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Volumn 99, Issue 5, 1999, Pages 533-543

Structure and mechanism of yeast RNA triphosphatase: An essential component of the mRNA capping apparatus

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PHOSPHATASE;

EID: 0033601125     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81541-X     Document Type: Article
Times cited : (118)

References (42)
  • 1
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial F1 ATPase
    • Abrahams, J.P., and Leslie, A.G.W. (1996). Methods used in the structure determination of bovine mitochondrial F1 ATPase. Acta Crystallogr. D 52, 30-42.
    • (1996) Acta Crystallogr. D , vol.52 , pp. 30-42
    • Abrahams, J.P.1    Leslie, A.G.W.2
  • 2
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A.T. (1992). The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature 355, 472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.T.1
  • 3
    • 0023140814 scopus 로고
    • Crystallographic R factor refinement by molecular dynamics
    • Brünger, A.T., Kuriyan, J., and Karplus, M. (1987). Crystallographic R factor refinement by molecular dynamics. Science 235, 458-460.
    • (1987) Science , vol.235 , pp. 458-460
    • Brünger, A.T.1    Kuriyan, J.2    Karplus, M.3
  • 4
    • 0031453408 scopus 로고    scopus 로고
    • MRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxyl-terminal domain
    • Cho, E., Takagi, T., Moore, C.R., and Buratowski, S. (1997). mRNA capping enzyme is recruited to the transcription complex by phosphorylation of the RNA polymerase II carboxyl-terminal domain. Genes Dev. 11, 3319-3326.
    • (1997) Genes Dev. , vol.11 , pp. 3319-3326
    • Cho, E.1    Takagi, T.2    Moore, C.R.3    Buratowski, S.4
  • 5
    • 0032533898 scopus 로고    scopus 로고
    • Allosteric interactions between capping enzyme subunits and the RNA polymerase II carboxyl-terminal domain
    • Cho, E., Rodriguez, C.R., Takagi, T., and Buratowski, S. (1998). Allosteric interactions between capping enzyme subunits and the RNA polymerase II carboxyl-terminal domain. Genes Dev. 12, 3482-3487.
    • (1998) Genes Dev. , vol.12 , pp. 3482-3487
    • Cho, E.1    Rodriguez, C.R.2    Takagi, T.3    Buratowski, S.4
  • 6
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 7
    • 0027609916 scopus 로고
    • SETOR: Hardware-lighted three-dimensional solid model representations of macromolecules
    • Evans, S.V. (1993). SETOR: hardware-lighted three-dimensional solid model representations of macromolecules. J. Mol. Graph. 11, 134-138.
    • (1993) J. Mol. Graph. , vol.11 , pp. 134-138
    • Evans, S.V.1
  • 8
    • 0031772992 scopus 로고    scopus 로고
    • RNA5′-triphosphatase, nucleoside triphosphatase, and guanylyltransferase activities of baculovirus LEF-4 protein
    • Gross, C.H., and Shuman, S. (1998). RNA5′-triphosphatase, nucleoside triphosphatase, and guanylyltransferase activities of baculovirus LEF-4 protein. J. Virol. 72, 10020-10028.
    • (1998) J. Virol. , vol.72 , pp. 10020-10028
    • Gross, C.H.1    Shuman, S.2
  • 9
    • 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., and Wigley, D.B. (1997). X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes. Cell 89, 545-553.
