Molecular characterization of zeta class glutathione s-transferases from pinus brutia ten.

dc.authorid0000-0003-2572-8391en_US
dc.contributor.authorÖztetik, Elif
dc.contributor.authorKöçkar, Feray
dc.contributor.authorAlper, Meltem
dc.contributor.authorİşcan, Mehmet
dc.date.accessioned2019-10-17T07:16:04Z
dc.date.available2019-10-17T07:16:04Z
dc.date.issued2015en_US
dc.departmentFakülteler, Fen-Edebiyat Fakültesi, Biyoloji Bölümüen_US
dc.descriptionKöçkar, Feray (Balikesir Author)en_US
dc.description.abstractGlutathione transferases (GSTs; EC 2.5.1.18) play important roles in stress tolerance and metabolic detoxification in plants. In higher plants, studies on GSTs have focussed largely on agricultural plants. There is restricted information about molecular characterization of GSTs in gymnosperms. To date, only tau class GST enzymes have been characterized from some pinus species. For the first time, the present study reports cloning and molecular characterization of two zeta class GST genes, namely PbGSTZ1 and PbGSTZ2 from Pinus brutia Ten., which is an economically important pine native to the eastern Mediterranean region and have to cope with several environmental stress conditions. The PbGSTZ1 gene was isolated from cDNA, whereas PbGSTZ2 was isolated from genomic DNA. Sequence analysis of PbGSTZ1 and PbGSTZ2 revealed the presence of an open reading frame of 226 amino acids with typical consensus sequences of the zeta class plant GSTs. Protein and secondary structure prediction analysis of two zeta class PbGSTZs have shared common features of other plant zeta class GSTs. Genomic clone, PbGSTZ2 gene, is unexpectedly intronless. Extensive sequence analysis of PbGSTZ2, with cDNA clone, PbGSTZ1, revealed 87% identity at nucleotide and 81% identity at amino acid levels with 41 amino acids differences suggesting that genomic PbGSTZ2 gene might be an allelic or a paralogue version of PbGSTZ1.en_US
dc.description.sponsorshipTubitak University of Anadolu Reseach Projecten_US
dc.identifier.doi10.1007/s12041-015-0538-5
dc.identifier.endpage423en_US
dc.identifier.issn0022-1333
dc.identifier.issn0973-7731
dc.identifier.issue3en_US
dc.identifier.scopus2-s2.0-84945469305
dc.identifier.scopusqualityQ3
dc.identifier.startpage417en_US
dc.identifier.urihttps://doi.org/10.1007/s12041-015-0538-5
dc.identifier.urihttps://hdl.handle.net/20.500.12462/7575
dc.identifier.volume94en_US
dc.identifier.wosWOS:000363980200006
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.language.isoenen_US
dc.publisherIndian Acad Sciencesen_US
dc.relation.ispartofJournal of Geneticsen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/embargoedAccessen_US
dc.subjectIsozymesen_US
dc.subjectGlutathione Transferasesen_US
dc.subjectGymnospermsen_US
dc.subjectGlutathione Transferases Zetaen_US
dc.titleMolecular characterization of zeta class glutathione s-transferases from pinus brutia ten.en_US
dc.typeArticleen_US

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