메뉴 건너뛰기




Volumn 19, Issue 3, 2009, Pages 267-276

Toward a structural understanding of IRES RNA function

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; SINGLE STRANDED RNA; TRANSFER RNA; VIRUS RNA;

EID: 66849089596     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2009.03.005     Document Type: Review
Times cited : (155)

References (78)
  • 1
    • 33846991130 scopus 로고    scopus 로고
    • The mechanism of translation initiation in eukaryotes
    • Mathews M.B., Sonenberg N., and Hershey J.W.B. (Eds), Cold Sring Harbor Laboratory Press
    • Pestova T., Lorsch J.R., and Hellen C.U. The mechanism of translation initiation in eukaryotes. In: Mathews M.B., Sonenberg N., and Hershey J.W.B. (Eds). Translational Control in Biology and Medicine (2007), Cold Sring Harbor Laboratory Press 87-128
    • (2007) Translational Control in Biology and Medicine , pp. 87-128
    • Pestova, T.1    Lorsch, J.R.2    Hellen, C.U.3
  • 2
    • 36749042932 scopus 로고    scopus 로고
    • Translation initiation by viral internal ribosome entry sites
    • Mathews M.B., Sonenberg N., and Hershey J.W.B. (Eds), Cold Spring Harbor Laboratory Press
    • Doudna J.A., and Sarnow P. Translation initiation by viral internal ribosome entry sites. In: Mathews M.B., Sonenberg N., and Hershey J.W.B. (Eds). Translational Control in Biology and Medicine (2007), Cold Spring Harbor Laboratory Press 129-153
    • (2007) Translational Control in Biology and Medicine , pp. 129-153
    • Doudna, J.A.1    Sarnow, P.2
  • 3
    • 33846951996 scopus 로고    scopus 로고
    • Translation initiation via cellular internal ribosome entry sites
    • Mathews M.B., Sonenberg N., and Hershey J. (Eds), Cold Spring Harbor Laboratroy Press
    • Elroy-Stein O., and Merrick W.C. Translation initiation via cellular internal ribosome entry sites. In: Mathews M.B., Sonenberg N., and Hershey J. (Eds). Translational Control in Biology and Medicine (2007), Cold Spring Harbor Laboratroy Press 155-172
    • (2007) Translational Control in Biology and Medicine , pp. 155-172
    • Elroy-Stein, O.1    Merrick, W.C.2
  • 4
    • 28844476749 scopus 로고    scopus 로고
    • Alternative mechanisms of initiating translation of mammalian mRNAs
    • This review presents an accessible introduction to both cap-dependent and cap-independent translation initiation in eukaryotes, to include the molecules involved (what do you mean by this?) and a brief history of the field.
    • Jackson R.J. Alternative mechanisms of initiating translation of mammalian mRNAs. Biochem Soc Trans 33 (2005) 1231-1241. This review presents an accessible introduction to both cap-dependent and cap-independent translation initiation in eukaryotes, to include the molecules involved (what do you mean by this?) and a brief history of the field.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1231-1241
    • Jackson, R.J.1
  • 5
    • 33749259053 scopus 로고    scopus 로고
    • Searching for IRES
    • This comprehensive review examines what is known about cellular IRES structures as well as a critical evaluation of the tools that are used to examine these structures and perhaps predict the presence of an IRES based sequence information alone.
    • Baird S.D., Turcotte M., Korneluk R.G., and Holcik M. Searching for IRES. RNA 12 (2006) 1755-1785. This comprehensive review examines what is known about cellular IRES structures as well as a critical evaluation of the tools that are used to examine these structures and perhaps predict the presence of an IRES based sequence information alone.
    • (2006) RNA , vol.12 , pp. 1755-1785
    • Baird, S.D.1    Turcotte, M.2    Korneluk, R.G.3    Holcik, M.4
  • 6
    • 33646791554 scopus 로고    scopus 로고
    • Divergent IRES elements in invertebrates
    • Jan E. Divergent IRES elements in invertebrates. Virus Res 119 (2006) 16-28
    • (2006) Virus Res , vol.119 , pp. 16-28
    • Jan, E.1
  • 7
    • 0037369073 scopus 로고    scopus 로고
    • Viral internal ribosome entry site elements: novel ribosome-RNA complexes and roles in viral pathogenesis
    • Sarnow P. Viral internal ribosome entry site elements: novel ribosome-RNA complexes and roles in viral pathogenesis. J Virol 77 (2003) 2801-2806
    • (2003) J Virol , vol.77 , pp. 2801-2806
    • Sarnow, P.1
  • 8
    • 45749118708 scopus 로고    scopus 로고
    • In vitro expression of the HIV-2 genomic RNA is controlled by three distinct internal ribosome entry segments that are regulated by the HIV protease and the Gag polyprotein
    • Ricci E.P., Herbreteau C.H., Decimo D., Schaupp A., Datta S.A., Rein A., Darlix J.L., and Ohlmann T. In vitro expression of the HIV-2 genomic RNA is controlled by three distinct internal ribosome entry segments that are regulated by the HIV protease and the Gag polyprotein. RNA 14 (2008) 1443-1455
    • (2008) RNA , vol.14 , pp. 1443-1455
    • Ricci, E.P.1    Herbreteau, C.H.2    Decimo, D.3    Schaupp, A.4    Datta, S.A.5    Rein, A.6    Darlix, J.L.7    Ohlmann, T.8
  • 10
    • 13944276301 scopus 로고    scopus 로고
    • A preformed compact ribosome-binding domain in the cricket paralysis-like virus IRES RNAs
    • Costantino D., and Kieft J.S. A preformed compact ribosome-binding domain in the cricket paralysis-like virus IRES RNAs. RNA 11 (2005) 332-343
    • (2005) RNA , vol.11 , pp. 332-343
    • Costantino, D.1    Kieft, J.S.2
  • 11
    • 33845335508 scopus 로고    scopus 로고
    • Structural basis for ribosome recruitment and manipulation by a viral IRES RNA
    • This study presents the X-ray crystal structure of the ribosome binding domain of a member of the Dicistroviridae IGR IRES, revealing how it folds to create a recognition surface for the 40S subunit.
