메뉴 건너뛰기




Volumn 107, Issue 24, 2010, Pages 10884-10889

Structure of the Qβ replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins

Author keywords

Protein biosynthesis; Virus

Indexed keywords

Q BETA REPLICASE; RNA DIRECTED RNA POLYMERASE; VIRUS PROTEIN; ELONGATION FACTOR; ELONGATION FACTOR TS; ELONGATION FACTOR TU; ESCHERICHIA COLI PROTEIN; HYBRID PROTEIN; MULTIPROTEIN COMPLEX; PRIMER DNA;

EID: 77954636017     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1003015107     Document Type: Article
Times cited : (71)

References (40)
  • 2
    • 0031555656 scopus 로고    scopus 로고
    • Strongly reduced phage Qβ replication, but normal phage MS2 replication in an Escherichia coliK12 mutant with inactivated Qβ host factor (hfq) gene
    • Su Q, Schuppli D, Tsui HCT, Winkler ME, Weber H (1997) Strongly reduced phage Qβ replication, but normal phage MS2 replication in an Escherichia coliK12 mutant with inactivated Qβ host factor (hfq) gene. Virology 227:211-214.
    • (1997) Virology , vol.227 , pp. 211-214
    • Su, Q.1    Schuppli, D.2    Tsui, H.C.T.3    Winkler, M.E.4    Weber, H.5
  • 3
    • 0025914320 scopus 로고
    • Efficient templates for Qβ replicase are formed by recombination from heterologous sequences
    • Munishkin AV, et al. (1991) Efficient templates for Qβ replicase are formed by recombination from heterologous sequences. J Mol Biol 221:463-472.
    • (1991) J Mol Biol , vol.221 , pp. 463-472
    • Munishkin, A.V.1
  • 4
    • 0015519076 scopus 로고
    • Reconstitution of Qβ replicase lacking subunit with protein-synthesis-interference factor i
    • Kamen R, Kondo M, Römer W, Weissmann C (1972) Reconstitution of Qβ replicase lacking subunit with protein-synthesis-interference factor i. Eur J Biochem 31:44-51.
    • (1972) Eur J Biochem , vol.31 , pp. 44-51
    • Kamen, R.1    Kondo, M.2    Römer, W.3    Weissmann, C.4
  • 5
    • 49549157277 scopus 로고
    • The making of a phage
    • Weissmann C (1974) The making of a phage. FEBS Lett 40:S10-18.
    • (1974) FEBS Lett , vol.40
    • Weissmann, C.1
  • 6
    • 0035158897 scopus 로고    scopus 로고
    • Autonomous role of 3′-terminal CCCA in directing transcription of RNAs by Qβ replicase
    • Tretheway DM, Yoshinari S, Dreher TW (2001) Autonomous role of 3′-terminal CCCA in directing transcription of RNAs by Qβ replicase. J Virol 75:11373-11383.
    • (2001) J Virol , vol.75 , pp. 11373-11383
    • Tretheway, D.M.1    Yoshinari, S.2    Dreher, T.W.3
  • 7
    • 0018370008 scopus 로고
    • RNA replication: Function and structure of Qβ replicase
    • Blumenthal T, Carmichael GG (1979) RNA replication: Function and structure of Qβ replicase. Annu Rev Biochem 48:525-548.
    • (1979) Annu Rev Biochem , vol.48 , pp. 525-548
    • Blumenthal, T.1    Carmichael, G.G.2
  • 8
    • 0029859576 scopus 로고    scopus 로고
    • RNA replication by Qβ replicase: A working model
    • Brown D, Gold L (1996) RNA replication by Qβ replicase: A working model. Proc Natl Acad Sci USA 93:11558-11562.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11558-11562
    • Brown, D.1    Gold, L.2
  • 11
    • 0035196995 scopus 로고    scopus 로고
    • The NS5A protein of bovine viral diarrhoea virus interacts with the alpha subunit of translation elongation factor-1
    • Johnson CM, Perez DR, French R, Merrick WC, Donis RO (2001) The NS5A protein of bovine viral diarrhoea virus interacts with the alpha subunit of translation elongation factor-1. J Gen Virol 82:2935-2943. (Pubitemid 33107507)
    • (2001) Journal of General Virology , vol.82 , Issue.12 , pp. 2935-2943
    • Johnson, C.M.1    Perez, D.R.2    French, R.3    Merrick, W.C.4    Donis, R.O.5
  • 12
    • 0027959741 scopus 로고
    • Interaction ofpoliovirus ppolypeptide 3CDpro with the 5′ and 3′ termini of the poliovirus genome. Identification of viral and cellular cofactors needed for efficient binding
    • Harris KS, et al. (1994) Interaction ofpoliovirus ppolypeptide 3CDpro with the 5′ and 3′ termini of the poliovirus genome. Identification of viral and cellular cofactors needed for efficient binding. J Biol Chem 269:27004-27014.
    • (1994) J Biol Chem , vol.269 , pp. 27004-27014
    • Harris, K.S.1
  • 13
    • 33645028151 scopus 로고    scopus 로고
    • In vivo interaction between Tobacco mosaic virus RNA-dependent RNA polymerase and host translation elongation factor 1A
