Binding of miR398 to mRNA of Chaperone and Superoxide Dismutase Genes in Plants

<!DOCTYPE html> <html lang="en" dir="ltr"> <head>  <script async src="https://www.googletagmanager.com/gtag/js?id=G-P63WKM1TM1"></script> <script> window.dataLayer = window.dataLayer || []; function gtag(){dataLayer.push(arguments);} gtag('js', new Date()); gtag('config', 'G-P63WKM1TM1'); </script>  <script type="text/javascript" > (function(m,e,t,r,i,k,a){m[i]=m[i]||function(){(m[i].a=m[i].a||[]).push(arguments)}; m[i].l=1*new Date(); for (var j = 0; j < document.scripts.length; j++) {if (document.scripts[j].src === r) { return; }} k=e.createElement(t),a=e.getElementsByTagName(t)[0],k.async=1,k.src=r,a.parentNode.insertBefore(k,a)}) (window, document, "script", "https://mc.yandex.ru/metrika/tag.js", "ym"); ym(55165297, "init", { clickmap:false, trackLinks:true, accurateTrackBounce:true, webvisor:false }); </script> <noscript><div><img src="https://mc.yandex.ru/watch/55165297" style="position:absolute; left:-9999px;" alt="" /></div></noscript>    <title>Binding of miR398 to mRNA of Chaperone and Superoxide Dismutase Genes in Plants</title> <meta name="description" content="Binding of miR398 to mRNA of Chaperone and Superoxide Dismutase Genes in Plants"> <meta name="keywords" content="MicroRNA, mRNA, plant, superoxide dismutase."> <meta name="viewport" content="width=device-width, initial-scale=1, minimum-scale=1, maximum-scale=1, user-scalable=no"> <meta charset="utf-8"> <meta name="citation_title" content="Binding of miR398 to mRNA of Chaperone and Superoxide Dismutase Genes in Plants"> <meta name="citation_author" content="Assyl Bari"> <meta name="citation_author" content="Olga Berillo"> <meta name="citation_author" content="Saltanat Orazova"> <meta name="citation_author" content="Anatoliy Ivashchenko"> <meta name="citation_publication_date" content="2013/07/24"> <meta name="citation_journal_title" content="International Journal of Biotechnology and Bioengineering"> <meta name="citation_volume" content="7"> <meta name="citation_issue" content="7"> <meta 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Bari</a>, <a href="https://publications.waset.org/search?q=Olga%20Berillo"> Olga Berillo</a>, <a href="https://publications.waset.org/search?q=Saltanat%20Orazova"> Saltanat Orazova</a>, <a href="https://publications.waset.org/search?q=Anatoliy%20Ivashchenko"> Anatoliy Ivashchenko</a> </p> <p class="card-text"><strong>Abstract:</strong></p> <p>Among all microRNAs (miRNAs) in 12 plant species investigated in this study, only miR398 targeted the copper chaperone for superoxide dismutase (CCS). The nucleotide sequences of miRNA binding sites were located in the mRNA protein-coding sequence (CDS) and were highly homologous. These binding sites in CCS mRNA encoded a conservative GDLGTL hexapeptide. The binding sites for miR398 in the CDS of superoxide dismutase 1 mRNA encoded GDLGN pentapeptide. The conservative miR398 binding site located in the CDS of superoxide dismutase 2 mRNA encoded the GDLGNI hexapeptide. The miR398 binding site in the CDS of superoxide dismutase 3 mRNA encoded the GDLGNI or GDLGNV hexapeptide. Gene expression of the entire superoxide dismutase family in the studied plant species was regulated only by miR398. All members of the miR398 family, i.e. miR398a,b,c were connected to one site for each CuZnSOD and chaperone mRNA.</p> <iframe src="https://publications.waset.org/16260.pdf" style="width:100%; height:400px;" frameborder="0"></iframe> <p class="card-text"><strong>Keywords:</strong> <a href="https://publications.waset.org/search?q=MicroRNA" title="MicroRNA">MicroRNA</a>, <a href="https://publications.waset.org/search?q=mRNA" title=" mRNA"> mRNA</a>, <a href="https://publications.waset.org/search?q=plant" title=" plant"> plant</a>, <a href="https://publications.waset.org/search?q=superoxide%20dismutase." title=" superoxide dismutase."> superoxide dismutase.