Biochemistry and Molecular Biology
Volume 2, Issue 4, July 2017, Pages: 46-53
Received: Jun. 19, 2017;
Accepted: Jun. 29, 2017;
Published: Jul. 31, 2017
Views 1617 Downloads 139
Masashi Kurata, Division of Integrated Life Sciences, Graduate School of Biostudies, Kyoto University, Kyoto, Japan; Department of Oral and Maxillofacial Surgery, Graduate School of Medical Sciences, Nagoya City University, Nagoya, Japan
Mari Morimoto, Division of Integrated Life Sciences, Graduate School of Biostudies, Kyoto University, Kyoto, Japan
Yuko Kawamura, Department of Food and Nutrition, Kyoto Women’s University, Kyoto, Japan
Intisar Fouad Ali Mursi, Division of Integrated Life Sciences, Graduate School of Biostudies, Kyoto University, Kyoto, Japan
Keiko Momma, Department of Living and Welfare, Kyoto Women’s University, Kyoto, Japan
Masakazu Takahashi, Department of Bioscience, Fukui Prefectural University, Fukui, Japan
Yusaku Miyamae, Division of Integrated Life Sciences, Graduate School of Biostudies, Kyoto University, Kyoto, Japan
Taiho Kambe, Division of Integrated Life Sciences, Graduate School of Biostudies, Kyoto University, Kyoto, Japan
Masaya Nagao, Division of Integrated Life Sciences, Graduate School of Biostudies, Kyoto University, Kyoto, Japan
Hiroshi Narita, Department of Food and Nutrition, Kyoto Women’s University, Kyoto, Japan
Yasuyuki Shibuya, Department of Oral and Maxillofacial Surgery, Graduate School of Medical Sciences, Nagoya City University, Nagoya, Japan
Seiji Masuda, Division of Integrated Life Sciences, Graduate School of Biostudies, Kyoto University, Kyoto, Japan
Post-transcriptional modifications of nascent mRNA include 5’ capping, splicing and 3’ end polyadenylation, resulting in the emergence of mature mRNA. Recent findings indicate that mRNA splicing inhibitors can be potential anti-cancer candidates. Soy-isoflavone fractions displayed an inhibitory effect of mRNA processing among a number of dietary components. Two major components of the isoflavone fraction, daidzin and genistin did not have an inhibitory activity against mRNA maturation. The aglycone form of them also failed to inhibit mRNA maturation. Instead, compounds with flavone skeleton inhibited the mRNA maturation in the nucleus. Considering that the structural difference between flavone and isoflavone compounds is that B-ring is attached either on the 2’ or 3’ position of C-ring, respectively, anti-mRNA maturation activity may require a defined structural basis. These data indicate that compounds with flavone skeleton specifically alter the mRNA processing step.
Intisar Fouad Ali Mursi,
Inhibition of mRNA Maturation by Compounds Which Have a Flavonoid Skeleton, Biochemistry and Molecular Biology.
Vol. 2, No. 4,
2017, pp. 46-53.
Chang, TH, Tung, L, Yeh, FL, et al. Functions of the DExD/H-box proteins in nuclear pre-mRNA splicing, Biochim Biophys Acta. 2013; 1829:764-774.
de Klerk, E, t Hoen, PA. Alternative mRNA transcription, processing, and translation: insights from RNA sequencing, Trends Genet. 2015; 31:128-139.
Guo, J, Price, DH. RNA polymerase II transcription elongation control, Chem Rev. 2013; 113:8583-8603.
Han, J, Xiong, J, Wang, D, et al. Pre-mRNA splicing: where and when in the nucleus, Trends Cell Biol. 2011; 21:336-343.
Wickramasinghe, VO, Laskey, RA. Control of mammalian gene expression by selective mRNA export, Nature reviews. Molecular cell biology. 2015; 16:431-442.
Maniatis, T, Reed, R. An extensive network of coupling among gene expression machines, Nature. 2002;416:499-506.
Naftelberg, S, Schor, IE, Ast, G, et al. Regulation of alternative splicing through coupling with transcription and chromatin structure, Annu Rev Biochem. 2015; 84:165-198.
