dc.contributor.authorNikolaev, Yaroslav
dc.contributor.authorPervushin, Konstantin
dc.date.accessioned2013-06-24T08:42:52Z
dc.date.available2013-06-24T08:42:52Z
dc.date.copyright2012en_US
dc.date.issued2012
dc.identifier.citationNikolaev, Y., & Pervushin, K. (2012). Structural basis of RNA binding by leucine zipper GCN4. Protein Science, 21(5), 667-676.en_US
dc.identifier.issn0961-8368en_US
dc.identifier.urihttp://hdl.handle.net/10220/10556
dc.description.abstractRecently, we showed that leucine zipper (LZ) motifs of basic leucine zipper (bZIP) transcription factors GCN4 and c-Jun are capable of catalyzing degradation of RNA (Nikolaev et al., PLoS ONE 2010; 5:e10765). This observation is intriguing given the tight regulation of RNA turnover control and the antiquity of bZIP transcription factors. To support further mechanistic studies, herein, we elucidated RNA binding interface of the GCN4 leucine zipper motif from yeast. Solution NMR experiments showed that the LZ-RNA interaction interface is located in the first two heptads of LZ moiety, and that only the dimeric (coiled coil) LZ conformation is capable of binding RNA. Site-directed mutagenesis of the LZ-GCN4 RNA binding interface showed that substrate binding is facilitated by lysine and arginine side chains, and that at least one nucleophilic residue is located in proximity to the RNA phosphate backbone. Further studies in the context of full-length bZIP factors are envisaged to address the biological relevance of LZ RNase activity.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesProtein scienceen_US
dc.rights© 2012 The Protein Society.en_US
dc.subjectDRNTU::Science::Biological sciences
dc.titleStructural basis of RNA binding by leucine zipper GCN4en_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1002/pro.2051


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