Abstract
The mRNA-protein complexes (mRNPs, Messenger ribonucleoprotein particles) are the “couriers” of the modern eukaryotes that process, store and deliver messages (transcripts) from the nucleus to the appropriate subcellular compartments and beyond. Presence of mRNPs arbitrates the posttranscriptional control of gene expression by editing the precursor RNA to maturity, postulate its subcellular localization and/or storage and dictate its fate once in the cytoplasm; either to be translated or dispensed through mRNA degradation. Initiation of transcription is coupled with processing of the transcribed message and the immediate association of the transcript with a set of structural and regulatory proteins. Per se, mRNP complexes sub-optimize transcription by recruiting RNA-binding proteins which are the core component of the RNP activities that culminate overall distribution and abundance of individual proteins. This asymmetric distribution of the mRNA is the determinant of protein gradient and is known to influence cell polarity, cell fate and overall patterning during development. Embryo patterning in Drosophila, polarization of maternal mRNA to daughter cell in budding yeast and directional growth of mammalian neural cell and pollen tubes of flowering plants, are the most prominent examples of mRNP facilitated posttranscriptional control, influencing cell fates and patterns of development.
This chapter addresses the current knowledge on the mechanisms of posttranscriptional control reinforced by the formation of RNP particles and reviews differences in the underlying mechanisms. The outline of the chapter encompasses step-wise cellular processes leading to the formation of mRNPs and its implication to cellular activities. A dedicated section is also integrated discussing the recent findings on the unique mechanism of RNP formation in the male gametophyte of Nicotiana tabaccum. A proposed model outlines the network of posttranscriptional control with a focus on the role of RNPs is also presented aiming to stimulate future research with a perspective of advancing our knowledge on the subject and its plausible application in improving food quality.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Honys D, Reňák D, Feciková J et al. Cytoskeleton-associated large RNP complexes in tobacco male gametophyte (EPPs) are associated with ribosomes and are involved in protein synthesis, processing, and localization. J Proteome Res 2009; 8(4):2015–2031.
Wood AJ, Oliver MJ. Translational control in plant stress: the formation of messenger ribonucleoprotein particles (mRNPs) in response to desiccation of Tortula ruralis gametophytes. The Plant Journal 1999; 18(4):359–370.
Bailey-Serres J, Sorenson R, Juntawong P. Getting the message across: cytoplasmic ribonucleoprotein complexes. Trends Plant Sci 2009; 14(8):443–453.
Ephrussi A, Dickinson LK, Lehmann R. Oskar organizes the germ plasm and directs localization of the posterior determinant nanos. Cell 1991; 66(1):37–50.
Gavis ER, Lehmann R. Localization of nanos RNA controls embryonic polarity. CELL-CAMBRIDGE MA-1992; 71:301–301.
Kloc M, Zearfoss NR, Etkin LD. Mechanisms of subcellular mRNA localization. Cell 2002; 108(4):533–544.
Yamagata H, Sugimoto T, Tanaka K et al. Biosynthesis of storage proteins in developing rice seeds. Plant Physiol. 1982; 70(4): 1094.
Choi SB, Wang C, Muench DG et al. Messenger RNA targeting of rice seed storage proteins to specific ER subdomains. Nature 2000; 407(6805):765–767.
Honys D, Combe JP, Twell D et al. The translationally repressed pollen-specific ntp303 mRNA is stored in nonpolysomal mRNPs during pollen maturation. Sex Plant Reprod 2000; 13(3):135–144.
Twell D. Pollen developmental biology. In: O’Neil SD, ed. Plant Reproduction. Annual Plant Reviews Sheffield, UK: Sheffield Academic Press; 2002. p. 86–153.
Honys D, Twell D. Comparative analysis of the Arabidopsis pollen transcriptome. Plant Physiol 2003; 132(2):640.
Honys D, Twell D. Transcriptome analysis of haploid male gametophyte development in Arabidopsis. Genome Biol 2004; 5(11):R85.
Čapková V, Štorchová H, Tupý J. Protein synthesis in pollen tubes: preferential formation of new species independent of transcription. Sex Plant Reprod 1988; (1): 150–155.
Štorchová H, Čapková V, Tupý J. A Nicotiana tabacum mRNA encoding a 69-kDa glycoprotein occurring abundantly in pollen tubes is transcribed but not translated during pollen development in the anthers. Planta 1994; 192(3):441–445.
