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Cited by 47RNA and protein synthesis mechanismsRNA Research and SplicingRNA modifications and cancer

Functional Cyclization of Eukaryotic mRNAs

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Alekhina, Olga, Terenin, Ilya, Dmitriev, Sergey, Vassilenko, Konstantin·2020·International Journal of Molecular Sciences
DOI 10.3390/ijms21051677PMC PMC7084953
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Abstract

The closed-loop model of eukaryotic translation states that mRNA is circularized by a chain of the cap-eIF4E-eIF4G-poly(A)-binding protein (PABP)-poly(A) interactions that brings 5′ and 3′ ends together. This circularization is thought to promote the engagement of terminating ribosomes to a new round of translation at the same mRNA molecule, thus enhancing protein synthesis. Despite the general acceptance and the elegance of the hypothesis, it has never been proved experimentally. Using continuous in situ monitoring of luciferase synthesis in a mammalian in vitro system, we show here that the rate of translation initiation at capped and polyadenylated reporter mRNAs increases after the time required for the first ribosomes to complete mRNA translation. Such acceleration strictly requires the presence of a poly(A)-tail and is abrogated by the addition of poly(A) RNA fragments or m7GpppG cap analog to the translation reaction. The optimal functional interaction of mRNA termini requires 5′ untranslated region (UTR) and 3′ UTR of moderate lengths and provides stronger acceleration, thus a longer poly(A)-tail. Besides, we revealed that the inhibitory effect of the dominant negative R362Q mutant of initiation factor eIF4A diminishes in the course of translation reaction, suggesting a relaxed requirement for ATP. Taken together, our results imply that, upon the functional looping of an mRNA, the recycled ribosomes can be recruited to the start codon of the same mRNA molecule in an eIF4A-independent fashion. This non-canonical closed-loop assisted reinitiation (CLAR) mode provides efficient translation of the functionally circularized mRNAs.

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  • A critically important factor influencing differences in 5′ UTR activity is potential interactions between 5′ UTR and other regions of mRNA (CDS, 3′ UTR).

    “Moreover, a critically important factor influencing the differences in 5′ UTR activity is the potential interactions between the 5′ UTR and other regions of the mRNA (CDS, 3′ UTR).”

    From Identification of novel 5’ UTR variants for enhanced mRNA translation and vaccine immunogenicity (2026) · cites this paper as [35]

  • Such cross-talk can be realized through formation of long-range RNA-RNA interactions (secondary and tertiary structures) or mediated by components of translational machinery, such as RNA-binding proteins and factors that form mRNA closed-loop structure.

    “Such cross-talk can be realized through the formation of long-range RNA-RNA interactions (secondary and tertiary structures) or mediated by components of the translational machinery, such as RNA-binding proteins and factors that form the mRNA closed-loop structure [35].”