Saldi, T, Cortazar, MA, Sheridan, RM, et al. Coupling of RNA Polymerase II Transcription Elongation with Pre-mRNA Splicing, J Mol Biol. 2016; 428:2623-2635.
Liu, YC, Cheng, SC. Functional roles of DExD/H-box RNA helicases in Pre-mRNA splicing, J Biomed Sci. 2015;22:54.
Matera, AG, Wang, Z. A day in the life of the spliceosome, Nature reviews. Molecular cell biology. 2014; 15:108-121.
Misra, A, Green, MR. From polyadenylation to splicing: Dual role for mRNA 3' end formation factors, RNA Biol. 2016; 13:259-264.
Papasaikas, P, Valcarcel, J. The Spliceosome: The Ultimate RNA Chaperone and Sculptor, Trends Biochem Sci. 2016; 41:33-45.
Sperling, J, Azubel, M, Sperling, R. Structure and function of the Pre-mRNA splicing machine, Structure. 2008; 16:1605-1615.
Adamia, S, Pilarski, PM, Bar-Natan, M, et al. Alternative splicing in chronic myeloid leukemia (CML): a novel therapeutic target?, Curr Cancer Drug Targets. 2013; 13:735-748.
Arslan, AD, He, X, Wang, M, et al. A high-throughput assay to identify small-molecule modulators of alternative pre-mRNA splicing, J Biomol Screen. 2013; 18:180-190.
Bakkour, N, Lin, YL, Maire, S, et al. Small-molecule inhibition of HIV pre-mRNA splicing as a novel antiretroviral therapy to overcome drug resistance, PLoS Pathog. 2007; 3:1530-1539.
Daguenet, E, Dujardin, G, Valcarcel, J. The pathogenicity of splicing defects: mechanistic insights into pre-mRNA processing inform novel therapeutic approaches, EMBO Rep. 2015; 16:1640-1655.
Hahn, CN, Venugopal, P, Scott, HS, et al. Splice factor mutations and alternative splicing as drivers of hematopoietic malignancy, Immunol Rev. 2015; 263:257-278.
Le, KQ, Prabhakar, BS, Hong, WJ, et al. Alternative splicing as a biomarker and potential target for drug discovery, Acta Pharmacol Sin. 2015; 36:1212-1218.
Maguire, SL, Leonidou, A, Wai, P, et al. SF3B1 mutations constitute a novel therapeutic target in breast cancer, J Pathol. 2015; 235:571-580.
Nlend Nlend, R, Meyer, K, Schumperli, D. Repair of pre-mRNA splicing: prospects for a therapy for spinal muscular atrophy, RNA Biol. 2010; 7:430-440.
Salton, M, Misteli, T. Small Molecule Modulators of Pre-mRNA Splicing in Cancer Therapy, Trends Mol Med. 2016; 22:28-37.
Folco, EG, Coil, KE, Reed, R. The anti-tumor drug E7107 reveals an essential role for SF3b in remodeling U2 snRNP to expose the branch point-binding region, Genes Dev. 2011; 25:440-444.
Kaida, D, Motoyoshi, H, Tashiro, E, et al. Spliceostatin A targets SF3b and inhibits both splicing and nuclear retention of pre-mRNA, Nat Chem Biol. 2007; 3:576-583.
Kotake, Y, Sagane, K, Owa, T, et al. Splicing factor SF3b as a target of the antitumor natural product pladienolide, Nat Chem Biol. 2007; 3:570-575.
Hasegawa, M, Miura, T, Kuzuya, K, et al. Identification of SAP155 as the target of GEX1A (Herboxidiene), an antitumor natural product, ACS Chem Biol. 2011; 6:229-233.
O'Brien, K, Matlin, AJ, Lowell, AM, et al. The biflavonoid isoginkgetin is a general inhibitor of Pre-mRNA splicing, J Biol Chem. 2008; 283:33147-33154.
Pilch, B, Allemand, E, Facompre, M, et al. Specific inhibition of serine- and arginine-rich splicing factors phosphorylation, spliceosome assembly, and splicing by the antitumor drug NB-506, Cancer Res. 2001; 61:6876-6884.
