reductases were among prime enzymes involved in sulfite pathway. Finally, SOX-sulfite docked structures indicated that arginine residues particularly Arg374 is crucial for SOX-sulfite binding and additional two other residues such as Arg51 and Arg103 may be important for SOX-sulfite bindings in plants.en_US
dc.identifier.doi10.1007/s12298-017-0433-zen_US
dc.identifier.endpage395en_US
dc.identifier.issn0971-5894
dc.identifier.issn0974-0430
dc.identifier.issue2en_US
dc.identifier.scopusqualityQ1en_US
dc.identifier.startpage385en_US
dc.identifier.urihttps://doi.org/10.1007/s12298-017-0433-z
dc.identifier.urihttps://hdl.handle.net/20.500.12684/3379
dc.identifier.volume23en_US
dc.identifier.wosWOS:000399687900012en_US
dc.identifier.wosqualityQ3en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakPubMeden_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherSpringeren_US
dc.relation.ispartofPhysiology And Molecular Biology Of Plantsen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectMacroelementen_US
dc.subjectSulfiteen_US
dc.subjectcis-Elementen_US
dc.subjectStressen_US
dc.subjectModelingen_US
dc.subjectPPI networken_US
dc.subjectDockingen_US
dc.titleInsights into a key sulfite scavenger enzyme sulfite oxidase (SOX) gene in plantsen_US
dc.typeArticleen_US

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