</a> </p> <p class="card-text"><strong>Digital Object Identifier (DOI):</strong> <a href="https://doi.org/10.5281/zenodo.1086873" target="_blank">doi.org/10.5281/zenodo.1086873</a> </p> <a href="https://publications.waset.org/16260/binding-of-mir398-to-mrna-of-chaperone-and-superoxide-dismutase-genes-in-plants" class="btn btn-primary btn-sm">Procedia</a> <a href="https://publications.waset.org/16260/apa" target="_blank" rel="nofollow" class="btn btn-primary btn-sm">APA</a> <a href="https://publications.waset.org/16260/bibtex" target="_blank" rel="nofollow" class="btn btn-primary btn-sm">BibTeX</a> <a href="https://publications.waset.org/16260/chicago" target="_blank" rel="nofollow" class="btn btn-primary btn-sm">Chicago</a> <a href="https://publications.waset.org/16260/endnote" target="_blank" rel="nofollow" class="btn btn-primary btn-sm">EndNote</a> <a href="https://publications.waset.org/16260/harvard" target="_blank" rel="nofollow" class="btn btn-primary btn-sm">Harvard</a> <a href="https://publications.waset.org/16260/json" target="_blank" rel="nofollow" class="btn btn-primary btn-sm">JSON</a> <a href="https://publications.waset.org/16260/mla" target="_blank" rel="nofollow" class="btn btn-primary btn-sm">MLA</a> <a href="https://publications.waset.org/16260/ris" target="_blank" rel="nofollow" class="btn btn-primary btn-sm">RIS</a> <a href="https://publications.waset.org/16260/xml" target="_blank" rel="nofollow" class="btn btn-primary btn-sm">XML</a> <a href="https://publications.waset.org/16260/iso690" target="_blank" rel="nofollow" class="btn btn-primary btn-sm">ISO 690</a> <a href="https://publications.waset.org/16260.pdf" target="_blank" class="btn btn-primary btn-sm">PDF</a> <span class="bg-info text-light px-1 py-1 float-right rounded"> Downloads <span class="badge badge-light">1910</span> </span> <p class="card-text"><strong>References:</strong></p> <p><br>[1] X. Jia, V. Mendu, G. Tang, “An array platform for identification of stress-responsive microRNAs in plants,” Methods Mol. Biol., vol. 639, pp. 253-269, 2010. <br>[2] L. Beauclair, A. Yu, N. Bouché, “microRNA-directed cleavage and translational repression of the copper chaperone for superoxide dismutase mRNA in Arabidopsis,” Plant J., vol. 62, no. 3, pp. 454-462, 2010. <br>[3] K.A. Markossian, B.I. Kurganov, “Copper chaperones, intracellular copper trafficking proteins. Function, structure, and mechanism of action,” Biochemistry (Mosc), vol. 68, no. 8, pp. 827-837, 2003. <br>[4] H. Yamasaki, S.E. Abdel-Ghany, C.M. Cohu, Y. Kobayashi, T. Shikanai, M. Pilon, “Regulation of copper homeostasis by micro-RNA in Arabidopsis,” J. Biol. Chem., vol. 282, no. 22, pp.16369-16378, 2007. <br>[5] Y.F. Ding, C. Zhu, “The role of microRNAs in copper and cadmium homeostasis,” Biochem. Biophys. Res. Commun., vol. 386, no. 1, pp. 6- 10, 2009. <br>[6] G. Jagadeeswaran, A. Saini, R. Sunkar, “Biotic and abiotic stress downregulate miR398 expression in Arabidopsis,” Planta, vol. 229, no. 4, pp.1009-1014, 2009. <br>[7] Y.F. Ding, G.Y. Wang, Y.P. Fu, C. Zhu. Yi Chuan, “The role of miR398 in plant stress responses,” Yi Chuan, vol. 32, no. 2, pp. 129-134, 2010. <br>[8] N. Bouché, “New insights into miR398 functions in Arabidopsis,” Plant Signal Behav., vol. 5, no. 6, pp. 684-686, 2010. <br>[9] D.H. Jeong, M.A. German, L.A. Rymarquis, S.R. Thatcher, P.J. Green, “Abiotic stress-associated miRNAs: detection and functional analysis,” Methods Mol. Biol., vol. 592, pp. 203-230, 2010. <br>[10] Y. Lu, Z. Feng, L. Bian, H. Xie, J. Liang, “miR398 regulation in rice of the responses to abiotic and biotic stresses depends on CSD1 and CSD2 expression,” Func. Plant Biol., vol. 38, no. 1, pp. 44-53, 2010. <br>[11] M. Kantar, S.J. Lucas, H. 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Baier, “The strength of the miR398-Csd2-CCS1 regulon is subject to natural variation in Arabidopsis thaliana,” FEBS Lett., vol. 586, no. 19, pp. 3385-90, 2012. <br>[20] C.C. Chu, W.C. Lee, W.Y. Guo, S.M. Pan, L.J. Chen, H.M. Li, T.L. Jinn, “A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis,” Plant Physiol., vol. 139, no. 1, pp. 425-436, 2005. <br>[21] G.B. Robb, T.M. Rana, “RNA helicase. A interacts with RISC in human cells and functions in RISC loading,” Mol. 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Binding of miR398 to mRNA of Chaperone and Superoxide Dismutase Genes in Plants