    From Identification of novel 5’ UTR variants for enhanced mRNA translation and vaccine immunogenicity (2026) · cites this paper as [35]

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  1. [1]Mathias A.P. Williamson R. Huxley H.E. Page S. Occurrence and Function of Polysomes in Rabbit Reticulocytes J. Mol. Biol. 1964 9 154 167 10.1016/S0022-2836(64)80097-8 14200379 · DOI
  2. [2]Shelton E. Kuff E.L. Substructure and configuration of ribosomes isolated from mammalian cells J. Mol. Biol. 1966 22 23 24 10.1016/0022-2836(66)90177-X · DOI
  3. [3]Ladhoff A.M. Uerlings I. Rosenthal S. Electron microscopic evidence of circular molecules in 9-S globin mRNA from rabbit reticulocytes Mol. Biol. Rep. 1981 7 101 106 10.1007/BF00778739 7019667 · DOI
  4. [4]Christensen A.K. Kahn L.E. Bourne C.M. Circular polysomes predominate on the rough endoplasmic reticulum of somatotropes and mammotropes in the rat anterior pituitary Am. J. Anat. 1987 178 1 10 10.1002/aja.1001780102 3825959 · DOI
  5. [5]Philipps G.R. Haemoglobin Synthesis and Polysomes in Intact Reticulocytes Nature 1965 205 567 570 10.1038/205567a0 14298546 · DOI
  6. [6]Jacobson A. Poly(A) Metabolism and Translation: The Closed-loop Model Translational Control Hershey J.W.B. Mathews M.B. Sonenberg N. Springer Berlin/Heidelberg, Germany 1996 451 480
  7. [7]Jacobson A. Favreau M. Possible involvement of poly(A) in protein synthesis Nucleic Acids Res. 1983 11 6353 6368 10.1093/nar/11.18.6353 6137807 PMC326378 · DOI
  8. [8]Palatnik C.M. Wilkins C. Jacobson A. Translational control during early Dictyostelium development: Possible involvement of poly(A) sequences Cell 1984 36 1017 1025 10.1016/0092-8674(84)90051-5 6142768 · DOI
  9. [9]Gallie D.R. The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency Genes Dev. 1991 5 2108 2116 10.1101/gad.5.11.2108 1682219 · DOI · Paper page
  10. [10]Iizuka N. Najita L. Franzusoff A. Sarnow P. Cap-dependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae Mol. Cell. Biol. 1994 14 7322 7330 10.1128/MCB.14.11.7322 7935446 PMC359267 · DOI
  11. [11]Tarun S.Z. Jr. Sachs A.B. A common function for mRNA 5′ and 3′ ends in translation initiation in yeast Genes Dev. 1995 9 2997 3007 10.1101/gad.9.23.2997 7498795 · DOI
  12. [12]Tarun S.Z. Jr. Sachs A.B. Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G EMBO J. 1996 15 7168 7177 10.1002/j.1460-2075.1996.tb01108.x 9003792 PMC452544 · DOI
  13. [13]Wells S.E. Hillner P.E. Vale R.D. Sachs A.B. Circularization of mRNA by eukaryotic translation initiation factors Mol. Cell 1998 2 135 140 10.1016/S1097-2765(00)80122-7 9702200 · DOI
  14. [14]Le H. Tanguay R.L. Balasta M.L. Wei C.C. Browning K.S. Metz A.M. Goss D.J. Gallie D.R. Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity J. Biol. Chem. 1997 272 16247 16255 10.1074/jbc.272.26.16247 9195926 · DOI
  15. [15]Imataka H. Gradi A. Sonenberg N. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation EMBO J. 1998 17 7480 7489 10.1093/emboj/17.24.7480 9857202 PMC1171091 · DOI · Paper page
  16. [16]Archer S.K. Shirokikh N.E. Hallwirth C.V. Beilharz T.H. Preiss T. Probing the closed-loop model of mRNA translation in living cells RNA Biol. 2015 12 248 254 10.1080/15476286.2015.1017242 25826658 PMC4615164 · DOI