    • Pfingsten J.S., Costantino D.A., and Kieft J.S. Structural basis for ribosome recruitment and manipulation by a viral IRES RNA. Science 314 (2006) 1450-1454. This study presents the X-ray crystal structure of the ribosome binding domain of a member of the Dicistroviridae IGR IRES, revealing how it folds to create a recognition surface for the 40S subunit.
    • (2006) Science , vol.314 , pp. 1450-1454
    • Pfingsten, J.S.1    Costantino, D.A.2    Kieft, J.S.3
  • 12
    • 37849021316 scopus 로고    scopus 로고
    • tRNA-mRNA mimicry drives translation initiation from a viral IRES
    • This study presents the X-ray crystal structure of the 40S P-site occupying domain of a Dicistroviridae IGR IRES, suggesting a way in which the IRES uses precise (tRNA?) molecular mimicry to manipulate the ribosome.
    • Costantino D.A., Pfingsten J.S., Rambo R.P., and Kieft J.S. tRNA-mRNA mimicry drives translation initiation from a viral IRES. Nat Struct Mol Biol 15 (2008) 57-64. This study presents the X-ray crystal structure of the 40S P-site occupying domain of a Dicistroviridae IGR IRES, suggesting a way in which the IRES uses precise (tRNA?) molecular mimicry to manipulate the ribosome.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 57-64
    • Costantino, D.A.1    Pfingsten, J.S.2    Rambo, R.P.3    Kieft, J.S.4
  • 13
    • 4644247805 scopus 로고    scopus 로고
    • Cryo-EM visualization of a viral internal ribosome entry site bound to human ribosomes: the IRES functions as an RNA-based translation factor
    • This paper reports the cryo-EM structure of a complete IGR IRES RNA bound to the ribosome over the decoding groove. It shows that the IRES forms a compact structure on the ribosome, suggesting what elements of the ribosome interact with the IRES, and reveals that both the IRES and ribosome undergo conformational changes as a result of this interaction.
    • Spahn C.M., Jan E., Mulder A., Grassucci R.A., Sarnow P., and Frank J. Cryo-EM visualization of a viral internal ribosome entry site bound to human ribosomes: the IRES functions as an RNA-based translation factor. Cell 118 (2004) 465-475. This paper reports the cryo-EM structure of a complete IGR IRES RNA bound to the ribosome over the decoding groove. It shows that the IRES forms a compact structure on the ribosome, suggesting what elements of the ribosome interact with the IRES, and reveals that both the IRES and ribosome undergo conformational changes as a result of this interaction.
    • (2004) Cell , vol.118 , pp. 465-475
    • Spahn, C.M.1    Jan, E.2    Mulder, A.3    Grassucci, R.A.4    Sarnow, P.5    Frank, J.6
  • 15
    • 0037073485 scopus 로고    scopus 로고
    • Factorless ribosome assembly on the internal ribosome entry site of cricket paralysis virus
    • This study explores the structural elements used by the Dicistroviridae IGR IRES RNA to contact the ribosome, and how they might all work together to drive function of this RNA. It presents data critical for interpreting IRES RNA structure that came later.
    • Jan E., and Sarnow P. Factorless ribosome assembly on the internal ribosome entry site of cricket paralysis virus. J Mol Biol 324 (2002) 889-902. This study explores the structural elements used by the Dicistroviridae IGR IRES RNA to contact the ribosome, and how they might all work together to drive function of this RNA. It presents data critical for interpreting IRES RNA structure that came later.
    • (2002) J Mol Biol , vol.324 , pp. 889-902
    • Jan, E.1    Sarnow, P.2
  • 16
    • 34250223454 scopus 로고    scopus 로고
    • Conservation and diversity among the three-dimensional folds of the Dicistroviridae intergenic region IRESes
    • Pfingsten J.S., Costantino D.A., and Kieft J.S. Conservation and diversity among the three-dimensional folds of the Dicistroviridae intergenic region IRESes. J Mol Biol 370 (2007) 856-869
    • (2007) J Mol Biol , vol.370 , pp. 856-869
    • Pfingsten, J.S.1    Costantino, D.A.2    Kieft, J.S.3
  • 17
    • 0038750886 scopus 로고    scopus 로고
    • Structural elements in the internal ribosome entry site of Plautia stali intestine virus responsible for binding with ribosomes
    • As in reference 15, this study explores the ribosome-binding ability of a Dicistroviridae IGR IRES, closely relating the structure to function and providing models that were later proved accurate by subsequent X-ray structures.
    • Nishiyama T., Yamamoto H., Shibuya N., Hatakeyama Y., Hachimori A., Uchiumi T., and Nakashima N. Structural elements in the internal ribosome entry site of Plautia stali intestine virus responsible for binding with ribosomes. Nucleic Acids Res 31 (2003) 2434-2442. As in reference 15, this study explores the ribosome-binding ability of a Dicistroviridae IGR IRES, closely relating the structure to function and providing models that were later proved accurate by subsequent X-ray structures.
    • (2003) Nucleic Acids Res , vol.31 , pp. 2434-2442
    • Nishiyama, T.1    Yamamoto, H.2    Shibuya, N.3    Hatakeyama, Y.4    Hachimori, A.5    Uchiumi, T.6    Nakashima, N.7
  • 18
    • 0034682720 scopus 로고    scopus 로고
    • Initiation of protein synthesis from the A site of the ribosome
    • Wilson J.E., Pestova T.V., Hellen C.U., and Sarnow P. Initiation of protein synthesis from the A site of the ribosome. Cell 102 (2000) 511-520
    • (2000) Cell , vol.102 , pp. 511-520
    • Wilson, J.E.1    Pestova, T.V.2    Hellen, C.U.3    Sarnow, P.4
  • 19
    • 45749123968 scopus 로고    scopus 로고
    • RNA structure-based ribosome recruitment: lessons from the Dicistroviridae intergenic region IRESes
    • Pfingsten J.S., and Kieft J.S. RNA structure-based ribosome recruitment: lessons from the Dicistroviridae intergenic region IRESes. RNA 14 (2008) 1255-1263
    • (2008) RNA , vol.14 , pp. 1255-1263
    • Pfingsten, J.S.1    Kieft, J.S.2
  • 20
    • 46549086974 scopus 로고    scopus 로고
    • Viral IRES RNA structures and ribosome interactions
    • This review focuses on how the structures of various viral IRES RNAs influence their ability to interact directly with the ribosome, what those interactions are, and what they might mean in terms of function.
