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Volumn 36, Issue 2, 2008, Pages 451-461

Magnesium-binding studies reveal fundamental differences between closely related RNA triphosphatases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GLUTAMIC ACID; MAGNESIUM ION; PHOSPHATASE; RNA TRIPHOSPHATASE; UNCLASSIFIED DRUG;

EID: 39149139012     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkm1067     Document Type: Article
Times cited : (3)

References (44)
  • 1
    • 0034567861 scopus 로고    scopus 로고
    • Viral and cellular mRNA capping: Past and prospects
    • Furuichi,Y. and Shatkin,A.J. (2000) Viral and cellular mRNA capping: past and prospects. Adv. Virol., Res., 55, 135-184.
    • (2000) Adv. Virol., Res , vol.55 , pp. 135-184
    • Furuichi, Y.1    Shatkin, A.J.2
  • 2
    • 0035201941 scopus 로고    scopus 로고
    • Structure, mechanism, and evolution of the mRNA capping apparatus
    • Shuman,S. (2000) Structure, mechanism, and evolution of the mRNA capping apparatus. Prog. Nucleic Acids Res. Mol. Biol., 66, 1-40.
    • (2000) Prog. Nucleic Acids Res. Mol. Biol , vol.66 , pp. 1-40
    • Shuman, S.1
  • 3
    • 0031572262 scopus 로고    scopus 로고
    • Viral and cellular enzymes involved in synthesis of mRNA cap structure
    • Bisaillon,M. and Lemay,G. (1997) Viral and cellular enzymes involved in synthesis of mRNA cap structure. Virology, 236, 1-7.
    • (1997) Virology , vol.236 , pp. 1-7
    • Bisaillon, M.1    Lemay, G.2
  • 4
    • 0034723208 scopus 로고    scopus 로고
    • Identification of the guanylyltranslerase region and active site in reovirus mRNA capping protein lambda2
    • Luongo,C.L.; Reinisch,K.M., Harrison,S.C. and Nibert,M.L. (2000) Identification of the guanylyltranslerase region and active site in reovirus mRNA capping protein lambda2. J. Biol. Chem., 275, 2804-2810.
    • (2000) J. Biol. Chem , vol.275 , pp. 2804-2810
    • Luongo, C.L.1    Reinisch, K.M.2    Harrison, S.C.3    Nibert, M.L.4
  • 5
    • 0030613775 scopus 로고    scopus 로고
    • Characterization of the reovirus lambdal protein RNA 5′-triphosphatase activity
    • Bisaillon,M. and Lemay,G.(1997) Characterization of the reovirus lambdal protein RNA 5′-triphosphatase activity. J. Biol. Chem., 272 29954-29957.
    • (1997) J. Biol. Chem , vol.272 , pp. 29954-29957
    • Bisaillon, M.1    Lemay, G.2
  • 6
    • 0031772992 scopus 로고    scopus 로고
    • RNA 5′-triphosphatase, nucleoside triphosphatase, and guanylyltransferase activities of baculo-irus LEF-4, protein
    • Gross,C.H. and,Shuman,S. (1998) RNA 5′-triphosphatase, nucleoside triphosphatase, and guanylyltransferase activities of baculo-irus LEF-4, protein. J. Virol., 72, 10020-10028.
    • (1998) J. Virol , vol.72 , pp. 10020-10028
    • Gross, C.H.1    Shuman, S.2
  • 7
    • 0030007647 scopus 로고    scopus 로고
    • Characterization of the vaccinia virus RNA 5′-tophosphatase and nucleotide triphosphate phosphohydrolase activities. Demonstration that both activities are carried out at the same active site
    • Myette,J.R. and Niles,E.G. (1996) Characterization of the vaccinia virus RNA 5′-tophosphatase and nucleotide triphosphate phosphohydrolase activities. Demonstration that both activities are carried out at the same active site. J. Biol. Chem., 271, 11945-11952.
    • (1996) J. Biol. Chem , vol.271 , pp. 11945-11952
    • Myette, J.R.1    Niles, E.G.2
  • 8
    • 31444440537 scopus 로고    scopus 로고
    • Energetics of RNA binding by the West Nile virus RNA triphosphatase
    • Benzaghou,I., Bougie,I., Picard-Jean,F. and Bisaillon,M. (2006) Energetics of RNA binding by the West Nile virus RNA triphosphatase. FEBS Lett., 580, 867-877.