  17. [17]Thompson M.K. Rojas-Duran M.F. Gangaramani P. Gilbert W.V. The ribosomal protein Asc1/RACK1 is required for efficient translation of short mRNAs eLife 2016 5 e11154 10.7554/eLife.11154 27117520 PMC4848094 · DOI
  18. [18]Afonina Z.A. Myasnikov A.G. Shirokov V.A. Klaholz B.P. Spirin A.S. Formation of circular polyribosomes on eukaryotic mRNA without cap-structure and poly(A)-tail: A cryo electron tomography study Nucleic Acids Res. 2014 42 9461 9469 10.1093/nar/gku599 25016525 PMC4132722 · DOI
  19. [19]Neusiedler J. Mocquet V. Limousin T. Ohlmann T. Morris C. Jalinot P. INT6 interacts with MIF4GD/SLIP1 and is necessary for efficient histone mRNA translation RNA 2012 18 1163 1177 10.1261/rna.032631.112 22532700 PMC3358639 · DOI
  20. [20]von Moeller H. Lerner R. Ricciardi A. Basquin C. Marzluff W.F. Conti E. Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins Nucleic Acids Res. 2013 41 7960 7971 10.1093/nar/gkt558 23804756 PMC3763545 · DOI
  21. [21]Vende P. Piron M. Castagne N. Poncet D. Efficient translation of rotavirus mRNA requires simultaneous interaction of NSP3 with the eukaryotic translation initiation factor eIF4G and the mRNA 3′ end J. Virol. 2000 74 7064 7071 10.1128/JVI.74.15.7064-7071.2000 10888646 PMC112224 · DOI
  22. [22]Groft C.M. Burley S.K. Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization Mol. Cell 2002 9 1273 1283 10.1016/S1097-2765(02)00555-5 12086624 · DOI
  23. [23]Gratia M. Sarot E. Vende P. Charpilienne A. Baron C.H. Duarte M. Pyronnet S. Poncet D. Rotavirus NSP3 Is a Translational Surrogate of the Poly(A) Binding Protein-Poly(A) Complex J. Virol. 2015 89 8773 8782 10.1128/JVI.01402-15 26063427 PMC4524085 · DOI
  24. [24]Bergamini G. Preiss T. Hentze M.W. Picornavirus IRESes and the poly(A) tail jointly promote cap-independent translation in a mammalian cell-free system RNA 2000 6 1781 1790 10.1017/S1355838200001679 11142378 PMC1370048 · DOI
  25. [25]Michel Y.M. Borman A.M. Paulous S. Kean K.M. Eukaryotic initiation factor 4G-poly(A) binding protein interaction is required for poly(A) tail-mediated stimulation of picornavirus internal ribosome entry segment-driven translation but not for X-mediated stimulation of hepatitis C virus translation Mol. Cell. Biol. 2001 21 4097 4109 10.1128/MCB.21.13.4097-4109.2001 11390639 PMC87071 · DOI
  26. [26]Svitkin Y.V. Imataka H. Khaleghpour K. Kahvejian A. Liebig H.D. Sonenberg N. Poly(A)-binding protein interaction with elF4G stimulates picornavirus IRES-dependent translation RNA 2001 7 1743 1752 11780631 PMC1370214
  27. [27]Ito T. Lai M.M. An internal polypyrimidine-tract-binding protein-binding site in the hepatitis C virus RNA attenuates translation, which is relieved by the 3′-untranslated sequence Virology 1999 254 288 296 10.1006/viro.1998.9541 9986795 · DOI
  28. [28]Choe J. Lin S. Zhang W. Liu Q. Wang L. Ramirez-Moya J. Du P. Kim W. Tang S. Sliz P. mRNA circularization by METTL3-eIF3h enhances translation and promotes oncogenesis Nature 2018 561 556 560 10.1038/s41586-018-0538-8 30232453 PMC6234840 · DOI
  29. [29]Wang X. Zhao B.S. Roundtree I.A. Lu Z. Han D. Ma H. Weng X. Chen K. Shi H. He C. N(6)-methyladenosine Modulates Messenger RNA Translation Efficiency Cell 2015 161 1388 1399 10.1016/j.cell.2015.05.014 26046440 PMC4825696 · DOI · Paper page