    • Kieft J.S. Viral IRES RNA structures and ribosome interactions. Trends Biochem Sci 33 (2008) 274-283. This review focuses on how the structures of various viral IRES RNAs influence their ability to interact directly with the ribosome, what those interactions are, and what they might mean in terms of function.
    • (2008) Trends Biochem Sci , vol.33 , pp. 274-283
    • Kieft, J.S.1
  • 21
    • 34247185278 scopus 로고    scopus 로고
    • Binding mode of the first aminoacyl-tRNA in translation initiation mediated by Plautia stali intestine virus IRES
    • Yamamoto H., Nakashima N., Ikeda Y., and Uchiumi T. Binding mode of the first aminoacyl-tRNA in translation initiation mediated by Plautia stali intestine virus IRES. J Biol Chem 282 (2007) 7770-7776
    • (2007) J Biol Chem , vol.282 , pp. 7770-7776
    • Yamamoto, H.1    Nakashima, N.2    Ikeda, Y.3    Uchiumi, T.4
  • 22
    • 0033600934 scopus 로고    scopus 로고
    • The hepatitis C virus internal ribosome entry site adopts an ion-dependent tertiary fold
    • Kieft J.S., Zhou K., Jubin R., Murray M.G., Lau J.Y., and Doudna J.A. The hepatitis C virus internal ribosome entry site adopts an ion-dependent tertiary fold. J Mol Biol 292 (1999) 513-529
    • (1999) J Mol Biol , vol.292 , pp. 513-529
    • Kieft, J.S.1    Zhou, K.2    Jubin, R.3    Murray, M.G.4    Lau, J.Y.5    Doudna, J.A.6
  • 23
    • 59749085225 scopus 로고    scopus 로고
    • Structure and function of HCV IRES domains
    • This recent review gives an interview of what is known about the structure of the HCV IRES and how that structure information helps explain function.
    • Lukavsky P.J. Structure and function of HCV IRES domains. Virus Res 139 (2009) 166-171. This recent review gives an interview of what is known about the structure of the HCV IRES and how that structure information helps explain function.
    • (2009) Virus Res , vol.139 , pp. 166-171
    • Lukavsky, P.J.1
  • 24
    • 33845623845 scopus 로고    scopus 로고
    • Structural and mechanistic insights into hepatitis C viral translation initiation
    • Fraser C.S., and Doudna J.A. Structural and mechanistic insights into hepatitis C viral translation initiation. Nat Rev Microbiol 5 (2007) 29-38
    • (2007) Nat Rev Microbiol , vol.5 , pp. 29-38
    • Fraser, C.S.1    Doudna, J.A.2
  • 25
    • 0033744387 scopus 로고    scopus 로고
    • A potential RNA drug target in the hepatitis C virus internal ribosomal entry site
    • Klinck R., Westhof E., Walker S., Afshar M., Collier A., and Aboul-Ela F. A potential RNA drug target in the hepatitis C virus internal ribosomal entry site. RNA 6 (2000) 1423-1431
    • (2000) RNA , vol.6 , pp. 1423-1431
    • Klinck, R.1    Westhof, E.2    Walker, S.3    Afshar, M.4    Collier, A.5    Aboul-Ela, F.6
  • 26
    • 0033673387 scopus 로고    scopus 로고
    • Structures of two RNA domains essential for hepatitis C virus internal ribosome entry site function
    • Lukavsky P.J., Otto G.A., Lancaster A.M., Sarnow P., and Puglisi J.D. Structures of two RNA domains essential for hepatitis C virus internal ribosome entry site function. Nat Struct Biol 7 (2000) 1105-1110
    • (2000) Nat Struct Biol , vol.7 , pp. 1105-1110
    • Lukavsky, P.J.1    Otto, G.A.2    Lancaster, A.M.3    Sarnow, P.4    Puglisi, J.D.5
  • 27
    • 0036237981 scopus 로고    scopus 로고
    • Crystal structure of an RNA tertiary domain essential to HCV IRES-mediated translation initiation
    • Kieft J.S., Zhou K., Grech A., Jubin R., and Doudna J.A. Crystal structure of an RNA tertiary domain essential to HCV IRES-mediated translation initiation. Nat Struct Biol 9 (2002) 370-374
    • (2002) Nat Struct Biol , vol.9 , pp. 370-374
    • Kieft, J.S.1    Zhou, K.2    Grech, A.3    Jubin, R.4    Doudna, J.A.5
  • 29
    • 0344628782 scopus 로고    scopus 로고
    • Structure of HCV IRES domain II determined by NMR
    • An NMR structure of a complete structural domain of the HCV IRES is revealed in this paper. This domain is critical for multiple aspects of IRES function, and was a large and challenging target for NMR structural studies.
    • Lukavsky P.J., Kim I., Otto G.A., and Puglisi J.D. Structure of HCV IRES domain II determined by NMR. Nat Struct Biol 10 (2003) 1033-1038. An NMR structure of a complete structural domain of the HCV IRES is revealed in this paper. This domain is critical for multiple aspects of IRES function, and was a large and challenging target for NMR structural studies.
