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Volumn 316, Issue 2, 2003, Pages 313-324

Identification of two histidines necessary for reovirus mRNA guanylyltransferase activity

Author keywords

Aquareovirus; Guanylyltransferase; Histidine protonation; Mammalian reovirus; mRNA capping; Orbivirus; Reoviridae; Reovirus; Rotavirus; Vaccinia virus

Indexed keywords

GUANOSINE PHOSPHATE; GUANYLYLTRANSFERASE; HISTIDINE; ISOENZYME; MESSENGER RNA; PROTEIN VP1; UNCLASSIFIED DRUG;

EID: 0344982823     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virol.2003.08.027     Document Type: Article
Times cited : (28)

References (50)
  • 1
    • 0036324190 scopus 로고    scopus 로고
    • Common evolutionary origin of aquareoviruses and orthoreoviruses revealed by genome characterization of Golden shiner reovirus, Grass carp reovirus, Striped bass reovirus and golden ide reovirus (genus Aquareovirus, family Reoviridae)
    • Attoui H., Fang Q., Jaafar F.M., Cantaloube J.F., Biagini P., de Micco P., de Lamballerie X. Common evolutionary origin of aquareoviruses and orthoreoviruses revealed by genome characterization of Golden shiner reovirus, Grass carp reovirus, Striped bass reovirus and golden ide reovirus (genus Aquareovirus, family Reoviridae). J. Gen. Virol. 83:(Pt. 8):2002;1941-1951.
    • (2002) J. Gen. Virol. , vol.83 , Issue.PT. 8 , pp. 1941-1951
    • Attoui, H.1    Fang, Q.2    Jaafar, F.M.3    Cantaloube, J.F.4    Biagini, P.5    De Micco, P.6    De Lamballerie, X.7
  • 2
    • 0019276997 scopus 로고
    • 5′-terminal cap structure in eucaryotic messenger ribonucleic acids
    • Banerjee A.K. 5′-terminal cap structure in eucaryotic messenger ribonucleic acids. Microbiol. Rev. 44:(2):1980;175-205.
    • (1980) Microbiol. Rev. , vol.44 , Issue.2 , pp. 175-205
    • Banerjee, A.K.1
  • 4
    • 0035450448 scopus 로고    scopus 로고
    • Mammalian reovirus L2 gene and lambda2 core spike protein sequences and whole-genome comparisons of reoviruses type 1 Lang, type 2 Jones, and type 3 Dearing
    • Breun L.A., Broering T.J., McCutcheon A.M., Harrison S.J., Luongo C.L., Nibert M.L. Mammalian reovirus L2 gene and lambda2 core spike protein sequences and whole-genome comparisons of reoviruses type 1 Lang, type 2 Jones, and type 3 Dearing. Virology. 287:(2):2001;333-348.
    • (2001) Virology , vol.287 , Issue.2 , pp. 333-348
    • Breun, L.A.1    Broering, T.J.2    McCutcheon, A.M.3    Harrison, S.J.4    Luongo, C.L.5    Nibert, M.L.6
  • 5
    • 0037853207 scopus 로고    scopus 로고
    • Membrane fusion induced by vesicular stomatitis virus depends on histidine protonation
    • Carneiro F.A., Stauffer F., Lima C.S., Juliano M.A., Juliano L., Da Poian A.T. Membrane fusion induced by vesicular stomatitis virus depends on histidine protonation. J. Biol. Chem. 278:(16):2003;13789-13794.
    • (2003) J. Biol. Chem. , vol.278 , Issue.16 , pp. 13789-13794
    • Carneiro, F.A.1    Stauffer, F.2    Lima, C.S.3    Juliano, M.A.4    Juliano, L.5    Da Poian, A.T.6
  • 6
    • 0035036348 scopus 로고    scopus 로고
    • Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein
    • Chandran K., Zhang X., Olson N.H., Walker S.B., Chappell J.D., Dermody T.S., Baker T.S., Nibert M.L. Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein. J. Virol. 75:(11):2001;5335-5342.
