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The Role of RNA Structure in Posttranscriptional Regulation of Gene Expression

Elina Jacobs James D. Mills Michael Janitz

Elina Jacobs, James D. Mills, Michael Janitz. The Role of RNA Structure in Posttranscriptional Regulation of Gene Expression[J]. Journal of Genetics and Genomics, 2012, 39(10): 535-543. doi: 10.1016/j.jgg.2012.08.002
Citation: Elina Jacobs, James D. Mills, Michael Janitz. The Role of RNA Structure in Posttranscriptional Regulation of Gene Expression[J]. Journal of Genetics and Genomics, 2012, 39(10): 535-543. doi: 10.1016/j.jgg.2012.08.002

doi: 10.1016/j.jgg.2012.08.002

The Role of RNA Structure in Posttranscriptional Regulation of Gene Expression

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    Corresponding author: E-mail address: m.janitz@unsw.edu.au (Michael Janitz)
  • Present address: College of Science and Engineering, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom.
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    Present address: College of Science and Engineering, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom.
  • [1] Araujo, P.R., Yoon, K., Ko, D. et al. Before it gets started: regulating translation at the 5′ UTR Comp. Funct. Genomics, 2012 (2012),p. 475731
    [2] Avila, J. The tau code Front Aging Neurosci., 1 (2009),p. 1
    [3] Babendure, J.R., Babendure, J.L., Ding, J.H. et al. Control of mammalian translation by mRNA structure near caps RNA, 12 (2006),pp. 851-861
    [4] Bentley, D.L. Rules of engagement: co-transcriptional recruitment of pre-mRNA processing factors Curr. Opin. Cell Biol., 17 (2005),pp. 251-256
    [5] Berget, S.M., Moore, C., Sharp, P.A. Spliced segments at the 5′ terminus of adenovirus 2 late mRNA Proc. Natl. Acad. Sci. USA, 74 (1977),pp. 3171-3175
    [6] Binder, R., Horowitz, J.A., Basilion, J.P. et al. Evidence that the pathway of transferrin receptor mRNA degradation involves an endonucleolytic cleavage within the 3′ UTR and does not involve poly(A) tail shortening EMBO J., 13 (1994),pp. 1969-1980
    [7] Bittencourt, D., Auboeuf, D. Analysis of co-transcriptional RNA processing by RNA-ChIP assay Methods Mol. Biol., 809 (2012),pp. 563-577
    [8] Black, D.L. Mechanisms of alternative pre-messenger RNA splicing Annu. Rev. Biochem., 72 (2003),pp. 291-336
    [9] Cheah, M.T., Wachter, A., Sudarsan, N. et al. Control of alternative RNA splicing and gene expression by eukaryotic riboswitches Nature, 447 (2007),pp. 497-500
    [10] Chen, Y., Carlini, D.B., Baines, J.F. et al. RNA secondary structure and compensatory evolution Genes Genet. Syst., 74 (1999),pp. 271-286
    [11] Chow, L.T., Gelinas, R.E., Broker, T.R. et al. An amazing sequence arrangement at the 5′ ends of adenovirus 2 messenger RNA Cell, 12 (1977),pp. 1-8
    [12] Ding, Y., Lawrence, C.E. Statistical prediction of single-stranded regions in RNA secondary structure and application to predicting effective antisense target sites and beyond Nucleic Acids Res., 29 (2001),pp. 1034-1046
    [13] Donahue, C.P., Muratore, C., Wu, J.Y. et al. Stabilization of the tau exon 10 stem loop alters pre-mRNA splicing J. Biol. Chem., 281 (2006),pp. 23302-23306
    [14] Estes, P.A., Cooke, N.E., Liebhaber, S.A. A native RNA secondary structure controls alternative splice-site selection and generates two human growth hormone isoforms J. Biol. Chem., 267 (1992),pp. 14902-14908
    [15] Ezkurdia, I., Del Pozo, A., Frankish, A. et al. Comparative proteomics reveals a significant bias toward alternative protein isoforms with conserved structure and function Mol. Biol. Evol., 29 (2012),pp. 2265-2283
    [16] Floris, M., Raimondo, D., Leoni, G. et al. MAISTAS: a tool for automatic structural evaluation of alternative splicing products Bioinformatics, 27 (2011),pp. 1625-1629
    [17] Gagna, C.E., Lambert, W.C. Med. Hypotheses, 67 (2006),pp. 1099-1114
    [18] Gagna, C.E., Lambert, W.C. Novel multistranded, alternative, plasmid and helical transitional DNA and RNA microarrays: implications for therapeutics Pharmacogenomics, 10 (2009),pp. 895-914
    [19] Gingold, H., Pilpel, Y. Determinants of translation efficiency and accuracy Mol. Syst. Biol., 7 (2011),p. 481
    [20] Gu, W., Zhou, T., Wilke, C.O. A universal trend of reduced mRNA stability near the translation-initiation site in prokaryotes and eukaryotes PLoS Comput. Biol., 6 (2010),p. e1000664