    • (2003) Nat Struct Biol , vol.10 , pp. 1033-1038
    • Lukavsky, P.J.1    Kim, I.2    Otto, G.A.3    Puglisi, J.D.4
  • 30
    • 33846959081 scopus 로고    scopus 로고
    • HCV and CSFV IRES domain II mediate eIF2 release during 80S ribosome assembly
    • Locker N., Easton L.E., and Lukavsky P.J. HCV and CSFV IRES domain II mediate eIF2 release during 80S ribosome assembly. EMBO J 26 (2007) 795-805
    • (2007) EMBO J , vol.26 , pp. 795-805
    • Locker, N.1    Easton, L.E.2    Lukavsky, P.J.3
  • 31
    • 33846064685 scopus 로고    scopus 로고
    • Functional architecture of HCV IRES domain II stabilized by divalent metal ions in the crystal and in solution
    • Dibrov S.M., Johnston-Cox H., Weng Y.H., and Hermann T. Functional architecture of HCV IRES domain II stabilized by divalent metal ions in the crystal and in solution. Angew Chem Int Ed Engl 46 (2007) 226-229
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 226-229
    • Dibrov, S.M.1    Johnston-Cox, H.2    Weng, Y.H.3    Hermann, T.4
  • 32
    • 5144229241 scopus 로고    scopus 로고
    • Mutational and structural analysis of stem-loop IIIC of the hepatitis C virus and GB virus B internal ribosome entry sites
    • Rijnbrand R., Thiviyanathan V., Kaluarachchi K., Lemon S.M., and Gorenstein D.G. Mutational and structural analysis of stem-loop IIIC of the hepatitis C virus and GB virus B internal ribosome entry sites. J Mol Biol 343 (2004) 805-817
    • (2004) J Mol Biol , vol.343 , pp. 805-817
    • Rijnbrand, R.1    Thiviyanathan, V.2    Kaluarachchi, K.3    Lemon, S.M.4    Gorenstein, D.G.5
  • 33
    • 27644484907 scopus 로고    scopus 로고
    • Structure of the hepatitis C Virus IRES bound to the human 80S ribosome: remodeling of the HCV IRES
    • This paper reveals the cryo-EM structure of the HCV IRES bound to the 80S ribosome allowed comparison of the binding surfaces of the IRES on the full ribosome with the binding in the context of the 40S subunit alone.
    • Boehringer D., Thermann R., Ostareck-Lederer A., Lewis J.D., and Stark H. Structure of the hepatitis C Virus IRES bound to the human 80S ribosome: remodeling of the HCV IRES. Structure (Camb) 13 (2005) 1695-1706. This paper reveals the cryo-EM structure of the HCV IRES bound to the 80S ribosome allowed comparison of the binding surfaces of the IRES on the full ribosome with the binding in the context of the 40S subunit alone.
    • (2005) Structure (Camb) , vol.13 , pp. 1695-1706
    • Boehringer, D.1    Thermann, R.2    Ostareck-Lederer, A.3    Lewis, J.D.4    Stark, H.5
  • 34
    • 0035831269 scopus 로고    scopus 로고
    • Hepatitis C virus IRES RNA-induced changes in the conformation of the 40s ribosomal subunit
    • The first cryo-EM structure of an IRES bound to a ribosome subunit is reported in this paper and reveals the location of the HCV IRES on the 40S subunit and also the surprising result that the HCV IRES changes the structure of the the ribosome when it binds.
    • Spahn C.M., Kieft J.S., Grassucci R.A., Penczek P.A., Zhou K., Doudna J.A., and Frank J. Hepatitis C virus IRES RNA-induced changes in the conformation of the 40s ribosomal subunit. Science 291 (2001) 1959-1962. The first cryo-EM structure of an IRES bound to a ribosome subunit is reported in this paper and reveals the location of the HCV IRES on the 40S subunit and also the surprising result that the HCV IRES changes the structure of the the ribosome when it binds.
    • (2001) Science , vol.291 , pp. 1959-1962
    • Spahn, C.M.1    Kieft, J.S.2    Grassucci, R.A.3    Penczek, P.A.4    Zhou, K.5    Doudna, J.A.6    Frank, J.7
  • 35
    • 0031905698 scopus 로고    scopus 로고
    • 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
    • This classic paper identifies the minimal set of factors needed to position the ribosome on the HCV IRES, showing that direct IRES-40S binding occurs. It also reveals details of the binding interaction that has guided many subsequent studies.
    • Pestova T.V., Shatsky I.N., Fletcher S.P., Jackson R.J., and Hellen C.U.T. 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 12 (1998) 67-83. This classic paper identifies the minimal set of factors needed to position the ribosome on the HCV IRES, showing that direct IRES-40S binding occurs. It also reveals details of the binding interaction that has guided many subsequent studies.