  30. [30]Thompson M.K. Gilbert W.V. mRNA length-sensing in eukaryotic translation: Reconsidering the “closed loop” and its implications for translational control Curr. Genet. 2017 63 613 620 10.1007/s00294-016-0674-3 28028558 PMC5484751 · DOI
  31. [31]Fakim H. Fabian M.R. Communication Is Key: 5′-3′ Interactions that Regulate mRNA Translation and Turnover Adv. Exp. Med. Biol. 2019 1203 149 164 31811634
  32. [32]Vicens Q. Kieft J.S. Rissland O.S. Revisiting the Closed-Loop Model and the Nature of mRNA 5′-3′ Communication Mol. Cell 2018 72 805 812 10.1016/j.molcel.2018.10.047 30526871 PMC6294470 · DOI
  33. [33]Pelletier J. Sonenberg N. The Organizing Principles of Eukaryotic Ribosome Recruitment Annu. Rev. BioChem. 2019 88 307 335 10.1146/annurev-biochem-013118-111042 31220979 · DOI
  34. [34]Madin K. Sawasaki T. Kamura N. Takai K. Ogasawara T. Yazaki K. Takei T. Miura K. Endo Y. Formation of circular polyribosomes in wheat germ cell-free protein synthesis system FEBS Lett. 2004 562 155 159 10.1016/S0014-5793(04)00221-2 15044017 · DOI
  35. [35]Mayr C. Regulation by 3′-Untranslated Regions Annu. Rev. Genet. 2017 51 171 194 10.1146/annurev-genet-120116-024704 28853924 · DOI · Paper page
  36. [36]Rogers D.W. Bottcher M.A. Traulsen A. Greig D. Ribosome reinitiation can explain length-dependent translation of messenger RNA PLoS Comput. Biol. 2017 13 e1005592 10.1371/journal.pcbi.1005592 28598992 PMC5482490 · DOI
  37. [37]Marshall E. Stansfield I. Romano M.C. Ribosome recycling induces optimal translation rate at low ribosomal availability J. R. Soc. Interface 2014 11 20140589 10.1098/rsif.2014.0589 25008084 PMC4233708 · DOI
  38. [38]Kolb V.A. Makeyev E.V. Spirin A.S. Folding of firefly luciferase during translation in a cell-free system EMBO J. 1994 13 3631 3637 10.1002/j.1460-2075.1994.tb06670.x 8062837 PMC395268 · DOI
  39. [39]Alekhina O.M. Vassilenko K.S. Spirin A.S. Translation of non-capped mRNAs in a eukaryotic cell-free system: Acceleration of initiation rate in the course of polysome formation Nucleic Acids Res. 2007 35 6547 6559 10.1093/nar/gkm725 17897963 PMC2095793 · DOI
  40. [40]Vassilenko K.S. Alekhina O.M. Dmitriev S.E. Shatsky I.N. Spirin A.S. Unidirectional constant rate motion of the ribosomal scanning particle during eukaryotic translation initiation Nucleic Acids Res. 2011 39 5555 5567 10.1093/nar/gkr147 21415006 PMC3141257 · DOI
  41. [41]Andreev D.E. Dmitriev S.E. Terenin I.M. Prassolov V.S. Merrick W.C. Shatsky I.N. Differential contribution of the m7G-cap to the 5′ end-dependent translation initiation of mammalian mRNAs Nucleic Acids Res. 2009 37 6135 6147 10.1093/nar/gkp665 19696074 PMC2764426 · DOI
  42. [42]Dmitriev S.E. Andreev D.E. Adyanova Z.V. Terenin I.M. Shatsky I.N. Efficient cap-dependent translation of mammalian mRNAs with long and highly structured 5′-untranslated regions in vitro and in vivo Mol. Biol. (Mosk.) 2009 43 108 113 10.1134/S0026893309010154 19334534 · DOI
  43. [43]Shatsky I.N. Dmitriev S.E. Andreev D.E. Terenin I.M. Transcriptome-wide studies uncover the diversity of modes of mRNA recruitment to eukaryotic ribosomes Crit. Rev. BioChem. Mol. Biol. 2014 49 164 177 10.3109/10409238.2014.887051 24520918 · DOI