Tazi, J, Bakkour, N, Soret, J, et al. Selective inhibition of topoisomerase I and various steps of spliceosome assembly by diospyrin derivatives, Mol Pharmacol. 2005; 67:1186-1194.
Ting, CY, Hsu, CT, Hsu, HT, et al. Isodiospyrin as a novel human DNA topoisomerase I inhibitor, Biochem Pharmacol. 2003; 66:1981-1991.
Muraki, M, Ohkawara, B, Hosoya, T, et al. Manipulation of alternative splicing by a newly developed inhibitor of Clks, J Biol Chem. 2004; 279:24246-24254.
Soret, J, Bakkour, N, Maire, S, et al. Selective modification of alternative splicing by indole derivatives that target serine-arginine-rich protein splicing factors, Proc Natl Acad Sci U S A. 2005; 102:8764-8769.
Baur, JA, Sinclair, DA. Therapeutic potential of resveratrol: the in vivo evidence, Nat Rev Drug Discov. 2006; 5:493-506.
Markus, MA, Marques, FZ, Morris, BJ. Resveratrol, by modulating RNA processing factor levels, can influence the alternative splicing of pre-mRNAs, PLoS One. 2011; 6:e28926.
Fujita, K, Okamura, M, Nishimoto, S, et al. Establishment of a monitoring system to detect inhibition of mRNA processing, Biosci Biotechnol Biochem. 2012; 76:1248-1251.
Kurata, M, Murata, Y, Momma, K, et al. The isoflavone fraction from soybean presents the mRNA maturation inhibition activity., Biosci Biotechnol Biochem. 2017; 81:551-554.
Fujiwara, N, Yoshikawa, M, Yamazaki, T, et al. A screening method tuned for mRNA processing factors in human cells by evaluation of the luciferase reporter activity and the subcellular distribution of bulk poly (A)+ RNA, Biosci Biotechnol Biochem. 2010; 74:1512-1516.
Masuda, S, Das, R, Cheng, H, et al. Recruitment of the human TREX complex to mRNA during splicing, Genes Dev. 2005; 19:1512-1517.
Yamazaki, T, Fujiwara, N, Yukinaga, H, et al. The closely related RNA helicases, UAP56 and URH49, preferentially form distinct mRNA export machineries and coordinately regulate mitotic progression, Mol Biol Cell. 2010; 21:2953-2965.
Kai, M, Yamauchi, A, Tominaga, K, et al. Soybean isoflavones eliminate nifedipine-induced flushing of tail skin in ovariectomized mice, J Pharmacol Sci. 2004; 95:476-478.
Schwartz, TU. The Structure Inventory of the Nuclear Pore Complex, J Mol Biol. 2016; 428:1986-2000.
Knockenhauer, KE, Schwartz, TU. The Nuclear Pore Complex as a Flexible and Dynamic Gate, Cell. 2016; 164:1162-1171.
von Appen, A, Beck, M. Structure Determination of the Nuclear Pore Complex with Three-Dimensional Cryo electron Microscopy, J Mol Biol. 2016; 428:2001-2010.
Hurt, E, Beck, M. Towards understanding nuclear pore complex architecture and dynamics in the age of integrative structural analysis, Curr Opin Cell Biol. 2015; 34:31-38.
Kabachinski, G, Schwartz, TU. The nuclear pore complex--structure and function at a glance, J Cell Sci. 2015; 128:423-429.
Ptak, C, Aitchison, JD, Wozniak, RW. The multifunctional nuclear pore complex: a platform for controlling gene expression, Curr Opin Cell Biol. 2014; 28:46-53.
Grossman, E, Medalia, O, Zwerger, M. Functional architecture of the nuclear pore complex, Annu Rev Biophys. 2012; 41:557-584.
Raices, M, D'Angelo, MA. Nuclear pore complex composition: a new regulator of tissue-specific and developmental functions, Nature reviews. Molecular cell biology. 2012; 13:687-699.
Hoelz, A, Debler, EW, Blobel, G. The structure of the nuclear pore complex, Annu Rev Biochem. 2011; 80:613-643.