Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/97237
Title: Structural basis of RNA binding by leucine zipper GCN4
Authors: Nikolaev, Yaroslav
Pervushin, Konstantin
Keywords: DRNTU::Science::Biological sciences
Issue Date: 2012
Source: Nikolaev, Y., & Pervushin, K. (2012). Structural basis of RNA binding by leucine zipper GCN4. Protein Science, 21(5), 667-676.
Series/Report no.: Protein science
Abstract: Recently, 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.
URI: https://hdl.handle.net/10356/97237
http://hdl.handle.net/10220/10556
ISSN: 0961-8368
DOI: http://dx.doi.org/10.1002/pro.2051
Rights: © 2012 The Protein Society.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

Google ScholarTM

Check

Altmetric

Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.