    • (1998) Genes Dev , vol.12 , pp. 67-83
    • Pestova, T.V.1    Shatsky, I.N.2    Fletcher, S.P.3    Jackson, R.J.4    Hellen, C.U.T.5
  • 36
    • 41949130892 scopus 로고    scopus 로고
    • eIF2-dependent and eIF2-independent modes of initiation on the CSFV IRES: a common role of domain II
    • Pestova T.V., de Breyne S., Pisarev A.V., Abaeva I.S., and Hellen C.U. eIF2-dependent and eIF2-independent modes of initiation on the CSFV IRES: a common role of domain II. EMBO J 27 (2008) 1060-1072
    • (2008) EMBO J , vol.27 , pp. 1060-1072
    • Pestova, T.V.1    de Breyne, S.2    Pisarev, A.V.3    Abaeva, I.S.4    Hellen, C.U.5
  • 37
    • 33646186734 scopus 로고    scopus 로고
    • Initiation factor-independent translation mediated by the hepatitis C virus internal ribosome entry site
    • Lancaster A.M., Jan E., and Sarnow P. Initiation factor-independent translation mediated by the hepatitis C virus internal ribosome entry site. RNA 12 (2006) 894-902
    • (2006) RNA , vol.12 , pp. 894-902
    • Lancaster, A.M.1    Jan, E.2    Sarnow, P.3
  • 38
    • 0034602386 scopus 로고    scopus 로고
    • Demonstration of functional requirement of polypyrimidine tract-binding protein by SELEX RNA during hepatitis C virus internal ribosome entry site-mediated translation initiation
    • Anwar A., Ali N., Tanveer R., and Siddiqui A. Demonstration of functional requirement of polypyrimidine tract-binding protein by SELEX RNA during hepatitis C virus internal ribosome entry site-mediated translation initiation. J Biol Chem 275 (2000) 34231-34235
    • (2000) J Biol Chem , vol.275 , pp. 34231-34235
    • Anwar, A.1    Ali, N.2    Tanveer, R.3    Siddiqui, A.4
  • 39
    • 7044269394 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein (PTB) inhibits hepatitis C virus internal ribosome entry site (HCV IRES)-mediated translation, but does not affect HCV replication
    • Tischendorf J.J., Beger C., Korf M., Manns M.P., and Kruger M. Polypyrimidine tract-binding protein (PTB) inhibits hepatitis C virus internal ribosome entry site (HCV IRES)-mediated translation, but does not affect HCV replication. Arch Virol 149 (2004) 1955-1970
    • (2004) Arch Virol , vol.149 , pp. 1955-1970
    • Tischendorf, J.J.1    Beger, C.2    Korf, M.3    Manns, M.P.4    Kruger, M.5
  • 40
    • 0029166747 scopus 로고
    • Interaction of polypyrimidine tract-binding protein with the 5′ noncoding region of the hepatitis C virus RNA genome and its functional requirement in internal initation of translation
    • Ali N., and Siddiqui A. Interaction of polypyrimidine tract-binding protein with the 5′ noncoding region of the hepatitis C virus RNA genome and its functional requirement in internal initation of translation. J Virol 69 (1995) 6367-6375
    • (1995) J Virol , vol.69 , pp. 6367-6375
    • Ali, N.1    Siddiqui, A.2
  • 41
    • 0034623002 scopus 로고    scopus 로고
    • Human La antigen is required for the hepatitis C virus internal ribosome entry site-mediated translation
    • Ali N., Pruijn G.J., Kenan D.J., Keene J.D., and Siddiqui A. Human La antigen is required for the hepatitis C virus internal ribosome entry site-mediated translation. J Biol Chem 275 (2000) 27531-27540
    • (2000) J Biol Chem , vol.275 , pp. 27531-27540
    • Ali, N.1    Pruijn, G.J.2    Kenan, D.J.3    Keene, J.D.4    Siddiqui, A.5
  • 42
    • 0031003235 scopus 로고    scopus 로고
    • The La antigen binds 5′ noncoding region of the hepatitis C virus RNA in the context of the initiator AUG codon and stimulates internal ribosome entry site-mediated translation
    • Ali N., and Siddiqui A. The La antigen binds 5′ noncoding region of the hepatitis C virus RNA in the context of the initiator AUG codon and stimulates internal ribosome entry site-mediated translation. Proc Natl Acad Sci U S A 94 (1997) 2249-2254
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2249-2254
    • Ali, N.1    Siddiqui, A.2
  • 43
    • 0038485613 scopus 로고    scopus 로고
    • Hepatitis C virus internal ribosome entry site-mediated translation is stimulated by specific interaction of independent regions of human La autoantigen
    • Pudi R., Abhiman S., Srinivasan N., and Das S. Hepatitis C virus internal ribosome entry site-mediated translation is stimulated by specific interaction of independent regions of human La autoantigen. J Biol Chem 278 (2003) 12231-12240
    • (2003) J Biol Chem , vol.278 , pp. 12231-12240
    • Pudi, R.1    Abhiman, S.2    Srinivasan, N.3    Das, S.4
  • 44
    • 3142757866 scopus 로고    scopus 로고
    • La protein binding at the GCAC site near the initiator AUG facilitates the ribosomal assembly on the hepatitis C virus RNA to influence internal ribosome entry site-mediated translation
    • Pudi R., Srinivasan P., and Das S. La protein binding at the GCAC site near the initiator AUG facilitates the ribosomal assembly on the hepatitis C virus RNA to influence internal ribosome entry site-mediated translation. J Biol Chem 279 (2004) 29879-29888
    • (2004) J Biol Chem , vol.279 , pp. 29879-29888
    • Pudi, R.1    Srinivasan, P.2    Das, S.3
  • 46
    • 47249142502 scopus 로고    scopus 로고
    • Comparative aspects on the role of polypyrimidine tract-binding protein in internal initiation of hepatitis C virus and picornavirus RNAs
    • Nishimura T., Saito M., Takano T., Nomoto A., Kohara M., and Tsukiyama-Kohara K. Comparative aspects on the role of polypyrimidine tract-binding protein in internal initiation of hepatitis C virus and picornavirus RNAs. Comp Immunol Microbiol Infect Dis 31 (2008) 435-448
    • (2008) Comp Immunol Microbiol Infect Dis , vol.31 , pp. 435-448
    • Nishimura, T.1    Saito, M.2    Takano, T.3    Nomoto, A.4    Kohara, M.5    Tsukiyama-Kohara, K.6
  • 47
    • 0034899176 scopus 로고    scopus 로고
    • The ribosome binding site of hepatitis C virus mRNA
    • Lytle J.R., Wu L., and Robertson H.D. The ribosome binding site of hepatitis C virus mRNA. J Virol 75 (2001) 7629-7636
    • (2001) J Virol , vol.75 , pp. 7629-7636
    • Lytle, J.R.1    Wu, L.2    Robertson, H.D.3
  • 48
    • 0036677165 scopus 로고    scopus 로고
    • Domains on the hepatitis C virus internal ribosome entry site for 40s subunit binding
    • Lytle J.R., Wu L., and Robertson H.D. Domains on the hepatitis C virus internal ribosome entry site for 40s subunit binding. RNA 8 (2002) 1045-1055
    • (2002) RNA , vol.8 , pp. 1045-1055
    • Lytle, J.R.1    Wu, L.2    Robertson, H.D.3
  • 49
    • 0033932448 scopus 로고    scopus 로고
    • An enzymatic footprinting analysis of the interaction of 40S ribosomal subunits with the internal ribosomal entry site of hepatitis C virus
    • Kolupaeva V.G., Pestova T.V., and Hellen C.U. An enzymatic footprinting analysis of the interaction of 40S ribosomal subunits with the internal ribosomal entry site of hepatitis C virus. J Virol 74 (2000) 6242-6250
    • (2000) J Virol , vol.74 , pp. 6242-6250
    • Kolupaeva, V.G.1    Pestova, T.V.2    Hellen, C.U.3
  • 50
    • 0036077344 scopus 로고    scopus 로고
    • Ribosomal proteins mediate the hepatitis C virus IRES-HeLa 40S interaction
    • Otto G.A., Lukavsky P.J., Lancaster A.M., Sarnow P., and Puglisi J.D. Ribosomal proteins mediate the hepatitis C virus IRES-HeLa 40S interaction. RNA 8 (2002) 913-923
    • (2002) RNA , vol.8 , pp. 913-923
    • Otto, G.A.1    Lukavsky, P.J.2    Lancaster, A.M.3    Sarnow, P.4    Puglisi, J.D.5
  • 51
    • 7044228006 scopus 로고    scopus 로고
    • The pathway of HCV IRES-mediated translation initiation
    • Using a biochemical approach, this paper explores the molecular steps used by the HCV IRES to position an 80S ribosome and relates those steps to specific sequences and structural domains.