  44. [44]Shatsky I.N. Dmitriev S.E. Terenin I.M. Andreev D.E. Cap- and IRES-independent scanning mechanism of translation initiation as an alternative to the concept of cellular IRESs Mol. Cells 2010 30 285 293 10.1007/s10059-010-0149-1 21052925 · DOI
  45. [45]Terenin I.M. Smirnova V.V. Andreev D.E. Dmitriev S.E. Shatsky I.N. A researcher’s guide to the galaxy of IRESs Cell. Mol. Life Sci. CMLS 2017 74 1431 1455 10.1007/s00018-016-2409-5 27853833 PMC11107752 · DOI
  46. [46]Pisarev A.V. Chard L.S. Kaku Y. Johns H.L. Shatsky I.N. Belsham G.J. Functional and structural similarities between the internal ribosome entry sites of hepatitis C virus and porcine teschovirus, a picornavirus J. Virol. 2004 78 4487 4497 10.1128/JVI.78.9.4487-4497.2004 15078929 PMC387690 · DOI
  47. [47]Wilson J.E. Pestova T.V. Hellen C.U. Sarnow P. Initiation of protein synthesis from the A site of the ribosome Cell 2000 102 511 520 10.1016/S0092-8674(00)00055-6 10966112 · DOI
  48. [48]Sorensen M.A. Pedersen S. Determination of the peptide elongation rate in vivo Methods Mol. Biol. 1998 77 129 142 9770666
  49. [49]Dmitriev S.E. Andreev D.E. Terenin I.M. Olovnikov I.A. Prassolov V.S. Merrick W.C. Shatsky I.N. Efficient translation initiation directed by the 900-nucleotide-long and GC-rich 5′ untranslated region of the human retrotransposon LINE-1 mRNA is strictly cap dependent rather than internal ribosome entry site mediated Mol. Cell. Biol. 2007 27 4685 4697 10.1128/MCB.02138-06 17470553 PMC1951496 · DOI
  50. [50]Leppek K. Das R. Barna M. Functional 5′ UTR mRNA structures in eukaryotic translation regulation and how to find them Nat. Rev. Mol. Cell Biol. 2018 19 158 174 10.1038/nrm.2017.103 29165424 PMC5820134 · DOI · Paper page
  51. [51]Akulich K.A. Andreev D.E. Terenin I.M. Smirnova V.V. Anisimova A.S. Makeeva D.S. Arkhipova V.I. Stolboushkina E.A. Garber M.B. Prokofjeva M.M. Four translation initiation pathways employed by the leaderless mRNA in eukaryotes Sci. Rep. 2016 6 37905 10.1038/srep37905 27892500 PMC5124965 · DOI
  52. [52]Tian B. Hu J. Zhang H. Lutz C.S. A large-scale analysis of mRNA polyadenylation of human and mouse genes Nucleic Acids Res. 2005 33 201 212 10.1093/nar/gki158 15647503 PMC546146 · DOI
  53. [53]Nicholson A.L. Pasquinelli A.E. Tales of Detailed Poly(A) Tails Trends Cell Biol. 2019 29 191 200 10.1016/j.tcb.2018.11.002 30503240 PMC7083203 · DOI · Paper page
  54. [54]Weill L. Belloc E. Bava F.A. Mendez R. Translational control by changes in poly(A) tail length: Recycling mRNAs Nat. Struct. Mol. Biol. 2012 19 577 585 10.1038/nsmb.2311 22664985 · DOI · Paper page
  55. [55]Svitkin Y.V. Sonenberg N. An efficient system for cap- and poly(A)-dependent translation in vitro Methods Mol. Biol. 2004 257 155 170 14770004
  56. [56]Eliseeva I.A. Lyabin D.N. Ovchinnikov L.P. Poly(A)-binding proteins: Structure, domain organization, and activity regulation Biochem. Biokhimiia 2013 78 1377 1391 10.1134/S0006297913130014 24490729 · DOI
  57. [57]Pause A. Methot N. Svitkin Y. Merrick W.C. Sonenberg N. Dominant negative mutants of mammalian translation initiation factor eIF-4A define a critical role for eIF-4F in cap-dependent and cap-independent initiation of translation EMBO J. 1994 13 1205 1215 10.1002/j.1460-2075.1994.tb06370.x 8131750 PMC394930 · DOI