    • (2006) FEBS Lett , vol.580 , pp. 867-877
    • Benzaghou, I.1    Bougie, I.2    Picard-Jean, F.3    Bisaillon, M.4
  • 9
    • 0034625437 scopus 로고    scopus 로고
    • Identification of a novel function of the alphavirus capping apparatus. RNA 5′-triphosphatase activity of Nsp2
    • Vasiljeva,L., Merits,A., Auvinen,P. and Kaariainen,L. (2000) Identification of a novel function of the alphavirus capping apparatus. RNA 5′-triphosphatase activity of Nsp2. J. Biol. Chem., 275 17281-17287.
    • (2000) J. Biol. Chem , vol.275 , pp. 17281-17287
    • Vasiljeva, L.1    Merits, A.2    Auvinen, P.3    Kaariainen, L.4
  • 10
    • 0029817880 scopus 로고    scopus 로고
    • Expression and characterization of an RNA capping enzyme encoded by Chlorella virus PBCV-1
    • Ho,C.K., Van Etten,J.L. and Shuman,S. (1996) Expression and characterization of an RNA capping enzyme encoded by Chlorella virus PBCV-1. J. Virol., 70, 6658-6664.
    • (1996) J. Virol , vol.70 , pp. 6658-6664
    • Ho, C.K.1    Van Etten, J.L.2    Shuman, S.3
  • 11
    • 2542461026 scopus 로고    scopus 로고
    • The broad spectrum antiviral nucleoside ribavirin as a substrate for a viral RNA capping enzyme
    • Bougie,I. and Bisaillon,M. (2004) The broad spectrum antiviral nucleoside ribavirin as a substrate for a viral RNA capping enzyme. J. Biol. Chem., 279, 22124-22130.
    • (2004) J. Biol. Chem , vol.279 , pp. 22124-22130
    • Bougie, I.1    Bisaillon, M.2
  • 12
    • 26444479397 scopus 로고    scopus 로고
    • Inhibitors of respiratory syncytial virus replication target cotranscriptional mRNA guanylylation by viral RNA-dependent RNA polymerase
    • Liuzzi,M., Mason,S.W., Cartier,M., Lawetz,C., Mccollum,R.S., Dansereau,N., Bolger,G., Lapeyre,N., Gaudette,Y. et al. (2005) Inhibitors of respiratory syncytial virus replication target cotranscriptional mRNA guanylylation by viral RNA-dependent RNA polymerase. J. Virol., 79, 13105-13115.
    • (2005) J. Virol , vol.79 , pp. 13105-13115
    • Liuzzi, M.1    Mason, S.W.2    Cartier, M.3    Lawetz, C.4    Mccollum, R.S.5    Dansereau, N.6    Bolger, G.7    Lapeyre, N.8    Gaudette, Y.9
  • 13
    • 0032545284 scopus 로고    scopus 로고
    • Yeast and viral RNA 5′ triphosphatases comprise a new nucleoside triphosphatase family
    • Ho,C.K., Pei,Y. and Shuman,S. (1998) Yeast and viral RNA 5′ triphosphatases comprise a new nucleoside triphosphatase family. J. Biol. Chem., 273, 34151-34156.
    • (1998) J. Biol. Chem , vol.273 , pp. 34151-34156
    • Ho, C.K.1    Pei, Y.2    Shuman, S.3
  • 14
    • 0034634475 scopus 로고    scopus 로고
    • Mechanism of phosphoanhydride cleavage by baculovirus phosphatase
    • Martins,A. and Shuman,S. (2000) Mechanism of phosphoanhydride cleavage by baculovirus phosphatase. J. Biol. Chem., 275, 35070-35076.
    • (2000) J. Biol. Chem , vol.275 , pp. 35070-35076
    • Martins, A.1    Shuman, S.2
  • 15
    • 0031820701 scopus 로고    scopus 로고
    • Characterization of a baculovirus-encoded RNA 5′-triphosphatase
    • Gross,C.H. and Shuman,S. (1998) Characterization of a baculovirus-encoded RNA 5′-triphosphatase. J. Virol., 72, 7057-7063.
    • (1998) J. Virol , vol.72 , pp. 7057-7063
    • Gross, C.H.1    Shuman, S.2
  • 16
    • 0021645897 scopus 로고    scopus 로고
    • Itoh,N., Mizumoto,K. and Kaziro,Y. (1984) Messenger RNA guanlyltransferase from Saccharomyces cerevisiae. Catalytic properties. J. Biol. Chem., b259, 13930-13936.