    • (1997) Cell , vol.89 , pp. 545-553
    • Hakansson, K.1    Doherty, A.J.2    Shuman, S.3    Wigley, D.B.4
  • 10
    • 3543026832 scopus 로고    scopus 로고
    • Genetic, physical, and functional interactions between the triphosphatase and guanylyltransferase components of the yeast mRNA capping apparatus
    • Ho, C.K., Schwer, B., and Shuman, S. (1998a). Genetic, physical, and functional interactions between the triphosphatase and guanylyltransferase components of the yeast mRNA capping apparatus. Mol. Cell. Biol. 18, 5189-5198.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5189-5198
    • Ho, C.K.1    Schwer, B.2    Shuman, S.3
  • 11
    • 0032540231 scopus 로고    scopus 로고
    • The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II
    • Ho, C.K., Sriskanda, V., McCracken, S., Bentley, D., Schwer, B., and Shuman, S. (1998b). The guanylyltransferase domain of mammalian mRNA capping enzyme binds to the phosphorylated carboxyl-terminal domain of RNA polymerase II. J. Biol. Chem. 273, 9577-9585.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9577-9585
    • Ho, C.K.1    Sriskanda, V.2    McCracken, S.3    Bentley, D.4    Schwer, B.5    Shuman, S.6
  • 12
    • 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. (1998c). 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
  • 13
    • 0033572891 scopus 로고    scopus 로고
    • An essential surface motif (WAQKW) of yeast RNA triphosphatase mediates formation of the mRNA capping enzyme complex with RNA guanylyltransferase
    • in press
    • Ho, C.K., Lehman, K., and Shuman, S. (1999). An essential surface motif (WAQKW) of yeast RNA triphosphatase mediates formation of the mRNA capping enzyme complex with RNA guanylyltransferase. Nucleic Acids Res., in press.
    • (1999) Nucleic Acids Res.
    • Ho, C.K.1    Lehman, K.2    Shuman, S.3
  • 14
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distant matrices
    • Holm, L., and Sander, C. (1993). Protein structure comparison by alignment of distant matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 15
    • 0033529716 scopus 로고    scopus 로고
    • Structure of the DNA repair enzyme endonuclease IV and its DNA complex: Double-nucleotide flipping at abasic sites and three-metal-ion catalysis
    • Hosfield, D.J., Guan, Y., Haas, B.J., Cunningham, R.J., and Tainer, U.A. (1999). Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis. Cell 98, 397-408.
    • (1999) Cell , vol.98 , pp. 397-408
    • Hosfield, D.J.1    Guan, Y.2    Haas, B.J.3    Cunningham, R.J.4    Tainer, U.A.5
  • 16
    • 0031775225 scopus 로고    scopus 로고
    • The LEF-4 subunit of baculovirus RNA polymerase has RNA 5′-triphosphatase and ATPase activities
    • Jin, J., Dong, W., and Guarino, L.A. (1998). The LEF-4 subunit of baculovirus RNA polymerase has RNA 5′-triphosphatase and ATPase activities. J. Virol. 72, 10011-10019.
    • (1998) J. Virol. , vol.72 , pp. 10011-10019
    • Jin, J.1    Dong, W.2    Guarino, L.A.3
  • 17
    • 0000127585 scopus 로고
    • Automated refinement of protein models
    • Lamzin, V.S., and Wilson, K.S. (1993). Automated refinement of protein models. Acta Crystallogr. D 49, 129-149.
    • (1993) Acta Crystallogr. D , vol.49 , pp. 129-149
    • Lamzin, V.S.1    Wilson, K.S.2
  • 18
    • 0033529501 scopus 로고    scopus 로고
    • A conserved domain of yeast RNA triphosphatase flanking the catalytic core regulates self-association and interaction with the guanylyltransferase component of the mRNA capping apparatus
    • Lehman, K., Schwer, B., Ho, C.K., Rouzankina, I., and Shuman, S. (1999). A conserved domain of yeast RNA triphosphatase flanking the catalytic core regulates self-association and interaction with the guanylyltransferase component of the mRNA capping apparatus. J. Biol. Chem. 274, 22668-22678.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22668-22678
    • Lehman, K.1    Schwer, B.2    Ho, C.K.3    Rouzankina, I.4    Shuman, S.5
  • 19
    • 0030060410 scopus 로고    scopus 로고
    • Mutational analysis of the Saccharomyces cerevisiae ABD1 gene: Cap methyltransferase activity is essential for cell growth
    • Mao, X., Schwer, B., and Shuman, S. (1996). Mutational analysis of the Saccharomyces cerevisiae ABD1 gene: cap methyltransferase activity is essential for cell growth. Mol. Cell. Biol. 16, 475-480.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 475-480
    • Mao, X.1    Schwer, B.2    Shuman, S.3
  • 21
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N., Vagin, A.A., and Dodson, E.J. (1997). Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D 53, 240-255.
    • (1997) Acta Crystallogr. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 22
    • 0028961335 scopus 로고
    • Scop: A structural classification of proteins database for the investigation of sequences and structures
    • Murzin, A.G., Brenner, S.E., Hubbard, T., and Chothia, C. (1995). scop: a structural classification of proteins database for the investigation of sequences and structures. J. Mol. Biol. 247, 536-540.