  58. [58]Pause A. Methot N. Sonenberg N. The HRIGRXXR region of the DEAD box RNA helicase eukaryotic translation initiation factor 4A is required for RNA binding and ATP hydrolysis Mol. Cell. Biol. 1993 13 6789 6798 10.1128/MCB.13.11.6789 8413273 PMC364741 · DOI
  59. [59]Pestova T.V. Kolupaeva V.G. The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection Genes Dev. 2002 16 2906 2922 10.1101/gad.1020902 12435632 PMC187480 · DOI
  60. [60]Villalba A. Coll O. Gebauer F. Cytoplasmic polyadenylation and translational control Curr. Opin. Genet. Dev. 2011 21 452 457 10.1016/j.gde.2011.04.006 21536428 · DOI
  61. [61]Machida K. Shigeta T. Yamamoto Y. Ito T. Svitkin Y. Sonenberg N. Imataka H. Dynamic interaction of poly(A)-binding protein with the ribosome Sci. Rep. 2018 8 17435 10.1038/s41598-018-35753-1 30487538 PMC6261967 · DOI
  62. [62]Kahvejian A. Svitkin Y.V. Sukarieh R. M’Boutchou M.N. Sonenberg N. Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms Genes Dev. 2005 19 104 113 10.1101/gad.1262905 15630022 PMC540229 · DOI · Paper page
  63. [63]Borman A.M. Michel Y.M. Kean K.M. Biochemical characterisation of cap-poly(A) synergy in rabbit reticulocyte lysates: The eIF4G-PABP interaction increases the functional affinity of eIF4E for the capped mRNA 5′-end Nucleic Acids Res. 2000 28 4068 4075 10.1093/nar/28.21.4068 11058101 PMC113128 · DOI
  64. [64]Bushell M. Wood W. Carpenter G. Pain V.M. Morley S.J. Clemens M.J. Disruption of the interaction of mammalian protein synthesis eukaryotic initiation factor 4B with the poly(A)-binding protein by caspase- and viral protease-mediated cleavages J. Biol. Chem. 2001 276 23922 23928 10.1074/jbc.M100384200 11274152 · DOI
  65. [65]Wei C.C. Balasta M.L. Ren J. Goss D.J. Wheat germ poly(A) binding protein enhances the binding affinity of eukaryotic initiation factor 4F and (iso)4F for cap analogues Biochemistry 1998 37 1910 1916 10.1021/bi9724570 9485317 · DOI
  66. [66]Bi X. Goss D.J. Wheat germ poly(A)-binding protein increases the ATPase and the RNA helicase activity of translation initiation factors eIF4A, eIF4B, and eIF-iso4F J. Biol. Chem. 2000 275 17740 17746 10.1074/jbc.M909464199 10748132 · DOI
  67. [67]Searfoss A. Dever T.E. Wickner R. Linking the 3′ poly(A) tail to the subunit joining step of translation initiation: Relations of Pab1p, eukaryotic translation initiation factor 5b (Fun12p), and Ski2p-Slh1p Mol. Cell. Biol. 2001 21 4900 4908 10.1128/MCB.21.15.4900-4908.2001 11438647 PMC87206 · DOI
  68. [68]Filbin M.E. Kieft J.S. Linking Alpha to Omega: Diverse and dynamic RNA-based mechanisms to regulate gene expression by 5′-to-3′ communication F1000Research 2016 5 4995689 10.12688/f1000research.7913.1 PMC4995689 27610229 · DOI
  69. [69]Adivarahan S. Livingston N. Nicholson B. Rahman S. Wu B. Rissland O.S. Zenklusen D. Spatial Organization of Single mRNPs at Different Stages of the Gene Expression Pathway Mol. Cell 2018 72 727 738.e5 10.1016/j.molcel.2018.10.010 30415950 PMC6592633 · DOI
  70. [70]Khong A. Parker R. mRNP architecture in translating and stress conditions reveals an ordered pathway of mRNP compaction J. Cell Biol. 2018 217 4124 4140 10.1083/jcb.201806183 30322972 PMC6279387 · DOI