    • Itoh,N., Mizumoto,K. and Kaziro,Y. (1984) Messenger RNA guanlyltransferase from Saccharomyces cerevisiae. Catalytic properties. J. Biol. Chem., b259, 13930-13936.
  • 17
    • 0025315981 scopus 로고
    • Catalytic activity of vaccinia mRNA capping enzyme subunits coexpressed in Escherichia coli
    • Shuman,S. (1990) Catalytic activity of vaccinia mRNA capping enzyme subunits coexpressed in Escherichia coli. J. Biol. Chem., 265 11960-11966.
    • (1990) J. Biol. Chem , vol.265 , pp. 11960-11966
    • Shuman, S.1
  • 18
    • 0032508492 scopus 로고    scopus 로고
    • Isolation and characterization of the Candida albicans gene for mRNA 5′-triphosphatase: Association of mRNA 5′-triphosphatase and mRNA 5′-guanylyltransferase activities is essential for the function of mRNA 5′-capping enzyme in vivo
    • Yamada-Okabe,T., Mio,T., Matsui,M., Kashima,Y., Arisawa,M. and Yamada-Okabe,H. (1998) Isolation and characterization of the Candida albicans gene for mRNA 5′-triphosphatase: Association of mRNA 5′-triphosphatase and mRNA 5′-guanylyltransferase activities is essential for the function of mRNA 5′-capping enzyme in vivo. FEBS Lett., 435, 49-54.
    • (1998) FEBS Lett , vol.435 , pp. 49-54
    • Yamada-Okabe, T.1    Mio, T.2    Matsui, M.3    Kashima, Y.4    Arisawa, M.5    Yamada-Okabe, H.6
  • 19
    • 0033601125 scopus 로고    scopus 로고
    • Structure and mechanism of yeast RNA triphosphatase: An essential component of the mRNA capping apparatus
    • Lima,C.D., Wang,L.K. and Shuman,S. (1999) Structure and mechanism of yeast RNA triphosphatase: An essential component of the mRNA capping apparatus. Cell, 99, 533-543.
    • (1999) Cell , vol.99 , pp. 533-543
    • Lima, C.D.1    Wang, L.K.2    Shuman, S.3
  • 20
    • 0035873620 scopus 로고    scopus 로고
    • Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme
    • Changela,A., Ho,C.K., Martins,A., Shuman,S. and Mondragon,A. (2001) Structure and mechanism of the RNA triphosphatase component of mammalian mRNA capping enzyme. EMBO J., 20, 2575-2586.
    • (2001) EMBO J , vol.20 , pp. 2575-2586
    • Changela, A.1    Ho, C.K.2    Martins, A.3    Shuman, S.4    Mondragon, A.5
  • 21
    • 24044463223 scopus 로고    scopus 로고
    • Crystal structure of baculovirus RNA triphosphatase complexed with phosphate
    • Changela,A., Martins,A., Shuman,S. and Mondragon,A. (2005) Crystal structure of baculovirus RNA triphosphatase complexed with phosphate. J. Biol. Chem., 280, 17848-17856.
    • (2005) J. Biol. Chem , vol.280 , pp. 17848-17856
    • Changela, A.1    Martins, A.2    Shuman, S.3    Mondragon, A.4
  • 23
    • 0035139064 scopus 로고    scopus 로고
    • RNA triphosphatase component of the mRNA capping apparatus of Paramecium bursaria Chlorella virus 1
    • Ho,C.K., Gong,C. and Shuman,S. (2001) RNA triphosphatase component of the mRNA capping apparatus of Paramecium bursaria Chlorella virus 1. J. Virol., 75, 1744-1750.
    • (2001) J. Virol , vol.75 , pp. 1744-1750
    • Ho, C.K.1    Gong, C.2    Shuman, S.3
  • 24
    • 0037013218 scopus 로고    scopus 로고
    • Chlorella virus RNA triphosphatase. Mutational analysis and mechanism of inhibition by tripolyphosphate
    • Gong,C. and Shuman,S. (2002) Chlorella virus RNA triphosphatase. Mutational analysis and mechanism of inhibition by tripolyphosphate. J. Biol. Chem., 277, 15317-15324.
    • (2002) J. Biol. Chem , vol.277 , pp. 15317-15324
    • Gong, C.1    Shuman, S.2
  • 25
    • 0141818000 scopus 로고    scopus 로고
    • Investigating the role of metal ions in the catalytic mechanism of the yeast RNA triphosphatase
    • Bisaillon,M. and Bougie,I. (2003) Investigating the role of metal ions in the catalytic mechanism of the yeast RNA triphosphatase. J. Biol. Chem., 278, 33963-33971.