    • Otto G.A., and Puglisi J.D. The pathway of HCV IRES-mediated translation initiation. Cell 119 (2004) 369-380. Using a biochemical approach, this paper explores the molecular steps used by the HCV IRES to position an 80S ribosome and relates those steps to specific sequences and structural domains.
    • (2004) Cell , vol.119 , pp. 369-380
    • Otto, G.A.1    Puglisi, J.D.2
  • 52
    • 10344243545 scopus 로고    scopus 로고
    • Coordinated assembly of human translation initiation complexes by the hepatitis C virus internal ribosome entry site RNA
    • Ji H., Fraser C.S., Yu Y., Leary J., and Doudna J.A. Coordinated assembly of human translation initiation complexes by the hepatitis C virus internal ribosome entry site RNA. Proc Natl Acad Sci U S A 101 (2004) 16990-16995
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 16990-16995
    • Ji, H.1    Fraser, C.S.2    Yu, Y.3    Leary, J.4    Doudna, J.A.5
  • 53
    • 28544439977 scopus 로고    scopus 로고
    • Structural roles for human translation factor eIF3 in initiation of protein synthesis
    • Siridechadilok B., Fraser C.S., Hall R.J., Doudna J.A., and Nogales E. Structural roles for human translation factor eIF3 in initiation of protein synthesis. Science 310 (2005) 1513-1515
    • (2005) Science , vol.310 , pp. 1513-1515
    • Siridechadilok, B.1    Fraser, C.S.2    Hall, R.J.3    Doudna, J.A.4    Nogales, E.5
  • 54
    • 42449114149 scopus 로고    scopus 로고
    • New insights into internal ribosome entry site elements relevant for viral gene expression
    • Martinez-Salas E., Pacheco A., Serrano P., and Fernandez N. New insights into internal ribosome entry site elements relevant for viral gene expression. J Gen Virol 89 (2008) 611-626
    • (2008) J Gen Virol , vol.89 , pp. 611-626
    • Martinez-Salas, E.1    Pacheco, A.2    Serrano, P.3    Fernandez, N.4
  • 55
    • 59749086877 scopus 로고    scopus 로고
    • Relevance of RNA structure for the activity of picornavirus IRES elements
    • This recent review provides a clear introduction to the structure-function relationship of the picornavirus IRES RNAs.
    • Fernandez-Miragall O., Quinto S.L., and Martinez-Salas E. Relevance of RNA structure for the activity of picornavirus IRES elements. Virus Res 139 (2009) 172-182. This recent review provides a clear introduction to the structure-function relationship of the picornavirus IRES RNAs.
    • (2009) Virus Res , vol.139 , pp. 172-182
    • Fernandez-Miragall, O.1    Quinto, S.L.2    Martinez-Salas, E.3
  • 56
    • 10644253021 scopus 로고    scopus 로고
    • Functional and structural similarities between the internal ribosome entry sites of hepatitis C virus and porcine teschovirus, a picornavirus
    • This paper shows that HCV-like IRESs can exist in picornavirus RNAs, illustrating that IRESs can be independent elements and that they likely have been "swapped" between viruses.
    • Pisarev A.V., Chard L.S., Kaku Y., Johns H.L., Shatsky I.N., and Belsham G.J. Functional and structural similarities between the internal ribosome entry sites of hepatitis C virus and porcine teschovirus, a picornavirus. J Virol 78 (2004) 4487-4497. This paper shows that HCV-like IRESs can exist in picornavirus RNAs, illustrating that IRESs can be independent elements and that they likely have been "swapped" between viruses.
    • (2004) J Virol , vol.78 , pp. 4487-4497
    • Pisarev, A.V.1    Chard, L.S.2    Kaku, Y.3    Johns, H.L.4    Shatsky, I.N.5    Belsham, G.J.6
  • 57
    • 31144437122 scopus 로고    scopus 로고
    • Functional analyses of RNA structures shared between the internal ribosome entry sites of hepatitis C virus and the picornavirus porcine teschovirus 1 Talfan
    • Chard L.S., Kaku Y., Jones B., Nayak A., and Belsham G.J. Functional analyses of RNA structures shared between the internal ribosome entry sites of hepatitis C virus and the picornavirus porcine teschovirus 1 Talfan. J Virol 80 (2006) 1271-1279
    • (2006) J Virol , vol.80 , pp. 1271-1279
    • Chard, L.S.1    Kaku, Y.2    Jones, B.3    Nayak, A.4    Belsham, G.J.5
  • 58
    • 59749095351 scopus 로고    scopus 로고
    • Divergent picornavirus IRES elements
    • An introductory review to picornavirus IRES elements that are HCV-like.