  71. [71]Metkar M. Ozadam H. Lajoie B.R. Imakaev M. Mirny L.A. Dekker J. Moore M.J. Higher-Order Organization Principles of Pre-translational mRNPs Mol. Cell 2018 72 715 726.e3 10.1016/j.molcel.2018.09.012 30415953 PMC6239896 · DOI
  72. [72]Kopeina G.S. Afonina Z.A. Gromova K.V. Shirokov V.A. Vasiliev V.D. Spirin A.S. Step-wise formation of eukaryotic double-row polyribosomes and circular translation of polysomal mRNA Nucleic Acids Res. 2008 36 2476 2488 10.1093/nar/gkm1177 18310103 PMC2377419 · DOI
  73. [73]Afonina Z.A. Myasnikov A.G. Shirokov V.A. Klaholz B.P. Spirin A.S. Conformation transitions of eukaryotic polyribosomes during multi-round translation Nucleic Acids Res. 2015 43 618 628 10.1093/nar/gku1270 25520190 PMC4288168 · DOI
  74. [74]Pierron G. Weil D. Re-viewing the 3D Organization of mRNPs Mol. Cell 2018 72 603 605 10.1016/j.molcel.2018.10.044 30444995 · DOI
  75. [75]Lai W.C. Kayedkhordeh M. Cornell E.V. Farah E. Bellaousov S. Rietmeijer R. Salsi E. Mathews D.H. Ermolenko D.N. mRNAs and lncRNAs intrinsically form secondary structures with short end-to-end distances Nat. Commun. 2018 9 4328 10.1038/s41467-018-06792-z 30337527 PMC6193969 · DOI
  76. [76]Hoshino S. Imai M. Kobayashi T. Uchida N. Katada T. The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein J. Biol. Chem. 1999 274 16677 16680 10.1074/jbc.274.24.16677 10358005 · DOI
  77. [77]Pestova T.V. Shatsky I.N. Fletcher S.P. Jackson R.J. Hellen C.U. A prokaryotic-like mode of cytoplasmic eukaryotic ribosome binding to the initiation codon during internal translation initiation of hepatitis C and classical swine fever virus RNAs Genes Dev. 1998 12 67 83 10.1101/gad.12.1.67 9420332 PMC316404 · DOI
  78. [78]Terenin I.M. Dmitriev S.E. Andreev D.E. Royall E. Belsham G.J. Roberts L.O. Shatsky I.N. A cross-kingdom internal ribosome entry site reveals a simplified mode of internal ribosome entry Mol. Cell. Biol. 2005 25 7879 7888 10.1128/MCB.25.17.7879-7888.2005 16107731 PMC1190281 · DOI
  79. [79]Agalarov S. Sakharov P.A. Fattakhova D. Sogorin E.A. Spirin A.S. Internal translation initiation and eIF4F/ATP-independent scanning of mRNA by eukaryotic ribosomal particles Sci. Rep. 2014 4 4438 10.1038/srep04438 24657959 PMC3963034 · DOI
  80. [80]Mancera-Martinez E. Brito Querido J. Valasek L.S. Simonetti A. Hashem Y. ABCE1: A special factor that orchestrates translation at the crossroad between recycling and initiation RNA Biol. 2017 14 1279 1285 10.1080/15476286.2016.1269993 28498001 PMC5711452 · DOI
  81. [81]Valasek L.S. Zeman J. Wagner S. Beznoskova P. Pavlikova Z. Mohammad M.P. Hronova V. Herrmannova A. Hashem Y. Gunisova S. Embraced by eIF3: Structural and functional insights into the roles of eIF3 across the translation cycle Nucleic Acids Res. 2017 45 10948 10968 10.1093/nar/gkx805 28981723 PMC5737393 · DOI
  82. [82]Ivanov A. Mikhailova T. Eliseev B. Yeramala L. Sokolova E. Susorov D. Shuvalov A. Schaffitzel C. Alkalaeva E. PABP enhances release factor recruitment and stop codon recognition during translation termination Nucleic Acids Res. 2016 44 7766 7776 10.1093/nar/gkw635 27418677 PMC5027505 · DOI
  83. [83]Schleich S. Strassburger K. Janiesch P.C. Koledachkina T. Miller K.K. Haneke K. Cheng Y.S. Kuechler K. Stoecklin G. Duncan K.E. DENR-MCT-1 promotes translation re-initiation downstream of uORFs to control tissue growth Nature 2014 512 208 212 10.1038/nature13401 25043021 PMC4134322 · DOI