    • (2003) J. Biol. Chem , vol.278 , pp. 33963-33971
    • Bisaillon, M.1    Bougie, I.2
  • 26
    • 33748752792 scopus 로고    scopus 로고
    • Inhibition of a metal-dependent viral RNA triphosphatase by decavanadate
    • Bougie,I. and Bisaillon,M. (2006) Inhibition of a metal-dependent viral RNA triphosphatase by decavanadate. Biochem. J., 398, 557-567.
    • (2006) Biochem. J , vol.398 , pp. 557-567
    • Bougie, I.1    Bisaillon, M.2
  • 27
    • 0029156116 scopus 로고
    • Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding
    • Pace,C.N. (1995) Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding. Methods Enzymol., 259 538-554.
    • (1995) Methods Enzymol , vol.259 , pp. 538-554
    • Pace, C.N.1
  • 28
    • 0019593952 scopus 로고
    • Fluorescence quenching studies with proteins
    • Eftink,M.R. and Ghiron,C.A. (1981) Fluorescence quenching studies with proteins. Anal. Biochem., 114, 199-227.
    • (1981) Anal. Biochem , vol.114 , pp. 199-227
    • Eftink, M.R.1    Ghiron, C.A.2
  • 29
    • 0033615637 scopus 로고    scopus 로고
    • Thermodynamic analyses, reveal role of water release in epitope recognition by a monoclonal antibody against the human guanylyl cyclase C receptor
    • Swaminathan,C.P., Nandi,A., Visweswariah,S.S. and Surolia,A. (1999) Thermodynamic analyses, reveal role of water release in epitope recognition by a monoclonal antibody against the human guanylyl cyclase C receptor. J. Biol. Chem., 274, 31272-31278.
    • (1999) J. Biol. Chem , vol.274 , pp. 31272-31278
    • Swaminathan, C.P.1    Nandi, A.2    Visweswariah, S.S.3    Surolia, A.4
  • 30
    • 0025998147 scopus 로고    scopus 로고
    • Painter,G.R., WrightL.L., Hopkins,S. and Furman,P.A. (1991) Initial binding of 2′-deoxynucleoside 5′-triphosphates to human immunodeficiency virus type 1 reverse transcriptase. J. Biol. Chem. 266, 19362-19368.
    • Painter,G.R., WrightL.L., Hopkins,S. and Furman,P.A. (1991) Initial binding of 2′-deoxynucleoside 5′-triphosphates to human immunodeficiency virus type 1 reverse transcriptase. J. Biol. Chem. 266, 19362-19368.
  • 32
    • 0021114740 scopus 로고
    • Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence
    • Caloun,D.B., Vanderkoii,J.M. and Englander,S.W. (1983) Penetration of small molecules into proteins studied by quenching of phosphorescence and fluorescence. Biochemistry, 22, 1533-1539.
    • (1983) Biochemistry , vol.22 , pp. 1533-1539
    • Caloun, D.B.1    Vanderkoii, J.M.2    Englander, S.W.3
  • 33
    • 0035907366 scopus 로고    scopus 로고
    • Structure-function analysis of the active site tunnel of yeast RNA triphosphatase
    • Bisaillon,M. and Shuman,S. (2001) Structure-function analysis of the active site tunnel of yeast RNA triphosphatase. J. Biol. Chem., 276, 17261-17266.
    • (2001) J. Biol. Chem , vol.276 , pp. 17261-17266
    • Bisaillon, M.1    Shuman, S.2
  • 34
    • 0019241817 scopus 로고
    • The thermodynamics of nucleotide binding to proteins
    • Beaudette,N.V. and Langerman,N. (1980) The thermodynamics of nucleotide binding to proteins. Crit. Rev. Biochem., 9, 145-169.
    • (1980) Crit. Rev. Biochem , vol.9 , pp. 145-169
    • Beaudette, N.V.1    Langerman, N.2
  • 35
    • 0032479045 scopus 로고    scopus 로고
    • Role of water in the specific binding of mannose and mannooligosaccharides to Concanavalin A
    • Swaminathan,C.P., Surolia,N. and Surolia,A. (1998) Role of water in the specific binding of mannose and mannooligosaccharides to Concanavalin A. J. Am. Chem. Soc., 120, 5153-5159.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 5153-5159
    • Swaminathan, C.P.1    Surolia, N.2    Surolia, A.3
  • 36
    • 0029130871 scopus 로고
    • Macromolecules and water: Probing with osmotic stress
    • Parsegian,V.A., Rand,R.P. and Rau,D.C. (1995) Macromolecules and water: probing with osmotic stress. Methods Enzymol., 259, 43-94.
