Comparative analyses of phytochelatin synthase (PCS) genes in higher plants

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dc.contributor.authorFiliz, Ertuğrul
dc.contributor.authorSaraçoğlu, İbrahim Adnan
dc.contributor.authorÖzyiğit, İbrahim İlker
dc.contributor.authorYalçın, Bahattin
dc.date.accessioned2020-04-30T22:41:04Z
dc.date.available2020-04-30T22:41:04Z
dc.date.issued2019
dc.departmentDÜ, Çilimli Meslek Yüksekokulu, Bitkisel ve Hayvansal Üretim Bölümüen_US
dc.descriptionOzyigit, Ibrahim Ilker/0000-0002-0825-5951en_US
dc.descriptionWOS: 000475893100001en_US
dc.description.abstractPlants employ various defence strategies to ameliorate the effects of heavy metal exposures, leading to re-establishment of metal homeostasis. One of the strategies includes the biosynthesis of main heavy metal detoxifying peptides phytochelatins (PCs) by phytochelatin synthase (PCS). In the present study, 14 PCS homologues were identified in the genomes of 10 selected plants. The size of these PCSs was 452-545 amino acid residues, with characteristic phytochelatin and phytochelatin_C domains. The N-terminal site of the proteins is highly conserved, whereas the C-terminal site is less conserved. Further, the present study also identified fully conserved Cys residues involved in heavy metal binding reported earlier. In addition, other preserved cysteines, with minor substitutions Cys(C)-> Ser(S) or Tyr(Y) or Trp(W), were also identified in the PCS sequences that might be associated with metal binding. The reported catalytic triad residues from Arabidopsis, Cys56, His162 and Asp180, are all conserved at the respective sites of PCSs. A clear monocot/dicot separation was revealed by phylogenetic analysis and was further corroborated by the exon-intron organisations of the PCS genes. Moreover, gene ontology terms, co-expression network, cis-regulatory motif and miRNA analyses indicated that the complex as well as dynamic regulation of PCSs has significant involvement in different metabolic pathways associated with signalling, defence, stress and phytohormone, in addition to metal detoxification. Moreover, variations in protein structure are suggested to confer the functional divergence in PCS proteins.en_US
dc.identifier.doi10.1080/13102818.2018.1559096en_US
dc.identifier.endpage194en_US
dc.identifier.issn1310-2818
dc.identifier.issn1314-3530
dc.identifier.issue1en_US
dc.identifier.scopusqualityQ3en_US
dc.identifier.startpage178en_US
dc.identifier.urihttps://doi.org/10.1080/13102818.2018.1559096
dc.identifier.urihttps://hdl.handle.net/20.500.12684/3116
dc.identifier.volume33en_US
dc.identifier.wosWOS:000475893100001en_US
dc.identifier.wosqualityQ4en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.language.isoenen_US
dc.publisherTaylor & Francis Ltden_US
dc.relation.ispartofBiotechnology & Biotechnological Equipmenten_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectphytochelatinen_US
dc.subjectmetal homeostasisen_US
dc.subjectheavy metalen_US
dc.subjectbioinformaticsen_US
dc.titleComparative analyses of phytochelatin synthase (PCS) genes in higher plantsen_US
dc.typeArticleen_US

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