Structural basis of RNA binding by leucine zipper GCN4
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 a...
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| Format: | Journal Article |
| Language: | English |
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2013
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| Online Access: | https://hdl.handle.net/10356/97237 http://hdl.handle.net/10220/10556 |
| _version_ | 1824454668575571968 |
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| author | Nikolaev, Yaroslav Pervushin, Konstantin |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Nikolaev, Yaroslav Pervushin, Konstantin |
| author_sort | Nikolaev, Yaroslav |
| collection | NTU |
| description | 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. |
| first_indexed | 2025-02-19T03:25:58Z |
| format | Journal Article |
| id | ntu-10356/97237 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2025-02-19T03:25:58Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/972372022-02-16T16:27:23Z Structural basis of RNA binding by leucine zipper GCN4 Nikolaev, Yaroslav Pervushin, Konstantin School of Biological Sciences DRNTU::Science::Biological sciences 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. 2013-06-24T08:42:52Z 2019-12-06T19:40:28Z 2013-06-24T08:42:52Z 2019-12-06T19:40:28Z 2012 2012 Journal Article Nikolaev, Y., & Pervushin, K. (2012). Structural basis of RNA binding by leucine zipper GCN4. Protein Science, 21(5), 667-676. 0961-8368 https://hdl.handle.net/10356/97237 http://hdl.handle.net/10220/10556 10.1002/pro.2051 22374868 en Protein science © 2012 The Protein Society. |
| spellingShingle | DRNTU::Science::Biological sciences Nikolaev, Yaroslav Pervushin, Konstantin Structural basis of RNA binding by leucine zipper GCN4 |
| title | Structural basis of RNA binding by leucine zipper GCN4 |
| title_full | Structural basis of RNA binding by leucine zipper GCN4 |
| title_fullStr | Structural basis of RNA binding by leucine zipper GCN4 |
| title_full_unstemmed | Structural basis of RNA binding by leucine zipper GCN4 |
| title_short | Structural basis of RNA binding by leucine zipper GCN4 |
| title_sort | structural basis of rna binding by leucine zipper gcn4 |
| topic | DRNTU::Science::Biological sciences |
| url | https://hdl.handle.net/10356/97237 http://hdl.handle.net/10220/10556 |
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