    • (2001) J. Virol. , vol.75 , Issue.11 , pp. 5335-5342
    • Chandran, K.1    Zhang, X.2    Olson, N.H.3    Walker, S.B.4    Chappell, J.D.5    Dermody, T.S.6    Baker, T.S.7    Nibert, M.L.8
  • 8
    • 0022478937 scopus 로고
    • Reovirus guanylyltransferase is L2 gene product lambda 2
    • Cleveland D.R., Zarbl H., Millward S. Reovirus guanylyltransferase is L2 gene product lambda 2. J. Virol. 60:(1):1986;307-311.
    • (1986) J. Virol. , vol.60 , Issue.1 , pp. 307-311
    • Cleveland, D.R.1    Zarbl, H.2    Millward, S.3
  • 9
    • 0028862970 scopus 로고
    • Mutational analysis of mRNA capping enzyme identifies amino acids involved in GTP binding, enzyme-guanylate formation, and GMP transfer to RNA
    • Cong P., Shuman S. Mutational analysis of mRNA capping enzyme identifies amino acids involved in GTP binding, enzyme-guanylate formation, and GMP transfer to RNA. Mol. Cell Biol. 15:(11):1995;6222-6231.
    • (1995) Mol. Cell Biol. , vol.15 , Issue.11 , pp. 6222-6231
    • Cong, P.1    Shuman, S.2
  • 10
    • 0025003413 scopus 로고
    • Crystallization of the reovirus type 3 Dearing core. Crystal packing is determined by the lambda 2 protein
    • Coombs K.M., Fields B.N., Harrison S.C. Crystallization of the reovirus type 3 Dearing core. Crystal packing is determined by the lambda 2 protein. J. Mol. Biol. 215:(1):1990;1-5.
    • (1990) J. Mol. Biol. , vol.215 , Issue.1 , pp. 1-5
    • Coombs, K.M.1    Fields, B.N.2    Harrison, S.C.3
  • 11
    • 0027162058 scopus 로고
    • Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: Analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction
    • Dryden K.A., Wang G., Yeager M., Nibert M.L., Coombs K.M., Furlong D.B., Fields B.N., Baker T.S. Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation analysis of virions and subviral particles by cryoelectron microscopy and image reconstruction . J. Cell. Biol. 122:(5):1993;1023-1041.
    • (1993) J. Cell. Biol. , vol.122 , Issue.5 , pp. 1023-1041
    • Dryden, K.A.1    Wang, G.2    Yeager, M.3    Nibert, M.L.4    Coombs, K.M.5    Furlong, D.B.6    Fields, B.N.7    Baker, T.S.8
  • 13
    • 0025320720 scopus 로고
    • Active site localization in a viral mRNA capping enzyme
    • Fausnaugh J., Shatkin A.J. Active site localization in a viral mRNA capping enzyme. J. Biol. Chem. 265:(13):1990;7669-7672.
    • (1990) J. Biol. Chem. , vol.265 , Issue.13 , pp. 7669-7672
    • Fausnaugh, J.1    Shatkin, A.J.2
  • 14
    • 0028214041 scopus 로고
    • Active site of the mRNA-capping enzyme guanylyltransferase from Saccharomyces cerevisiae: Similarity to the nucleotidyl attachment motif of DNA and RNA ligases
    • Fresco L.D., Buratowski S. Active site of the mRNA-capping enzyme guanylyltransferase from Saccharomyces cerevisiae similarity to the nucleotidyl attachment motif of DNA and RNA ligases . Proc. Natl. Acad. Sci. USA. 91:(14):1994;6624-6628.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , Issue.14 , pp. 6624-6628
    • Fresco, L.D.1    Buratowski, S.2
  • 15
    • 0023945392 scopus 로고
    • Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles
    • Furlong D.B., Nibert M.L., Fields B.N. Sigma 1 protein of mammalian reoviruses extends from the surfaces of viral particles. J. Virol. 62:(1):1988;246-256.