    • (1995) Methods Enzymol , vol.259 , pp. 43-94
    • Parsegian, V.A.1    Rand, R.P.2    Rau, D.C.3
  • 37
    • 0004448739 scopus 로고
    • Protein dynamics: Hydration, temperature, and solvent viscosity effects as revealed by Rayleigh scattering of Mossbauer radiation
    • Gregory,R.H, ed, Marcel Dekker Inc, NY, pp
    • Goldanskii,V.I. and Krupyanskii,Y.F. (1995) Protein dynamics: Hydration, temperature, and solvent viscosity effects as revealed by Rayleigh scattering of Mossbauer radiation. In Gregory,R.H. (ed), Protein-Solvent Interactions. Marcel Dekker Inc., NY, pp. 289-326.
    • (1995) Protein-Solvent Interactions , pp. 289-326
    • Goldanskii, V.I.1    Krupyanskii, Y.F.2
  • 38
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff,S.N. (1993) The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct., 22, 67-97.
    • (1993) Annu. Rev. Biophys. Biomol. Struct , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 39
    • 0028071439 scopus 로고
    • Arc repressor will not denature under pressure in the absence of water
    • Oliveira,A.C., Gaspar,L.P., Da Poian,A.T. and Silva,J.L. (1994) Arc repressor will not denature under pressure in the absence of water. J. Mol. Biol., 240, 184-187.
    • (1994) J. Mol. Biol , vol.240 , pp. 184-187
    • Oliveira, A.C.1    Gaspar, L.P.2    Da Poian, A.T.3    Silva, J.L.4
  • 40
    • 0030028764 scopus 로고    scopus 로고
    • Glycerol decreases the volume and compressibility of protein interior
    • Priev,A., Almagor,A., Yedgar,S. and Gavish,B. (1996) Glycerol decreases the volume and compressibility of protein interior. Biochemistry, 35, 2061-2066.
    • (1996) Biochemistry , vol.35 , pp. 2061-2066
    • Priev, A.1    Almagor, A.2    Yedgar, S.3    Gavish, B.4
  • 41
    • 0014690424 scopus 로고
    • Changes in ultraviolet absorption produced by alteration of protein conformation
    • Donovan,J.W. (1969) Changes in ultraviolet absorption produced by alteration of protein conformation. J. Biol. Chem., 244, 1961-1967.
    • (1969) J. Biol. Chem , vol.244 , pp. 1961-1967
    • Donovan, J.W.1
  • 42
    • 0037337254 scopus 로고    scopus 로고
    • Mapping the triphosphatase active site of baculovirus mRNA capping enzyme LEF-4 and evidence for a two-metal mechanism
    • Martins,A. and Shuman,S. (2001) Mapping the triphosphatase active site of baculovirus mRNA capping enzyme LEF-4 and evidence for a two-metal mechanism. Nucleic Acids Res., 31, 1455-1463.
    • (2001) Nucleic Acids Res , vol.31 , pp. 1455-1463
    • Martins, A.1    Shuman, S.2
  • 43
    • 0347065370 scopus 로고    scopus 로고
    • Structure-function analysis of Trypanosoma brucei RNA triphosphatase and evidence for a two-metal mechanism
    • Gong,C., Martins,A. and Shuman,S. (2003) Structure-function analysis of Trypanosoma brucei RNA triphosphatase and evidence for a two-metal mechanism. J. Biol. Chem., 278, 50843-50852.
    • (2003) J. Biol. Chem , vol.278 , pp. 50843-50852
    • Gong, C.1    Martins, A.2    Shuman, S.3
  • 44
    • 33748329366 scopus 로고    scopus 로고
    • Divalent metal requirements for catalysis and stability of the RNA triphosphatase from Trypanosoma cruzi
    • Kikuti,C.M., Tersariol,I.L.S. and Schenkman,S. (2006) Divalent metal requirements for catalysis and stability of the RNA triphosphatase from Trypanosoma cruzi. Mol. Biochem. Parasitol., 150, 83-95.
    • (2006) Mol. Biochem. Parasitol , vol.150 , pp. 83-95
    • Kikuti, C.M.1    Tersariol, I.L.S.2    Schenkman, S.3


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