Hachet O, Ephrussi A. Splicing of oskar RNA in the nucleus is coupled to its cytoplasmic localization. Nature 2004; 428(6986):959–963.
Tange TØ, Nott A, Moore MJ. The ever-increasing complexities of the exon junction complex. Curr Opin Cell Biol 2004; 16(3):279–284.
Lewis RA, Kress TL, Cote CA et al. Conserved and clustered RNA recognition sequences are a critical feature of signals directing RNA localization in Xenopus oocytes. Mech Dev 2004; 121(1):101–109.
Gonzalez I, Buonomo SBC, Nasmyth K et al. ASH1 mRNA localization in yeast involves multiple secondary structural elementsand Ash1 protein translation. Curr Biol 1999; 9(6):337–340.
Arn EA, Cha BJ, Theurkauf WE et al. Recognition of a bicoid mRNA localization signal by a protein complex containing Swallow, Nod and RNA binding proteins. Dev Cell 2003; 4(1):41–51.
Lipshitz HD, Smibert CA. Mechanisms of RNA localization and translational regulation. Curr Opin Genet Dev 2000; 10(5):476–488.
Martin KC, Ephrussi A. mRNA localization: gene expression in the spatial dimension. Cell 2009; 136(4):719–730.
Ross A, Oleynikov Y, Kislauskis E et al. Characterization of a beta-actin mRNA zipcode-binding protein. Mol Cell Biol 1997; 17(4):2158.
Farina KL, Huttelmaier S, Musunuru K et al. Two ZBP1 KH domains facilitate ta-actin mRNA localization, granule formation and cytoskeletal attachment. J Cell Biol 2003; 160(1):77.
Wang C, Washida H, Crofts AJ et al. The cytoplasmic-localized, cytoskeletal-associated RNA binding protein Os Tudor-SN: evidence for an essential role in storage protein RNA transport and localization. The Plant Journal 2008; 55(3):443–454.
Anderson P, Kedersha N. RNA granules: posttranscriptional and epigenetic modulators of gene expression. Nat Rev Mol Cell Biol 2009; 10(6):430–436.
Kiriakidou M, Tan GS, Lamprinaki S et al. An mRNA m7G cap binding-like motif within human Ago2 represses translation. Cell 2007; 129(6):1141–1151.
Crofts AJ, Washida H, Okita TW et al. Targeting of proteins to endoplasmic reticulum-derived compartments in plants. The importance of RNA localization. Plant Physiol 2004; 136(3):3414.
Muench DG, Park NI. Messages on the move: the role of the cytoskeleton in mRNA localization and translation in plant cells. Botany 2006; 84(4): 572–580.
de Heredia ML, Jansen RP. mRNA localization and the cytoskeleton.Curr Opin Cell Biol 2004; 16(1):80–85.
St Johnston D. Moving messages: the intracellular localization of mRNAs. Nat Rev Mol Cell Biol 2005; 6:363–375.
Lazarowitz SG, Beachy RN. Viral movement proteins as probes for intracellular and intercellular trafficking in plants. The Plant Cell Online 1999; 11(4):535.
Okita TW, Choi SB. mRNA localization in plants: targeting to the cell’s cortical region and beyond. Curr Opin Plant Biol 2002; 5(6):553–559.
Bartel DP. MicroRNAs genomics, biogenesis, mechanism and function. Cell 2004; 116(2):281–297.
Kidner CA, Martienssen RA. The developmental role of microRNA in plants. Curr Opin Plant Biol 2005; 8(1):38–44.
Why cells move messages: the biological functions of mRNA localization. Seminars in Cell and Developmental Biology: Elsevier; 2007.
Hannapel DJ. A model system of development regulated by the long-distance transport of mRNA. J Integr Plant Biol 2010; 52(1):40–52.
Anderson P, Kedersha N. RNA granules. J Cell Biol 2006; 172(6):803.
Boag PR, Atalay A, Robida S et al. Protection of specific maternal messenger RNAs by the P body protein CGH-1 (Dhh1/RCK) during Caenorhabditis elegans oogenesis. J Cell Biol 2008; 182(3):543.
Weterings K, Reijnen W, Aarssen R et al. Characterization of a pollen-specific cDNA clone from Nicotiana tabacum expressed during microgametogenesis and germination. Plant Mol Biol 1992; 18(6): 1101–1111.
Bayer M, Nawy T, Giglione C et al. Paternal control of embryonic patterning in Arabidopsis thaliana. Science’s STKE 2009; 323(5920): 1485.