    • Belsham G.J. Divergent picornavirus IRES elements. Virus Res 139 (2009) 183-192. An introductory review to picornavirus IRES elements that are HCV-like.
    • (2009) Virus Res , vol.139 , pp. 183-192
    • Belsham, G.J.1
  • 59
    • 10744229009 scopus 로고    scopus 로고
    • Structural organization of a viral IRES depends on the integrity of the GNRA motif
    • Fernandez-Miragall O., and Martinez-Salas E. Structural organization of a viral IRES depends on the integrity of the GNRA motif. RNA 9 (2003) 1333-1344
    • (2003) RNA , vol.9 , pp. 1333-1344
    • Fernandez-Miragall, O.1    Martinez-Salas, E.2
  • 60
    • 31044449305 scopus 로고    scopus 로고
    • Evidence of reciprocal tertiary interactions between conserved motifs involved in organizing RNA structure essential for internal initiation of translation
    • Fernandez-Miragall O., Ramos R., Ramajo J., and Martinez-Salas E. Evidence of reciprocal tertiary interactions between conserved motifs involved in organizing RNA structure essential for internal initiation of translation. RNA 12 (2006) 223-234
    • (2006) RNA , vol.12 , pp. 223-234
    • Fernandez-Miragall, O.1    Ramos, R.2    Ramajo, J.3    Martinez-Salas, E.4
  • 61
    • 36248972579 scopus 로고    scopus 로고
    • In vivo footprint of a picornavirus internal ribosome entry site reveals differences in accessibility to specific RNA structural elements
    • This paper probes the structure of an IRES element within the cell, suggesting structural changes occur when the IRES is in its normal cellular environment versus in vitro.
    • Fernandez-Miragall O., and Martinez-Salas E. In vivo footprint of a picornavirus internal ribosome entry site reveals differences in accessibility to specific RNA structural elements. J Gen Virol 88 (2007) 3053-3062. This paper probes the structure of an IRES element within the cell, suggesting structural changes occur when the IRES is in its normal cellular environment versus in vitro.
    • (2007) J Gen Virol , vol.88 , pp. 3053-3062
    • Fernandez-Miragall, O.1    Martinez-Salas, E.2
  • 62
    • 0034663980 scopus 로고    scopus 로고
    • A cell cycle-dependent protein serves as a template-specific translation initiation factor
    • This reported the identification of an ITAF protein that binds to a picornavirus IRES RNA, and suggests how the interaction of this cell-type specific protein with the IRES could explain the preferential? activity of certain IRESs in certain cell types.
    • Pilipenko E.V., Pestova T.V., Kolupaeva V.G., Khitrina E.V., Poperechnaya A.N., Agol V.I., and Hellen C.U. A cell cycle-dependent protein serves as a template-specific translation initiation factor. Genes Dev 14 (2000) 2028-2045. This reported the identification of an ITAF protein that binds to a picornavirus IRES RNA, and suggests how the interaction of this cell-type specific protein with the IRES could explain the preferential? activity of certain IRESs in certain cell types.
    • (2000) Genes Dev , vol.14 , pp. 2028-2045
    • Pilipenko, E.V.1    Pestova, T.V.2    Kolupaeva, V.G.3    Khitrina, E.V.4    Poperechnaya, A.N.5    Agol, V.I.6    Hellen, C.U.7
  • 63
    • 0035062960 scopus 로고    scopus 로고
    • Functional interaction of translation initiation factor eIF4G with the foot-and-mouth disease virus internal ribosome entry site
    • Saleh L., Rust R.C., Fullkrug R., Beck E., Bassili G., Ochs K., and Niepmann M. Functional interaction of translation initiation factor eIF4G with the foot-and-mouth disease virus internal ribosome entry site. J Gen Virol 82 (2001) 757-763
    • (2001) J Gen Virol , vol.82 , pp. 757-763
    • Saleh, L.1    Rust, R.C.2    Fullkrug, R.3    Beck, E.4    Bassili, G.5    Ochs, K.6    Niepmann, M.7
  • 64
    • 0035040192 scopus 로고    scopus 로고
    • A novel protein-RNA binding assay: functional interactions of the foot-and-mouth disease virus internal ribosome entry site with cellular proteins
    • Stassinopoulos I.A., and Belsham G.J. A novel protein-RNA binding assay: functional interactions of the foot-and-mouth disease virus internal ribosome entry site with cellular proteins. RNA 7 (2001) 114-122
    • (2001) RNA , vol.7 , pp. 114-122
    • Stassinopoulos, I.A.1    Belsham, G.J.2
  • 65
    • 0034852292 scopus 로고    scopus 로고
    • IRES interaction with translation initiation factors: functional characterization of novel RNA contacts with eIF3, eIF4B, and eIF4GII
    • Lopez de Quinto S., Lafuente E., and Martinez-Salas E. IRES interaction with translation initiation factors: functional characterization of novel RNA contacts with eIF3, eIF4B, and eIF4GII. RNA 7 (2001) 1213-1226
    • (2001) RNA , vol.7 , pp. 1213-1226
    • Lopez de Quinto, S.1    Lafuente, E.2    Martinez-Salas, E.3
  • 66
    • 28344442948 scopus 로고    scopus 로고
    • Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation
    • Song Y., Tzima E., Ochs K., Bassili G., Trusheim H., Linder M., Preissner K.T., and Niepmann M. Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation. RNA 11 (2005) 1809-1824
    • (2005) RNA , vol.11 , pp. 1809-1824
    • Song, Y.1    Tzima, E.2    Ochs, K.3    Bassili, G.4    Trusheim, H.5    Linder, M.6    Preissner, K.T.7    Niepmann, M.8
  • 67
    • 0036000028 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1alpha mRNA contains an internal ribosome entry site that allows efficient translation during normoxia and hypoxia