    • (1988) J. Virol. , vol.62 , Issue.1 , pp. 246-256
    • Furlong, D.B.1    Nibert, M.L.2    Fields, B.N.3
  • 16
    • 0017141875 scopus 로고
    • Mechanism of formation of reovirus mRNA 5′-terminal blocked and methylated sequence, m7GpppGmpC
    • Furuichi Y., Muthukrishnan S., Tomasz J., Shatkin A.J. Mechanism of formation of reovirus mRNA 5′-terminal blocked and methylated sequence, m7GpppGmpC. J. Biol. Chem. 251:(16):1976;5043-5053.
    • (1976) J. Biol. Chem. , vol.251 , Issue.16 , pp. 5043-5053
    • Furuichi, Y.1    Muthukrishnan, S.2    Tomasz, J.3    Shatkin, A.J.4
  • 17
    • 0031772992 scopus 로고    scopus 로고
    • RNA 5′-triphosphatase, nucleoside triphosphatase, and guanylyltransferase activities of baculovirus LEF-4 protein
    • Gross C.H., Shuman S. RNA 5′-triphosphatase, nucleoside triphosphatase, and guanylyltransferase activities of baculovirus LEF-4 protein. J. Virol. 72:(12):1998;10020-10028.
    • (1998) J. Virol. , vol.72 , Issue.12 , pp. 10020-10028
    • Gross, C.H.1    Shuman, S.2
  • 18
    • 0038228666 scopus 로고    scopus 로고
    • X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes
    • Hakansson K., Doherty A.J., Shuman S., Wigley D.B. X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes. Cell. 89:(4):1997;545-553.
    • (1997) Cell , vol.89 , Issue.4 , pp. 545-553
    • Hakansson, K.1    Doherty, A.J.2    Shuman, S.3    Wigley, D.B.4
  • 19
    • 0032539677 scopus 로고    scopus 로고
    • Structure of a complex between a cap analogue and mRNA guanylyltransferase demonstrates the structural chemistry of RNA capping
    • Hakansson K., Wigley D.B. Structure of a complex between a cap analogue and mRNA guanylyltransferase demonstrates the structural chemistry of RNA capping. Proc. Natl. Acad. Sci. USA. 95:(4):1998;1505-1510.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.4 , pp. 1505-1510
    • Hakansson, K.1    Wigley, D.B.2
  • 20
    • 0027008546 scopus 로고
    • Structure of bluetongue virus particles by cryoelectron microscopy
    • Hewat E.A., Booth T.F., Roy P. Structure of bluetongue virus particles by cryoelectron microscopy. J. Struct. Biol. 109:(1):1992;61-69.
    • (1992) J. Struct. Biol. , vol.109 , Issue.1 , pp. 61-69
    • Hewat, E.A.1    Booth, T.F.2    Roy, P.3
  • 21
    • 0036297716 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of avian reovirus guanylyltransferase
    • Hsiao J., Martinez-Costas J., Benavente J., Vakharia V.N. Cloning, expression, and characterization of avian reovirus guanylyltransferase. Virology. 296:(2):2002;288-299.
    • (2002) Virology , vol.296 , Issue.2 , pp. 288-299
    • Hsiao, J.1    Martinez-Costas, J.2    Benavente, J.3    Vakharia, V.N.4
  • 22
    • 0030585155 scopus 로고    scopus 로고
    • When two strands are better than one: The mediators and modulators of the cellular responses to double-stranded RNA
    • Jacobs B.L., Langland J.O. When two strands are better than one the mediators and modulators of the cellular responses to double-stranded RNA . Virology. 219:(2):1996;339-349.
    • (1996) Virology , vol.219 , Issue.2 , pp. 339-349
    • Jacobs, B.L.1    Langland, J.O.2
  • 23
    • 0026778224 scopus 로고
    • The expressed VP4 protein of bluetongue virus binds GTP and is the candidate guanylyl transferase of the virus
    • Le Blois H., French T., Mertens P.P., Burroughs J.N., Roy P. The expressed VP4 protein of bluetongue virus binds GTP and is the candidate guanylyl transferase of the virus. Virology. 189:(2):1992;757-761.