    • Yamaji Y, et al. (2006) In vivo interaction between Tobacco mosaic virus RNA-dependent RNA polymerase and host translation elongation factor 1A. Virology 347:100-108.
    • (2006) Virology , vol.347 , pp. 100-108
    • Yamaji, Y.1
  • 14
    • 33750285215 scopus 로고    scopus 로고
    • Structure and function of RNA replication
    • Ortin J, Parra F (2006) Structure and function of RNA replication. Annu Rev Microbiol 60:305-326.
    • (2006) Annu Rev Microbiol , vol.60 , pp. 305-326
    • Ortin, J.1    Parra, F.2
  • 15
    • 33746750133 scopus 로고    scopus 로고
    • Functional Qβ replicase genetically fusing essential subunits EF-Ts and EF-Tu with beta-subunit
    • Kita H, et al. (2006) Functional Qβ replicase genetically fusing essential subunits EF-Ts and EF-Tu with beta-subunit. J Biosci Bioeng 101:421-426.
    • (2006) J Biosci Bioeng , vol.101 , pp. 421-426
    • Kita, H.1
  • 16
    • 0000167256 scopus 로고
    • A viral cleavage site cassette: Identification of amino acid sequences required for tobacco etch virus polyprotein processing
    • Carrington JC, Dougherty WG (1988) A viral cleavage site cassette: Identification of amino acid sequences required for tobacco etch virus polyprotein processing. Proc Natl Acad Sci USA 85:3391-3395.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 3391-3395
    • Carrington, J.C.1    Dougherty, W.G.2
  • 17
    • 0242666438 scopus 로고    scopus 로고
    • Qβ replicase discriminates between legitimate and illegitimate templates by having different mechanisms of initiation
    • Ugarov VI, Demidenko AA, Chetverin AB (2003) Qβ replicase discriminates between legitimate and illegitimate templates by having different mechanisms of initiation. J Biol Chem 278:44139-44146.
    • (2003) J Biol Chem , vol.278 , pp. 44139-44146
    • Ugarov, V.I.1    Demidenko, A.A.2    Chetverin, A.B.3
  • 18
    • 40649100793 scopus 로고    scopus 로고
    • Structure-function relationships among RNA-dependent RNA polymerases
    • Ng KK, Arnold JJ, Cameron CE (2008) Structure-function relationships among RNA-dependent RNA polymerases. Curr Top Microbiol Immunol 320:137-156.
    • (2008) Curr Top Microbiol Immunol , vol.320 , pp. 137-156
    • Ng, K.K.1    Arnold, J.J.2    Cameron, C.E.3
  • 19
    • 0037386414 scopus 로고    scopus 로고
    • A structural and primary sequence comparison of the viral RNA-dependent RNA polymerases
    • Bruenn JA (2003) A structural and primary sequence comparison of the viral RNA-dependent RNA polymerases. Nucleic Acids Res 31:1821-1829.
    • (2003) Nucleic Acids Res , vol.31 , pp. 1821-1829
    • Bruenn, J.A.1
  • 20
    • 0033539482 scopus 로고    scopus 로고
    • Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus
    • Bressanelli S, et al. (1999) Crystal structure of the RNA-dependent RNA polymerase of hepatitis C virus. Proc Natl Acad Sci USA 96:13034-13039.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13034-13039
    • Bressanelli, S.1
  • 21
    • 18744392514 scopus 로고    scopus 로고
    • RNA synthesis in a cage - Structural studies of reovirus polymerase λ3
    • DOI 10.1016/S0092-8674(02)01110-8
    • Tao Y, Farsetta DL, Nibert ML, Harrison SC (2002) RNA synthesis in a cage - Structural studies of reovirus polymerase λ3. Cell 111:733-745. (Pubitemid 35452525)
    • (2002) Cell , vol.111 , Issue.5 , pp. 733-745
    • Tao, Y.1    Farsetta, D.L.2    Nibert, M.L.3    Harrison, S.C.4
  • 22
    • 0030025671 scopus 로고    scopus 로고
    • The structure of the Escherichia coli EF-Tu • EF-Ts complex at 2.5 Å resolution
    • Kawashima T, Berthet-Colomunas C, Wulff M, Cusack S, Leberman R (1996) The structure of the Escherichia coli EF-Tu • EF-Ts complex at 2.5 Å resolution. Nature 379:511-518.
    • (1996) Nature , vol.379 , pp. 511-518
    • Kawashima, T.1    Berthet-Colomunas, C.2    Wulff, M.3    Cusack, S.4    Leberman, R.5
  • 23
    • 0028812785 scopus 로고
    • Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu and a GTP analog
    • Nissen P, et al. (1995) Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu and a GTP analog. Science 270:1464-1472.
    • (1995) Science , vol.270 , pp. 1464-1472
    • Nissen, P.1
  • 24
    • 43149087336 scopus 로고    scopus 로고
    • Structural insights into mechanisms of catalysis and inhibition in Norwalk virus polymerase
    • Zamyatkin DF, et al. (2008) Structural insights into mechanisms of catalysis and inhibition in Norwalk virus polymerase. J Biol Chem 283:7705-7712.