    • Lang K.J., Kappel A., and Goodall G.J. Hypoxia-inducible factor-1alpha mRNA contains an internal ribosome entry site that allows efficient translation during normoxia and hypoxia. Mol Biol Cell 13 (2002) 1792-1801
    • (2002) Mol Biol Cell , vol.13 , pp. 1792-1801
    • Lang, K.J.1    Kappel, A.2    Goodall, G.J.3
  • 68
    • 33646884832 scopus 로고    scopus 로고
    • Assessing IRES activity in the HIF-1alpha and other cellular 5′ UTRs
    • Bert A.G., Grepin R., Vadas M.A., and Goodall G.J. Assessing IRES activity in the HIF-1alpha and other cellular 5′ UTRs. RNA 12 (2006) 1074-1083
    • (2006) RNA , vol.12 , pp. 1074-1083
    • Bert, A.G.1    Grepin, R.2    Vadas, M.A.3    Goodall, G.J.4
  • 69
    • 52449108643 scopus 로고    scopus 로고
    • FGF2 translationally induced by hypoxia is involved in negative and positive feedback loops with HIF-1alpha
    • Conte C., Riant E., Toutain C., Pujol F., Arnal J.F., Lenfant F., and Prats A.C. FGF2 translationally induced by hypoxia is involved in negative and positive feedback loops with HIF-1alpha. PLoS ONE 3 (2008) e3078
    • (2008) PLoS ONE , vol.3
    • Conte, C.1    Riant, E.2    Toutain, C.3    Pujol, F.4    Arnal, J.F.5    Lenfant, F.6    Prats, A.C.7
  • 70
    • 33847058369 scopus 로고    scopus 로고
    • Translational induction of VEGF internal ribosome entry site elements during the early response to ischemic stress
    • This manuscript reports a direct link between a cellular mRNA containing two IRESs and a specific cellular response to stress in vivo.
    • Bornes S., Prado-Lourenco L., Bastide A., Zanibellato C., Iacovoni J.S., Lacazette E., Prats A.C., Touriol C., and Prats H. Translational induction of VEGF internal ribosome entry site elements during the early response to ischemic stress. Circ Res 100 (2007) 305-308. This manuscript reports a direct link between a cellular mRNA containing two IRESs and a specific cellular response to stress in vivo.
    • (2007) Circ Res , vol.100 , pp. 305-308
    • Bornes, S.1    Prado-Lourenco, L.2    Bastide, A.3    Zanibellato, C.4    Iacovoni, J.S.5    Lacazette, E.6    Prats, A.C.7    Touriol, C.8    Prats, H.9
  • 72
    • 4644351957 scopus 로고    scopus 로고
    • Enhancement of IRES-mediated translation of the c-myc and BiP mRNAs by the poly(A) tail is independent of intact eIF4G and PABP
    • Thoma C., Bergamini G., Galy B., Hundsdoerfer P., and Hentze M.W. Enhancement of IRES-mediated translation of the c-myc and BiP mRNAs by the poly(A) tail is independent of intact eIF4G and PABP. Mol Cell 15 (2004) 925-935
    • (2004) Mol Cell , vol.15 , pp. 925-935
    • Thoma, C.1    Bergamini, G.2    Galy, B.3    Hundsdoerfer, P.4    Hentze, M.W.5
  • 73
    • 34548535363 scopus 로고    scopus 로고
    • Cap-independent translation is required for starvation-induced differentiation in yeast
    • This paper reports the discovery of a sequence in a yeast mRNA that functions as a platform for recruiting the ribosome internally, how this is used in response to specific conditions, and how it might work on the molecular level.
    • Gilbert W.V., Zhou K., Butler T.K., and Doudna J.A. Cap-independent translation is required for starvation-induced differentiation in yeast. Science 317 (2007) 1224-1227. This paper reports the discovery of a sequence in a yeast mRNA that functions as a platform for recruiting the ribosome internally, how this is used in response to specific conditions, and how it might work on the molecular level.
    • (2007) Science , vol.317 , pp. 1224-1227
    • Gilbert, W.V.1    Zhou, K.2    Butler, T.K.3    Doudna, J.A.4
  • 75
    • 0037349339 scopus 로고    scopus 로고
    • The Apaf-1 internal ribosome entry segment attains the correct structural conformation for function via interactions with PTB and unr
    • Mitchell S.A., Spriggs K.A., Coldwell M.J., Jackson R.J., and Willis A.E. The Apaf-1 internal ribosome entry segment attains the correct structural conformation for function via interactions with PTB and unr. Mol Cell 11 (2003) 757-771
    • (2003) Mol Cell , vol.11 , pp. 757-771
    • Mitchell, S.A.1    Spriggs, K.A.2    Coldwell, M.J.3    Jackson, R.J.4    Willis, A.E.5
  • 76
    • 76549116230 scopus 로고    scopus 로고
    • Strong eukaryotic IRESs have weak secondary structure
    • Xia X., and Holcik M. Strong eukaryotic IRESs have weak secondary structure. PLoS ONE 4 (2009) e4136
    • (2009) PLoS ONE , vol.4
    • Xia, X.1    Holcik, M.2
  • 77
    • 38849172516 scopus 로고    scopus 로고
    • Re-programming of translation following cell stress allows IRES-mediated translation to predominate
    • Spriggs K.A., Stoneley M., Bushell M., and Willis A.E. Re-programming of translation following cell stress allows IRES-mediated translation to predominate. Biol Cell 100 (2008) 27-38
    • (2008) Biol Cell , vol.100 , pp. 27-38
    • Spriggs, K.A.1    Stoneley, M.2    Bushell, M.3    Willis, A.E.4
  • 78
    • 39149111540 scopus 로고    scopus 로고
    • For IRES trans-acting factors, it is all about location
    • Lewis S.M., and Holcik M. For IRES trans-acting factors, it is all about location. Oncogene 27 (2008) 1033-1035
    • (2008) Oncogene , vol.27 , pp. 1033-1035
    • Lewis, S.M.1    Holcik, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.