Brengues M, Parker R. Accumulation of Polyadenylated mRNA, Pab1p, eIF4E and eIF4G with P-Bodies in Saccharomyces cerevisiae. Mol Biol Cell 2007; E06.
Baulcombe D. RNA silencing in plants. Nature 2004; 431(7006):356–363.
Kim VN, Han J, Siomi MC. Biogenesis of small RNAs in animals. Nat Rev Mol Cell Biol 2009; 10(2):126–139.
Fiore R, Siegel G, Schratt G. MicroRNA function in neuronal development, plasticity and disease. Biochim Biophys Acta 2008; 1779(8):471–478.
Aukerman MJ, Sakai H. Regulation of flowering time and floral organ identity by a microRNA and its APETALA2-like target genes. The Plant Cell Online 2003; 15(11):2730.
Chen X. A microRNA as a translational repressor of APETALA2 in Arabidopsis flower development. Science’s STKE 2004; 303(5666):2022.
Brodersen P, Sakvarelidze-Achard L, Bruun-Rasmussen M et al. Widespread translational inhibition by plant miRNAs and siRNAs. Science 2008; 320(5880):1185.
Collins LJ, Penny D. The RNA infrastructure: dark matter of the eukaryotic cell? Trends Genet 2009; 25(3):120–128.
Czaplinski K, Singer RH. Pathways for mRNA localization in the cytoplasm. Trends Biochem Sci 2006; 31(12):687–693.
Huttelmaier S, Zenklusen D, Lederer M et al. Spatial regulation of b-actin translation by Src-dependent phosphorylation of ZBP1. Nature 2005; 438:512–515.
Gu W, Deng Y, Zenklusen D et al. A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and is required for its localization. Genes Dev 2004; 18(12): 1452.
Meister G. miRNAs get an early start on translational silencing. Cell 2007; 131(1):25–28.
Holmes-Davis R, Tanaka CK, Vensel WH et al. Proteome mapping of mature pollen of Arabidopsis thaliana. Proteomics 2005; 5(18):4864–4884.
Noir S, Bräutigam A, Colby T et al. A reference map of the Arabidopsis thaliana mature pollen proteome. Biochem Biophys Res Commun 2005; 337(4):1257–1266.
Sheoran IS, Sproule KA, Olson DJH et al. Proteome profile and functional classification of proteins in Arabidopsis thaliana (Landsberg erecta) mature pollen. Sex Plant Reprod 2006; 19(4):185–196.
Grobei MA, Qeli E, Brunner E et al. Deterministic protein inference for shotgun proteomics data provides new insights into Arabidopsis pollen development and function. Genome Res 2009; 19(10):1786.
Forstemann K. Transposon defense in Drosophila somatic cells: A model for distinction of self and nonself in the genome. RNA Biol 2010; 7(2).
Malone CD, Brennecke J, Dus M et al. Specialized piRNA pathways act in germline and somatic tissues of the Drosophila ovary. Cell 2009; 137(3):522–535.
Pillai RS, Bhattacharyya SN, Artus CG et al. Inhibition of translational initiation by Let-7 MicroRNA in human cells. Science 2005; 309(5740):1573.
Sheth U, Parker R. Decapping and decay of messenger RNA occur in cytoplasmic processing bodies. Science 2003; 300(5620):805.
Sen GL, Blau HM. Argonaute 2/RISC resides in sites of mammalian mRNA decay known as cytoplasmic bodies. Nat Cell Biol 2005; 7(6):633–636.
Bhattacharyya SN, Habermacher R, Martine U et al. Relief of micro RNA-mediated translational repression in human cells subjected to stress. Cell 2006; 125(6): 1111–1124.
Chang Y, Imam JS, Wilkinson MF. The Nonsense-Mediated Decay RNA Surveillance Pathway. Annu Rev Biochem. 2007; 76(1):51–74.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2011 Landes Bioscience and Springer Science+Business Media, LLC
About this chapter
Cite this chapter
Hafidh, S., Čapková, V., Honys, D. (2011). Safe Keeping the Message: mRNP Complexes Tweaking after Transcription. In: Collins, L.J. (eds) RNA Infrastructure and Networks. Advances in Experimental Medicine and Biology, vol 722. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-0332-6_8
Download citation
DOI: https://doi.org/10.1007/978-1-4614-0332-6_8
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4614-0331-9
Online ISBN: 978-1-4614-0332-6
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)