    [21] Hallegger, M., Llorian, M., Smith, C.W. Alternative splicing: global insights FEBS J., 277 (2010),pp. 856-866
    [22] Hegyi, H., Kalmar, L., Horvath, T. et al. Verification of alternative splicing variants based on domain integrity, truncation length and intrinsic protein disorder Nucleic Acids Res., 39 (2011),pp. 1208-1219
    [23] Huynen, M.A., Konings, D.A., Hogeweg, P. Multiple coding and the evolutionary properties of RNA secondary structure J. Theor. Biol., 165 (1993),pp. 251-267
    [24] Jenkins, R.H., Bennagi, R., Martin, J. et al. A conserved stem loop motif in the 5′untranslated region regulates transforming growth factor-β1 translation PLoS ONE, 5 (2010),p. e12283
    [25] Jin, Y., Yang, Y., Zhang, P. New insight into RNA secondary structure on alternative splicing of pre-mRNA RNA Biology, 8 (2011),pp. 450-457
    [26] Kar, A., Fushimi, K., Zhou, X. et al. RNA helicase p68 (DDX5) regulates tau exon 10 splicing by modulating a stem-loop structure at the 5′ splice site Mol. Cell. Biol., 31 (2011),pp. 1812-1821
    [27] Kertesz, M., Wan, Y., Mazor, E. et al. Genome-wide measurement of RNA secondary structure in yeast Nature, 467 (2010),pp. 103-107
    [28] Kim, S.J., Park, K., Koeller, D. et al. Post-transcriptional regulation of the human transforming growth factor-β1 gene J. Biol. Chem., 267 (1992),pp. 13702-13707
    [29] Kochetov, A.V., Palyanov, A., Titov, I.I. et al. AUG_hairpin: prediction of a downstream secondary structure influencing the recognition of a translation start site BMC Bioinformatics, 8 (2007),p. 318
    [30] Kozak, M. Leader length and secondary structure modulate mRNA function under conditions of stress Mol. Cell. Biol., 8 (1988),pp. 2737-2744
    [31] Kozak, M. Circumstances and mechanisms of inhibition of translation by secondary structure in eucaryotic mRNAs Mol. Cell. Biol., 9 (1989),pp. 5134-5142
    [32] Kozak, M. Context effects and inefficient initiation at non-AUG codons in eucaryotic cell-free translation systems Mol. Cell. Biol., 9 (1989),pp. 5073-5080
    [33] Kozak, M. Downstream secondary structure facilitates recognition of initiator codons by eukaryotic ribosomes Proc. Natl. Acad. Sci. USA, 87 (1990),pp. 8301-8305
    [34] Kozak, M. Gene, 361 (2005),pp. 13-37
    [35] Li, X., Quon, G., Lipshitz, H.D. et al. Predicting in vivo binding sites of RNA-binding proteins using mRNA secondary structure RNA, 16 (2010),pp. 1096-1107
    [36] Lucks, J.B., Mortimer, S.A., Trapnell, C. et al. Multiplexed RNA structure characterization with selective 2′-hydroxyl acylation analyzed by primer extension sequencing (SHAPE-Seq) Proc. Natl. Acad. Sci. USA, 108 (2011),pp. 11063-11068
    [37] Mattick, J.S., Makunin, I.V. Non-coding RNA Hum. Mol. Genet., 15 Spec (2006),pp. R17-R29
    [38] McManus, C.J., Graveley, B.R. RNA structure and the mechanisms of alternative splicing Curr. Opin. Genet. Dev., 21 (2011),pp. 373-379
    [39] Melamud, E., Moult, J. Stochastic noise in splicing machinery Nucleic Acids Res., 37 (2009),pp. 4873-4886
    [40] Melamud, E., Moult, J. Structural implication of splicing stochastics Nucleic Acids Res., 37 (2009),pp. 4862-4872
    [41] Merino, E.J., Wilkinson, K.A., Coughlan, J.L. et al. RNA structure analysis at single nucleotide resolution by selective 2′-hydroxyl acylation and primer extension (SHAPE) J. Am. Chem. Soc., 127 (2005),pp. 4223-4231
    [42] Mignone, F., Gissi, C., Liuni, S. et al. Untranslated regions of mRNAs Genome Biol., 3 (2002)
    [43] Modrek, B., Lee, C.J. Alternative splicing in the human, mouse and rat genomes is associated with an increased frequency of exon creation and/or loss Nat. Genet., 34 (2003),pp. 177-180
    [44] Novikova, I.V., Hennelly, S.P., Sanbonmatsu, K.Y. Structural architecture of the human long non-coding RNA, steroid receptor RNA activator Nucleic Acids Res., 40 (2012),pp. 5034-5051
    [45] Oikawa, D., Tokuda, M., Hosoda, A. et al. Identification of a consensus element recognized and cleaved by IRE1 α Nucleic Acids Res., 38 (2010),pp. 6265-6273
    [46] Pan, Q., Shai, O., Lee, L.J. et al. Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing Nat. Genet., 40 (2008),pp. 1413-1415
    [47] Pan, Q., Shai, O., Misquitta, C. et al. Revealing global regulatory features of mammalian alternative splicing using a quantitative microarray platform Mol. Cell, 16 (2004),pp. 929-941