    • (2008) J Biol Chem , vol.283 , pp. 7705-7712
    • Zamyatkin, D.F.1
  • 25
    • 0036120573 scopus 로고    scopus 로고
    • Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides
    • DOI 10.1128/JVI.76.7.3482-3492.2002
    • Bressanelli S, Tomei L, Rey FA, De Francesco R (2002) Structural analysis of the hepatitis C virus RNA polymerase in complex with ribonucleotides. J Virol 76:3482-3492. (Pubitemid 34224549)
    • (2002) Journal of Virology , vol.76 , Issue.7 , pp. 3482-3492
    • Bressanelli, S.1    Tomei, L.2    Rey, F.A.3    De Francesco, R.4
  • 26
    • 0032518374 scopus 로고    scopus 로고
    • A mechanism for all polymerases
    • Steitz TA (1998) A mechanism for all polymerases. Nature 391:231-232.
    • (1998) Nature , vol.391 , pp. 231-232
    • Steitz, T.A.1
  • 27
    • 59649110607 scopus 로고    scopus 로고
    • Nucleic acid polymerases use a general acid for nucleotidyl transfer
    • Castro C, et al. (2009) Nucleic acid polymerases use a general acid for nucleotidyl transfer. Nat Struct Mol Biol 16:212-218.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 212-218
    • Castro, C.1
  • 28
    • 0014936343 scopus 로고
    • Characterization of the subunits of Qβ replicase
    • Kamen R (1970) Characterization of the subunits of Qβ replicase. Nature 228:527-533.
    • (1970) Nature , vol.228 , pp. 527-533
    • Kamen, R.1
  • 29
    • 0018791501 scopus 로고
    • RNA replication: Required intermediates and the dissociation of template, product, and Qβ replicase
    • Dobkin C, Mills DR, Kramer FR, Spiegelman S (1979) RNA replication: Required intermediates and the dissociation of template, product, and Qβ replicase. Biochemistry 18:2038-2044.
    • (1979) Biochemistry , vol.18 , pp. 2038-2044
    • Dobkin, C.1    Mills, D.R.2    Kramer, F.R.3    Spiegelman, S.4
  • 30
    • 2542473234 scopus 로고    scopus 로고
    • Replicable and recombinogenic RNAs
    • Chetverin AB (2004) Replicable and recombinogenic RNAs. FEBS Lett 567:35-41.
    • (2004) FEBS Lett , vol.567 , pp. 35-41
    • Chetverin, A.B.1
  • 31
    • 0014393938 scopus 로고
    • In vitro synthesis of phage RNA: The nature of the intermediates
    • Weissmann C, Feix G, Slor H (1968) In vitro synthesis of phage RNA: The nature of the intermediates. Cold SH Q B 33:83-100.
    • (1968) Cold SH Q B , vol.33 , pp. 83-100
    • Weissmann, C.1    Feix, G.2    Slor, H.3
  • 32
    • 0028808340 scopus 로고
    • Selection and characterization of RNAs replicated by Qβ replicase
    • Brown D, Gold L (1995) Selection and characterization of RNAs replicated by Qβ replicase. Biochemistry 34:14775-14782.
    • (1995) Biochemistry , vol.34 , pp. 14775-14782
    • Brown, D.1    Gold, L.2
  • 33
    • 0016174555 scopus 로고
    • Function and structure in ribonucleic acid phage Qβ ribonucleic acid replicase
    • Landers TA, Blumenthal T, Weber K (1974) Function and structure in ribonucleic acid phage Qβ ribonucleic acid replicase. J Biol Chem 249:5801-5808.
    • (1974) J Biol Chem , vol.249 , pp. 5801-5808
    • Landers, T.A.1    Blumenthal, T.2    Weber, K.3
  • 35
    • 0242500984 scopus 로고    scopus 로고
    • Isolation of Qβ polymerase complexes containing mutant species of elongation factor Tu
    • Mathu SGJ, Knudsen CR, van Duin J, Kraal B (2003) Isolation of Qβ polymerase complexes containing mutant species of elongation factor Tu. J Chromatogr B 786:279-286.
    • (2003) J Chromatogr B , vol.786 , pp. 279-286
    • Mathu, S.G.J.1    Knudsen, C.R.2    Van Duin, J.3    Kraal, B.4
  • 37
    • 1842490687 scopus 로고    scopus 로고
    • XDS
    • eds MG Rossmann and E Arnold (Kluwer Academic, Dordrecht)
    • Kabsch W (2001) XDS. International Tables for Crystallography, eds MG Rossmann and E Arnold (Kluwer Academic, Dordrecht), Vol F.
    • (2001) International Tables for Crystallography , vol.F
    • Kabsch, W.1
  • 38
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D 63:32-41.
    • (2007) Acta Crystallogr D , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 39
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D 60:2126-2132.
    • (2004) Acta Crystallogr D , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 40
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D 58:1948-1954.
    • (2002) Acta Crystallogr D , vol.58 , pp. 1948-1954
    • Adams, P.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.