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The full-length cloning and functional prediction of Nicotiana benthamiana cajal body protein |
GUO Xiao-nan, LI Yang, XIE Li, ZHENG Lu-ping* |
Key Laboratory of Biopesticide and Chemical Biology, Ministry of Education, Fujian Agriculture and Forestry University, Fuzhou 350002,China |
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Abstract Coilin is a marker of cajal body (CB), which involves in virus infection. Based on the blast results of Arabidopsis thaliana coilin against Nicotiana benthamiana genome database, primers were designed to amplify the putative full-length Nbcoilin gene with 3 017 bp in length. The complete coding region for this gene is 2 409 bp in length, encoding 803 amino acids. It contains the typical functional domains of coilin protein and an analog motif of the animal coilin ‘RGG' box. Phylogenetic analysis showed that the cloned Nbcoilin gene was placed in a cluster with other plant coilins. The subcellular localization analysis showed Nbcoilin was localized to the cajal bodies. These results indicated that the cloned Nbcoilin gene is a homologous protein of coilin, and laid a foundation for further studying the function of Nbcoilin and its interaction with plant viruses.
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Received: 28 October 2019
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[1] Gall J G. Cajal bodies: thefirst 100 years [J]. Annual Review of Cell and Development Biology, 2000, 16: 273-300. [2] Love A J, Yu C, Petukhova N V,et al. Cajal bodies and their role in plant stress and disease responses [J]. RNA Biology, 2017, 14(6): 779-790. [3] Makaro V V, Rakitin A D, Protopopova A, et al. Plant Coilin: Structural characteristics and RNA-binding properties [J].PLoS One, 2013, 8(1): e53571. [4] Pontes O, Pikaard C S.siRNA and miRNA processing: new functions for cajal bodies [J]. Current Opinion Genetics & Development, 2008, 18(2): 197-203. [5] Liu J L, Wu Z, Nizami Z,et al. Coilin is essential for cajal body organization in Drosophila melanogaster [J]. Molecular Biology of Cell, 2009, 20(6): 1661-1670. [6] Strzelecka M S, Trowitzsch G, Weber R,et al.Coilin-dependent snRNP assembly is essential for zebrafish embryogenesis [J]. Nature Structural & Molecular Biology, 2010, 17(4): 403-409. [7] Walker M P, Tian L, Matera A G. Reduced viability, fertility and fecundity in mice lacking the cajal body marker protein, coilin [J]. PLoS One, 2009, 4(7): e6171. [8] Kim S H, Ryabov E V, Kalinina N O, et al. Cajal bodies and the nucleolus are required for a plant virus systemic infection [J]. The EMBO Journal, 2007, 26(8): 2169-2179. [9] Kim S H, Macfarlane S, Kalinina N O, et al. Interaction of a plant virus-encoded protein with the major nucleolar protein fibrillarin is required for systemic virus infection [J]. Proceedings of the National Academy of Sciences of the United States of America, 2007, 104(26): 11115-11120. [10]Rajamäki M L,Valkonen J P.Control of nuclear and nucleolar localization of nuclear inclusion protein a of picorna-like Potato virus A in Nicotiana species [J].The Plant Cell Online, 2009,21 (8): 2485-2502. [11]Shaw J, Love A J, Makarova S S,et al. Coilin, the signature protein of Cajal bodies, differentially modulates the interactions of plants with viruses in widely different taxa [J]. Nucleus, 2014, 5(1): 85-94. [12]Sleeman J E, Ajuh P, Lamond A I. snRNP protein expression enhances the formation of Cajal bodies containing p80-coilin and SMN [J]. Journal of Cell Science, 2001, 114(24): 4407-4419. [13]Pontes O, Li C F, Costa Nunes P,et al. The Arabidopsis chromatin-modifying nuclear siRNA pathway involves a nucleolar RNA processing center [J]. Cell, 2006, 126(1): 79-92. [14]Reed M L, Dove B K, Jackson R M, et al. Delineation and modeling of a nucleolar retention signal the coronavirus nucleocapsid protein [J]. Traffic, 2006, 7(7): 833-848. [15]Hebert M D. Phosphorylation and the Cajal body: modification in search of function [J].Archives of Biochemistry and Biophysic, 2010, 496(2):69-76. [16]Yamada M, Sato T, Shimohata T, et al. Interaction between neuronal intranuclear inclusions and promyelocytic leukemia protein nuclear and coiled bodies in CAG repeat diseases [J]. The American Journal of Pathology, 2001,159(5):1785-1795. [17]Shaw P, Brown J. Nucleoli: composition, function, and dynamics [J]. Plant Physiology, 2012,158(1): 44-51. [18]Zheng L,Du Z,Lin C,et al. Rice stripe tenuivirus p2 may recruit or manipulate nucleolar functions through an interaction with fibrillarin to promote virus systemicmovement [J]. Molecular Plant Pathology, 2015, 16 (9): 921-930. [19]Chang C H, Hsu F C, Lee S C, et al. The nucleolar fibrillarin protein is required for helper virus-indepen-dent long-distance trafficking of a subviral satellite RNA in plants [J]. Plant Cell, 2016, 28 (10): 2586-2602. [20]Kumar D, Broor S, Rajala M S. Interaction of host nucleolin with Influenza A virus nucleoprotein in the early phase of infection limits the late viral gene expression [J]. PLoS One, 2016, 11(10): e0164146. |
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