    • (1992) Virology , vol.189 , Issue.2 , pp. 757-761
    • Le Blois, H.1    French, T.2    Mertens, P.P.3    Burroughs, J.N.4    Roy, P.5
  • 24
    • 0026766537 scopus 로고
    • Rotavirus VP3 expressed in insect cells possesses guanylyltransferase activity
    • Liu M., Mattion N.M., Estes M.K. Rotavirus VP3 expressed in insect cells possesses guanylyltransferase activity. Virology. 188:(1):1992;77-84.
    • (1992) Virology , vol.188 , Issue.1 , pp. 77-84
    • Liu, M.1    Mattion, N.M.2    Estes, M.K.3
  • 26
    • 0036296501 scopus 로고    scopus 로고
    • Mutational analysis of a mammalian reovirus mRNA capping enzyme
    • Luongo C.L. Mutational analysis of a mammalian reovirus mRNA capping enzyme. Biochem. Biophys. Res. Commun. 291:(4):2002;932-938.
    • (2002) Biochem. Biophys. Res. Commun. , vol.291 , Issue.4 , pp. 932-938
    • Luongo, C.L.1
  • 28
    • 0034723208 scopus 로고    scopus 로고
    • Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda2
    • Luongo C.L., Reinisch K.M., Harrison S.C., Nibert M.L. Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda2. J. Biol. Chem. 275:(4):2000;2804-2810.
    • (2000) J. Biol. Chem. , vol.275 , Issue.4 , pp. 2804-2810
    • Luongo, C.L.1    Reinisch, K.M.2    Harrison, S.C.3    Nibert, M.L.4
  • 30
    • 0025947194 scopus 로고
    • Isolation and enzymatic characterization of protein lambda 2, the reovirus guanylyltransferase
    • Mao Z.X., Joklik W.K. Isolation and enzymatic characterization of protein lambda 2, the reovirus guanylyltransferase. Virology. 185:(1):1991;377-386.
    • (1991) Virology , vol.185 , Issue.1 , pp. 377-386
    • Mao, Z.X.1    Joklik, W.K.2
  • 31
    • 0028853290 scopus 로고
    • Endogenous enzymatic activities of the avian reovirus S1133: Identification of the viral capping enzyme
    • Martinez-Costas J., Varela R., Benavente J. Endogenous enzymatic activities of the avian reovirus S1133 identification of the viral capping enzyme . Virology. 206:(2):1995;1017-1026.
    • (1995) Virology , vol.206 , Issue.2 , pp. 1017-1026
    • Martinez-Costas, J.1    Varela, R.2    Benavente, J.3
  • 32
    • 0023145305 scopus 로고
    • Purification and properties of virus particles, infectious subviral particles, and cores of bluetongue virus serotypes 1 and 4
    • Mertens P.P., Burroughs J.N., Anderson J. Purification and properties of virus particles, infectious subviral particles, and cores of bluetongue virus serotypes 1 and 4. Virology. 157:(2):1987;375-386.
    • (1987) Virology , vol.157 , Issue.2 , pp. 375-386
    • Mertens, P.P.1    Burroughs, J.N.2    Anderson, J.3
  • 33
    • 0017632673 scopus 로고
    • Modification of histidyl residues in proteins by diethylpyrocarbonate
    • Miles E.W. Modification of histidyl residues in proteins by diethylpyrocarbonate. Methods Enzymol. 47:1977;431-442.
    • (1977) Methods Enzymol. , vol.47 , pp. 431-442
    • Miles, E.W.1
  • 34
    • 0033919812 scopus 로고    scopus 로고
    • Trypsin-induced structural transformation in aquareovirus
    • Nason E.L., Samal S.K., Venkataram Prasad B.V. Trypsin-induced structural transformation in aquareovirus. J. Virol. 74:(14):2000;6546-6555.