  84. [84]Young D.J. Makeeva D.S. Zhang F. Anisimova A.S. Stolboushkina E.A. Ghobakhlou F. Shatsky I.N. Dmitriev S.E. Hinnebusch A.G. Guydosh N.R. Tma64/eIF2D, Tma20/MCT-1, and Tma22/DENR Recycle Post-termination 40S Subunits In Vivo Mol. Cell 2018 71 761 774.e5 10.1016/j.molcel.2018.07.028 30146315 PMC6225905 · DOI
  85. [85]Gao F. Alekhina O.M. Vassilenko K.S. Simon A.E. Unusual dicistronic expression from closely spaced initiation codons in an umbravirus subgenomic RNA Nucleic Acids Res. 2018 46 11726 11742 10.1093/nar/gky871 30272199 PMC6294492 · DOI
  86. [86]Meyer K.D. Patil D.P. Zhou J. Zinoviev A. Skabkin M.A. Elemento O. Pestova T.V. Qian S.B. Jaffrey S.R. 5′ UTR m(6)A Promotes Cap-Independent Translation Cell 2015 163 999 1010 10.1016/j.cell.2015.10.012 26593424 PMC4695625 · DOI
  87. [87]Yang Y. Fan X. Mao M. Song X. Wu P. Zhang Y. Jin Y. Yang Y. Chen L.L. Wang Y. Extensive translation of circular RNAs driven by N(6)-methyladenosine Cell Res. 2017 27 626 641 10.1038/cr.2017.31 28281539 PMC5520850 · DOI · Paper page
  88. [88]Rubtsova M.P. Sizova D.V. Dmitriev S.E. Ivanov D.S. Prassolov V.S. Shatsky I.N. Distinctive properties of the 5′-untranslated region of human hsp70 mRNA J. Biol. Chem. 2003 278 22350 22356 10.1074/jbc.M303213200 12682055 · DOI · Paper page
  89. [89]Prokhorova I.V. Akulich K.A. Makeeva D.S. Osterman I.A. Skvortsov D.A. Sergiev P.V. Dontsova O.A. Yusupova G. Yusupov M.M. Dmitriev S.E. Amicoumacin A induces cancer cell death by targeting the eukaryotic ribosome Sci. Rep. 2016 6 27720 10.1038/srep27720 27296282 PMC4906347 · DOI
  90. [90]Pokrovskaya I.D. Gurevich V.V. In vitro transcription: Preparative RNA yields in analytical scale reactions Anal. BioChem. 1994 220 420 423 10.1006/abio.1994.1360 7526740 · DOI

Cited by

Sorted by citations

Authors
Alekhina, O., Terenin, I., Dmitriev, S., & Vassilenko, K.
Affiliations
  • Russian Academy of Sciences (RU)
  • Sechenov University (RU)
  • Engelhardt Institute of Molecular Biology (RU)
Corresponding author
  • Dmitriev, Sergey
  • Vassilenko, Konstantin
ORCID
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2020-02-29
Volume
21
Issue
5
Pages
1677
ISSN
1422-0067 (ISSN-L)
DOI
10.3390/ijms21051677
PMC
PMC7084953
OpenAlex
W3010491315
Cited by
47
References
0
Citations by year
2026: 7 · 2025: 6 · 2024: 4 · 2023: 6 · 2022: 12 · 2021: 6 · 2020: 6
FWCI
2.40
Type
journal article
Language
en
Open access
Licence
Locations
  • International Journal of Molecular Sciences (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Russian Science Foundation (18-14-00291, 19-74-20186)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
Keywords
mRNA circularization, eIF4A, eIF4G, poly(A)-binding protein, poly(A) tail, translation initiation, 5' untranslated region, 3' untranslated region, eIF4E, ribosome recycling, luciferase reporter, eukaryotic translation
MeSH terms
Animals, Cell-Free System, Cyclization, Peptide Chain Initiation, Translational, Poly A, RNA Caps, RNA, Messenger, Protein Biosynthesis, 3' Untranslated Regions, Eukaryotic Initiation Factor-4E, Eukaryotic Initiation Factor-4G, Mice

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