    [48] Pesole, G., Grillo, G., Larizza, A. et al. The untranslated regions of eukaryotic mRNAs: structure, function, evolution and bioinformatic tools for their analysis Brief Bioinformatics, 1 (2000),pp. 236-249
    [49] Poliseno, L., Salmena, L., Zhang, J. et al. A coding-independent function of gene and pseudogene mRNAs regulates tumour biology Nature, 465 (2010),pp. 1033-1038
    [50] Rabl, J., Leibundgut, M., Ataide, S.F. et al. Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1 Science, 331 (2011),pp. 730-736
    [51] Romeo, D.S., Park, K., Roberts, A.B. et al. An element of the transforming growth factor-beta 1 5′-untranslated region represses translation and specifically binds a cytosolic factor Mol. Endocrinol., 7 (1993),pp. 759-766
    [52] Shepard, S., McCreary, M., Fedorov, A. The peculiarities of large intron splicing in animals PLoS ONE, 4 (2009),p. e7853
    [53] Singh, N.N., Androphy, E.J., Singh, R.N. An extended inhibitory context causes skipping of exon 7 of SMN2 in spinal muscular atrophy Biochem. Biophys. Res. Commun., 315 (2004),pp. 381-388
    [54] Singh, N.N., Singh, R.N., Androphy, E.J. Modulating role of RNA structure in alternative splicing of a critical exon in the spinal muscular atrophy genes Nucleic Acids Res., 35 (2007),pp. 371-389
    [55] Sirand-Pugnet, P., Durosay, P., Clouet d'Orval, B.C. et al. β-Tropomyosin pre-mRNA folding around a muscle-specific exon interferes with several steps of spliceosome assembly J. Mol. Biol., 251 (1995),pp. 591-602
    [56] Svitkin, Y.V., Pause, A., Haghighat, A. et al. The requirement for eukaryotic initiation factor 4A (elF4A) in translation is in direct proportion to the degree of mRNA 5′ secondary structure RNA, 7 (2001),pp. 382-394
    [57] Tsao, D., Shabalina, S.A., Gauthier, J. et al. Disruptive mRNA folding increases translational efficiency of catechol-O-methyltransferase variant Nucleic Acids Res., 39 (2011),pp. 6201-6212
    [58] Underwood, J.G., Uzilov, A.V., Katzman, S. et al. FragSeq: transcriptome-wide RNA structure probing using high-throughput sequencing Nat. Methods, 7 (2010),pp. 995-1001
    [59] Varani, L., Hasegawa, M., Spillantini, M.G. et al. Structure of tau exon 10 splicing regulatory element RNA and destabilization by mutations of frontotemporal dementia and parkinsonism linked to chromosome 17 Proc. Natl. Acad. Sci. USA, 96 (1999),pp. 8229-8234
    [60] Vogel, C., Abreu Rde, S., Ko, D. et al. Sequence signatures and mRNA concentration can explain two-thirds of protein abundance variation in a human cell line Mol. Syst. Biol., 6 (2010),p. 400
    [61] Wan, Y., Kertesz, M., Spitale, R.C. et al. Understanding the transcriptome through RNA structure Nat. Rev. Genet., 12 (2011),pp. 641-655
    [62] Wang, Z., Burge, C.B. Splicing regulation: from a parts list of regulatory elements to an integrated splicing code RNA, 14 (2008),pp. 802-813
    [63] Warf, M.B., Berglund, J.A. Role of RNA structure in regulating pre-mRNA splicing Trends Biochem. Sci., 35 (2010),pp. 169-178
    [64] Washietl, S. Sequence and structure analysis of noncoding RNAs Methods Mol. Biol., 609 (2010),pp. 285-306
    [65] Weeks, K.M., Mauger, D.M. Exploring RNA structural codes with SHAPE chemistry Acc. Chem. Res., 44 (2011),pp. 1280-1291
    [66] Wen, J.D., Lancaster, L., Hodges, C. et al. Following translation by single ribosomes one codon at a time Nature, 452 (2008),pp. 598-603
    [67] Wu, J., Yuan, H., Tan, S. et al. Increased complexity of gene structure and base composition in vertebrates J. Genet. Genomics, 38 (2011),pp. 297-305
    [68] Yang, Y., Zhan, L., Zhang, W. et al. RNA secondary structure in mutually exclusive splicing Nat. Struct. Mol. Biol., 18 (2011),pp. 159-168
    [69] Zhang, J., Kuo, C.C., Chen, L. GC content around splice sites affects splicing through pre-mRNA secondary structures BMC Genomics, 12 (2011),p. 90
    [70] Zheng, S., Chen, Y., Donahue, C.P. et al. Structural basis for stabilization of the tau pre-mRNA splicing regulatory element by novantrone (mitoxantrone) Chem. Biol., 16 (2009),pp. 557-566
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出版历程
  • 收稿日期:  2012-06-27
  • 录用日期:  2012-08-17
  • 修回日期:  2012-08-16
  • 网络出版日期:  2012-09-05
  • 刊出日期:  2012-10-20

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