Barley molybdenum cofactor sulfurase (MCSU): sequencing, modeling, and its comparison to other higher plants

dc.contributor.authorFiliz, Ertuğrul
dc.contributor.authorDistelfeld, Assaf
dc.contributor.authorFahima, Tzion
dc.contributor.authorMetin, Özge Karakaş
dc.contributor.authorNevo, Eviatar
dc.contributor.authorSong, Weining
dc.contributor.authorUncuoğlu, Ahu Altınkut
dc.date.accessioned2020-04-30T22:40:03Z
dc.date.available2020-04-30T22:40:03Z
dc.date.issued2015
dc.departmentDÜ, Çilimli Meslek Yüksekokulu, Bitkisel ve Hayvansal Üretim Bölümüen_US
dc.descriptionFiliz, Ertugrul/0000-0001-9636-6389; Distelfeld, Assaf/0000-0003-1777-3053; Fahima, Tzion/0000-0001-5555-0040en_US
dc.descriptionWOS: 000360286300015en_US
dc.description.abstractMolybdenum cofactor sulfurases (MCSUs) are important enzymes for plant development and response to environmental queues, including processes such as nitrogen metabolism and regulation of the abscisic acid levels in plant tissues. We cloned and sequenced MCSU gene from barley and performed in silico comparison with rice, tomato, and Arabidopsis. Physico-chemical properties and subcellular predictions were found to be similar in different plant species. All MCSUs had three critical domains: aminotransferase class-V (Pfam: PF00266), MOSC N-terminal beta barrel (Pfam: PF03476), and MOSC (Pfam: PF03473). Secondary structure analysis revealed that random coils were the most abundant, followed by alpha-helices and extended strands. Predicted binding sites of MCSUs were different in barley and Arabidopsis, whereas rice and tomato showed the same pattern. A conserved triple-cysteine motif was detected in all MCSUs with cys438-cys440-cys445, cys431-cys433-cys438, cys428-cys430-cys435, and cys425-cys427-cys432 in barley, rice, Arabidopsis, and tomato, respectively. Furthermore, a 3D structure analysis indicated that structural divergences were present in all MCSUs, even in the core domain structure. Phylogenetic analysis of MCSUs revealed that monocot-dicot divergence was clearly observed with high bootstrap values. The results of this study will contribute to the understanding of MCSU genes and proteins in plants. The data of this study will also constitute a scientific basis for wet-lab and in silico studies of MCSUs.en_US
dc.identifier.doi10.3906/tar-1411-68en_US
dc.identifier.endpage796en_US
dc.identifier.issn1300-011X
dc.identifier.issn1303-6173
dc.identifier.issue5en_US
dc.identifier.scopusqualityQ2en_US
dc.identifier.startpage786en_US
dc.identifier.urihttps://doi.org/10.3906/tar-1411-68
dc.identifier.urihttps://hdl.handle.net/20.500.12684/2893
dc.identifier.volume39en_US
dc.identifier.wosWOS:000360286300015en_US
dc.identifier.wosqualityQ2en_US
dc.indekslendigikaynakWeb of Scienceen_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakTR-Dizinen_US
dc.language.isoenen_US
dc.publisherTubitak Scientific & Technical Research Council Turkeyen_US
dc.relation.ispartofTurkish Journal Of Agriculture And Forestryen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectBarleyen_US
dc.subjectin silico analysisen_US
dc.subjectmolybdenum cofactor sulfuraseen_US
dc.subjectsequencingen_US
dc.subject3D structureen_US
dc.subjectplant proteinen_US
dc.titleBarley molybdenum cofactor sulfurase (MCSU): sequencing, modeling, and its comparison to other higher plantsen_US
dc.typeArticleen_US

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