    • (1995) J. Mol. Biol. , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 23
    • 84920325457 scopus 로고
    • AmoRe: An automated package for molecular replacement
    • Navaza, J. (1994). AmoRe: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163.
    • (1994) Acta Crystallogr. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 24
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 0032849895 scopus 로고    scopus 로고
    • Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus
    • Pei, Y., Ho, C.K., Schwer, B., and Shuman, S. (1999). Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus. J. Biol. Chem. 274, 28865-28874.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28865-28874
    • Pei, Y.1    Ho, C.K.2    Schwer, B.3    Shuman, S.4
  • 27
    • 0033562339 scopus 로고    scopus 로고
    • A Saccharomyces cerevisiae RNA 5′-triphosphatase related to mRNA capping enzyme
    • Rodriguez, C.R., Takagi, T., Cho, E., and Buratowski, S. (1999). A Saccharomyces cerevisiae RNA 5′-triphosphatase related to mRNA capping enzyme. Nucleic Acids. Res. 27, 2182-2188.
    • (1999) Nucleic Acids. Res. , vol.27 , pp. 2182-2188
    • Rodriguez, C.R.1    Takagi, T.2    Cho, E.3    Buratowski, S.4
  • 28
    • 0028211258 scopus 로고
    • Mutational analysis of yeast mRNA capping enzyme
    • Schwer, B., and Shuman, S. (1994). Mutational analysis of yeast mRNA capping enzyme. Proc. Natl. Acad. Sci. USA 91, 4328-4332.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4328-4332
    • Schwer, B.1    Shuman, S.2
  • 29
    • 0026733001 scopus 로고
    • MRNA capping enzyme: Isolation and characterization of the gene encoding mRNA guanylyltransferase subunit from Saccharomyces cerevisiae
    • Shibagaki, Y., Itoh, N., Yamada, H., Nagata, S., and Mizumoto, K. (1992). mRNA capping enzyme: isolation and characterization of the gene encoding mRNA guanylyltransferase subunit from Saccharomyces cerevisiae. J. Biol. Chem. 267, 9521-9528.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9521-9528
    • Shibagaki, Y.1    Itoh, N.2    Yamada, H.3    Nagata, S.4    Mizumoto, K.5
  • 30
    • 0029107231 scopus 로고
    • Capping enzyme in eukaryotic mRNA synthesis
    • Shuman, S. (1995). Capping enzyme in eukaryotic mRNA synthesis. Prog. Nucleic Acid Res. Mol. Biol. 50, 101-129.
    • (1995) Prog. Nucleic Acid Res. Mol. Biol. , vol.50 , pp. 101-129
    • Shuman, S.1
  • 31
    • 0000262312 scopus 로고
    • Mechanism of mRNA capping by vaccinia virus guanylyltransferase: Characterization of an enzyme-guanylate intermediate
    • Shuman, S., and Hurwitz, J. (1981). Mechanism of mRNA capping by vaccinia virus guanylyltransferase: characterization of an enzyme-guanylate intermediate. Proc. Natl. Acad. Sci. USA 78, 187-191.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 187-191
    • Shuman, S.1    Hurwitz, J.2
  • 32
    • 0029056990 scopus 로고
    • RNA capping enzyme and DNA ligase - A super-family of covalent nucleotidyl transferases
    • Shuman, S., and Schwer, B. (1995). RNA capping enzyme and DNA ligase - a super-family of covalent nucleotidyl transferases. Mol. Microbiol. 17, 405-410.
    • (1995) Mol. Microbiol. , vol.17 , pp. 405-410
    • Shuman, S.1    Schwer, B.2
  • 33
    • 0029938467 scopus 로고    scopus 로고
    • Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7
    • Subramanya, H.S., Doherty, A.J., Ashford, S.R., and Wigley, D.B. (1996). Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell 85, 607-615.
    • (1996) Cell , vol.85 , pp. 607-615
    • Subramanya, H.S.1    Doherty, A.J.2    Ashford, S.R.3    Wigley, D.B.4
  • 34
    • 0030807902 scopus 로고    scopus 로고
    • An RNA5′-triphosphatase related to the protein tyrosine phosphatases
    • Takagi, T., Moore, C.R., Diehn, F., and Buratowski, S. (1997). An RNA5′-triphosphatase related to the protein tyrosine phosphatases. Cell 89, 867-873.