    • (2000) J. Virol. , vol.74 , Issue.14 , pp. 6546-6555
    • Nason, E.L.1    Samal, S.K.2    Venkataram Prasad, B.V.3
  • 35
    • 0032903494 scopus 로고    scopus 로고
    • RNA-binding and capping activities of proteins in rotavirus open cores
    • Patton J.T., Chen D. RNA-binding and capping activities of proteins in rotavirus open cores. J. Virol. 73:(2):1999;1382-1391.
    • (1999) J. Virol. , vol.73 , Issue.2 , pp. 1382-1391
    • Patton, J.T.1    Chen, D.2
  • 36
    • 0029839752 scopus 로고    scopus 로고
    • Visualization of ordered genomic RNA and localization of transcriptional complexes in rotavirus
    • Prasad B.V., Rothnagel R., Zeng C.Q., Jakana J., Lawton J.A., Chiu W., Estes M.K. Visualization of ordered genomic RNA and localization of transcriptional complexes in rotavirus. Nature. 382:(6590):1996;471-473.
    • (1996) Nature , vol.382 , Issue.6590 , pp. 471-473
    • Prasad, B.V.1    Rothnagel, R.2    Zeng, C.Q.3    Jakana, J.4    Lawton, J.A.5    Chiu, W.6    Estes, M.K.7
  • 37
  • 38
    • 0019141032 scopus 로고
    • Subunit structure of the reovirus spike
    • Ralph S.J., Harvey J.D., Bellamy A.R. Subunit structure of the reovirus spike. J. Virol. 36:(3):1980;894-896.
    • (1980) J. Virol. , vol.36 , Issue.3 , pp. 894-896
    • Ralph, S.J.1    Harvey, J.D.2    Bellamy, A.R.3
  • 39
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6 a resolution
    • Reinisch K.M., Nibert M.L., Harrison S.C. Structure of the reovirus core at 3.6 A resolution. Nature. 404:(6781):2000;960-967.
    • (2000) Nature , vol.404 , Issue.6781 , pp. 960-967
    • Reinisch, K.M.1    Nibert, M.L.2    Harrison, S.C.3
  • 40
    • 0343773443 scopus 로고    scopus 로고
    • Orbivirus structure and assembly
    • Roy P. Orbivirus structure and assembly. Virology. 216:(1):1996;1-11.
    • (1996) Virology , vol.216 , Issue.1 , pp. 1-11
    • Roy, P.1
  • 41
    • 0023001929 scopus 로고
    • Role of the inner protein capsid on in vitro human rotavirus transcription
    • Sandino A.M., Jashes M., Faundez G., Spencer E. Role of the inner protein capsid on in vitro human rotavirus transcription. J. Virol. 60:(2):1986;797-802.
    • (1986) J. Virol. , vol.60 , Issue.2 , pp. 797-802
    • Sandino, A.M.1    Jashes, M.2    Faundez, G.3    Spencer, E.4
  • 42
    • 0023646021 scopus 로고
    • Complete nucleotide sequence of reovirus L2 gene and deduced amino acid sequence of viral mRNA guanylyltransferase
    • Seliger L.S., Zheng K., Shatkin A.J. Complete nucleotide sequence of reovirus L2 gene and deduced amino acid sequence of viral mRNA guanylyltransferase. J. Biol. Chem. 262:(34):1987;16289-16293.
    • (1987) J. Biol. Chem. , vol.262 , Issue.34 , pp. 16289-16293
    • Seliger, L.S.1    Zheng, K.2    Shatkin, A.J.3
  • 43
    • 0010021286 scopus 로고
    • Initiation of mRNA synthesis and 5′-terminal modification of reovirus transcripts
    • R.W. Compans, & D.H.L. Bishop. New York: Elsevier
    • Shatkin A.J., Furuichi Y., LaFiandra A.J., Yamakawa M. Initiation of mRNA synthesis and 5′-terminal modification of reovirus transcripts. Compans R.W., Bishop D.H.L. Double-Stranded RNA Viruses. 1983;43-54 Elsevier, New York.
    • (1983) Double-Stranded RNA Viruses , pp. 43-54
    • Shatkin, A.J.1    Furuichi, Y.2    Lafiandra, A.J.3    Yamakawa, M.4
  • 44
    • 0029107231 scopus 로고
    • Capping enzyme in eukaryotic mRNA synthesis
    • Shuman S. Capping enzyme in eukaryotic mRNA synthesis. Prog. Nucleic Acid Res. Mol. Biol. 50:1995;101-129.
    • (1995) Prog. Nucleic Acid Res. Mol. Biol. , vol.50 , pp. 101-129
    • Shuman, S.1
  • 45
    • 0019205794 scopus 로고
    • Purification and characterization of a GTP-pyrophosphate exchange activity from vaccinia virions. Association of the GTP-pyrophosphate exchange activity with vaccinia mRNA guanylyltransferase. RNA (guanine-7-) methyltransferase complex (capping enzyme)
    • Shuman S., Surks M., Furneaux H., Hurwitz J. Purification and characterization of a GTP-pyrophosphate exchange activity from vaccinia virions. Association of the GTP-pyrophosphate exchange activity with vaccinia mRNA guanylyltransferase. RNA (guanine-7-)methyltransferase complex (capping enzyme). J. Biol. Chem. 255:(23):1980;11588-11598.
    • (1980) J. Biol. Chem. , vol.255 , Issue.23 , pp. 11588-11598
    • Shuman, S.1    Surks, M.2    Furneaux, H.3    Hurwitz, J.4
  • 46
    • 0014627613 scopus 로고
    • Polypeptide components of virions, top component and cores of reovirus type 3
    • Smith R.E., Zweerink H.J., Joklik W.K. Polypeptide components of virions, top component and cores of reovirus type 3. Virology. 39:(4):1969;791-810.
    • (1969) Virology , vol.39 , Issue.4 , pp. 791-810
    • Smith, R.E.1    Zweerink, H.J.2    Joklik, W.K.3
  • 47
    • 0344894244 scopus 로고
    • Reoviridae: A brief introduction
    • B.N. Fields, D.M. Knipe, & P.M. Howley. New York: Raven Press
    • Tyler K.L., Fields B.N. Reoviridae a brief introduction . Fields B.N., Knipe D.M., Howley P.M. Fundamental Virology. second ed. 1991;583-585 Raven Press, New York.
    • (1991) Fundamental Virology Second Ed. , pp. 583-585
    • Tyler, K.L.1    Fields, B.N.2
  • 48
    • 0037292572 scopus 로고    scopus 로고
    • Identification of the essential histidine residue for high-affinity binding of AlbA protein to albicidin antibiotics
    • Weng L.X., Xu J.L., Li Q., Birch R.G., Zhang L.H. Identification of the essential histidine residue for high-affinity binding of AlbA protein to albicidin antibiotics. Microbiology. 149:(Pt 2):2003;451-457.
    • (2003) Microbiology , vol.149 , Issue.PT 2 , pp. 451-457
    • Weng, L.X.1    Xu, J.L.2    Li, Q.3    Birch, R.G.4    Zhang, L.H.5
  • 49
    • 0020024958 scopus 로고
    • Reovirus transcriptase and capping enzymes are active in intact virions
    • Yamakawa M., Furuichi Y., Shatkin A.J. Reovirus transcriptase and capping enzymes are active in intact virions. Virology. 118:(1):1982;157-168.
    • (1982) Virology , vol.118 , Issue.1 , pp. 157-168
    • Yamakawa, M.1    Furuichi, Y.2    Shatkin, A.J.3
  • 50
    • 0030728958 scopus 로고    scopus 로고
    • Structure-function analysis of the triphosphatase component of vaccinia virus mRNA capping enzyme
    • Yu L., Martins A., Deng L., Shuman S. Structure-function analysis of the triphosphatase component of vaccinia virus mRNA capping enzyme. J. Virol. 71:(12):1997;9837-9843.
    • (1997) J. Virol. , vol.71 , Issue.12 , pp. 9837-9843
    • Yu, L.1    Martins, A.2    Deng, L.3    Shuman, S.4


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