    • (1997) Cell , vol.89 , pp. 867-873
    • Takagi, T.1    Moore, C.R.2    Diehn, F.3    Buratowski, S.4
  • 35
    • 0033119895 scopus 로고    scopus 로고
    • Automated MAD and MIR structure solution
    • Terwilliger, T.C., and Berendzen, J. (1999). Automated MAD and MIR structure solution. Acta Crystallogr. D 55, 849-861.
    • (1999) Acta Crystallogr. D , vol.55 , pp. 849-861
    • Terwilliger, T.C.1    Berendzen, J.2
  • 36
    • 0031561370 scopus 로고    scopus 로고
    • Isolation and characterization of the yeast mRNA capping enzyme β subunit gene encoding RNA 5′-triphosphatase, which is essential for cell viability
    • Tsukamoto, T., Shibagaki, Y., Imajoh-Ohmi, S., Murakoshi, T., Suzuki, M., Nakamura, A., Gotoh, H., and Mizumoto, K. (1997). Isolation and characterization of the yeast mRNA capping enzyme β subunit gene encoding RNA 5′-triphosphatase, which is essential for cell viability. Biochem. Biophys. Res. Comm. 239, 116-122.
    • (1997) Biochem. Biophys. Res. Comm. , vol.239 , pp. 116-122
    • Tsukamoto, T.1    Shibagaki, Y.2    Imajoh-Ohmi, S.3    Murakoshi, T.4    Suzuki, M.5    Nakamura, A.6    Gotoh, H.7    Mizumoto, K.8
  • 37
    • 0000643270 scopus 로고    scopus 로고
    • Structure-function analysis of the mRNA cap methyltransferase of Saccharomyces cerevisiae
    • Wang, S.P., and Shuman, S. (1997). Structure-function analysis of the mRNA cap methyltransferase of Saccharomyces cerevisiae. J. Biol. Chem. 272, 14683-14689.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14683-14689
    • Wang, S.P.1    Shuman, S.2
  • 39
    • 0032514620 scopus 로고    scopus 로고
    • Mammalian capping enzyme binds RNA and uses protein tyrosine phosphatase mechanism
    • Wen, Y., Yue, Z., and Shatkin, A.J. (1998). Mammalian capping enzyme binds RNA and uses protein tyrosine phosphatase mechanism. Proc. Natl. Acad. Sci. USA 95, 12226-12231.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12226-12231
    • Wen, Y.1    Yue, Z.2    Shatkin, A.J.3
  • 40
    • 0032508492 scopus 로고    scopus 로고
    • Isolation and characterization of the Candida albicans gene for mRNA 5′-triphosphatase: Association of mRNA 5′-triphosphatse and mRNA 5′-guanylytransferase 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′-triphosphatse and mRNA 5′-guanylytransferase 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
  • 41
    • 0030728958 scopus 로고    scopus 로고
    • Structure-function analysis of the triphosphatase component of vaccinia virus mRNA capping enzyme
    • Yu, L, Martins, A., Deng, L, and Shuman, S. (1997). Structure-function analysis of the triphosphatase component of vaccinia virus mRNA capping enzyme. J. Virol. 71, 9837-9843.
    • (1997) J. Virol. , vol.71 , pp. 9837-9843
    • Yu, L.1    Martins, A.2    Deng, L.3    Shuman, S.4
  • 42
    • 0030660264 scopus 로고    scopus 로고
    • Mammalian capping enzyme complements mutant S. cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II
    • Yue, Z., Maldonado, E., Pillutla, R., Cho, H., Reinberg, D., and Shatkin, A.J. (1997). Mammalian capping enzyme complements mutant S. cerevisiae lacking mRNA guanylyltransferase and selectively binds the elongating form of RNA polymerase II. Proc. Natl. Acad. Sci. USA 94, 12898-12903.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12898-12903
    • Yue, Z.1    Maldonado, E.2    Pillutla, R.3    Cho, H.4    Reinberg, D.5    Shatkin, A.J.6


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