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Volumn 47, Issue 47, 2008, Pages 12562-12573

Differential RNA-dependent ATPase activities of four rRNA processing yeast DEAD-box proteins

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BINDING SITES; BIOCHEMISTRY; ESCHERICHIA COLI; NUCLEIC ACIDS; OLIGONUCLEOTIDES; PROBABILITY DENSITY FUNCTION; RANGE FINDING; RNA; WATER POLLUTION; YEAST;

EID: 56749093106     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8016119     Document Type: Article
Times cited : (15)

References (80)
  • 1
    • 1542344429 scopus 로고    scopus 로고
    • DEAD-box proteins: The driving forces behind RNA metabolism
    • Rocak, S., and Linder, P. (2004) DEAD-box proteins: the driving forces behind RNA metabolism. Nat. Rev. Mol. Cell Biol. 5 (3), 232-41.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , Issue.3 , pp. 232-241
    • Rocak, S.1    Linder, P.2
  • 2
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • Cordin, O., Banroques, J., Tanner, N. K., and Linder, P. (2006) The DEAD-box protein family of RNA helicases. Gene 367, 17-37.
    • (2006) Gene , vol.367 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 3
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya, A. E., and Koonin, E. V. (1993) Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 3, 419-429.
    • (1993) Curr. Opin. Struct. Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 4
    • 0037252143 scopus 로고    scopus 로고
    • The Q motif: A newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis
    • Tanner, N. K., Cordin, O., Banroques, J., Doere, M., and Linder, P. (2003) The Q motif: a newly identified motif in DEAD box helicases may regulate ATP binding and hydrolysis. Mol. Cell 11 (1), 127-38.
    • (2003) Mol. Cell , vol.11 , Issue.1 , pp. 127-138
    • Tanner, N.K.1    Cordin, O.2    Banroques, J.3    Doere, M.4    Linder, P.5
  • 5
    • 0026584599 scopus 로고
    • Structure of the recA protein-ADP complex
    • Story, R. M., and Steitz, T. A. (1992) Structure of the recA protein-ADP complex. Nature 355, 374-376.
    • (1992) Nature , vol.355 , pp. 374-376
    • Story, R.M.1    Steitz, T.A.2
  • 7
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding
    • Kim, J. L., Morgenstern, K. A., Griffith, J. P., Dwyer, M. D., Thomson, J. A., Murcko, M. A., Lin, C., and Caron, P. R. (1998) Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: The crystal structure provides insights into the mode of unwinding. Structure 6, 89-100.
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lin, C.7    Caron, P.R.8
  • 8
    • 33646017369 scopus 로고    scopus 로고
    • Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa
    • Sengoku, T., Nureki, O., Nakamura, A., Kobayashi, S., and Yokoyama, S. (2006) Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell 125 (2), 287-300.
    • (2006) Cell , vol.125 , Issue.2 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 9
    • 27444442034 scopus 로고    scopus 로고
    • YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain
    • Karginov, F. V., Caruthers, J. M., Hu, Y., McKay, D. B., and Uhlenbeck, O. C. (2005) YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain. J. Biol. Chem. 280 (42), 35499-505.
    • (2005) J. Biol. Chem , vol.280 , Issue.42 , pp. 35499-35505
    • Karginov, F.V.1    Caruthers, J.M.2    Hu, Y.3    McKay, D.B.4    Uhlenbeck, O.C.5
  • 10
    • 0036927393 scopus 로고    scopus 로고
    • The carboxy-terminal domain of the DExDH protein YxiN is sufficient to confer specificity for 23S rRNA
    • Kossen, K., Karginov, F. V., and Uhlenbeck, O. C. (2002) The carboxy-terminal domain of the DExDH protein YxiN is sufficient to confer specificity for 23S rRNA. J. Mol. Biol. 324 (4), 625-36.
    • (2002) J. Mol. Biol , vol.324 , Issue.4 , pp. 625-636
    • Kossen, K.1    Karginov, F.V.2    Uhlenbeck, O.C.3
  • 11
    • 0141430073 scopus 로고    scopus 로고
    • DExD/H-box proteins and their partners: Helping RNA helicases unwind
    • Silverman, E., Edwalds-Gilbert, G., and Lin, R. J. (2003) DExD/H-box proteins and their partners: Helping RNA helicases unwind. Gene 312, 1-16.
    • (2003) Gene , vol.312 , pp. 1-16
    • Silverman, E.1    Edwalds-Gilbert, G.2    Lin, R.J.3
  • 12
    • 0035147544 scopus 로고    scopus 로고
    • A new twist on RNA helicases: DExH/D box proteins as RNPases
    • Schwer, B. (2001) A new twist on RNA helicases: DExH/D box proteins as RNPases. Nat. Struct. Biol. 8 (2), 113-6.
    • (2001) Nat. Struct. Biol , vol.8 , Issue.2 , pp. 113-116
    • Schwer, B.1
  • 13
    • 0035808566 scopus 로고    scopus 로고
    • Active disruption of an RNA-protein interaction by a DExH/D RNA helicase
    • Jankowsky, E., Gross, C. H., Shuman, S., and Pyle, A. M. (2001) Active disruption of an RNA-protein interaction by a DExH/D RNA helicase. Science 291 (5501), 121-5.
    • (2001) Science , vol.291 , Issue.5501 , pp. 121-125
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 14
    • 0035476705 scopus 로고    scopus 로고
    • Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA
    • Diges, C. M., and Uhlenbeck, O. C. (2001) Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA. EMBO J. 20, 5503-12.
    • (2001) EMBO J , vol.20 , pp. 5503-5512
    • Diges, C.M.1    Uhlenbeck, O.C.2
  • 15
    • 0034719392 scopus 로고    scopus 로고
    • The DExH protein NPH-II is a processive and directional motor for unwinding RNA
    • Jankowsky, E., Gross, C. H., Shuman, S., and Pyle, A. M. (2000) The DExH protein NPH-II is a processive and directional motor for unwinding RNA. Nature 403, 447-51.
    • (2000) Nature , vol.403 , pp. 447-451
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 16
    • 0013217441 scopus 로고    scopus 로고
    • Helicases as Molecular Motors
    • Schliwa, M, Ed, pp, Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany
    • Levin, M. K., and Patel, S. S. (2003) Helicases as Molecular Motors, in Molecular Motor (Schliwa, M., Ed.) pp 179-206, Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany.
    • (2003) Molecular Motor , pp. 179-206
    • Levin, M.K.1    Patel, S.S.2
  • 17
    • 0035150184 scopus 로고    scopus 로고
    • Unwinding the 'Gordian knot' of helicase action
    • Soultanas, P., and Wigley, D. B. (2001) Unwinding the 'Gordian knot' of helicase action. Trends Biochem. Sci. 26 (1), 47-54.
    • (2001) Trends Biochem. Sci , vol.26 , Issue.1 , pp. 47-54
    • Soultanas, P.1    Wigley, D.B.2
  • 18
    • 0028138413 scopus 로고
    • Single-turnover kinetics of helicase-catalyzed DNA unwinding monitored continuously by fluorescence energy transfer
    • Bjornson, K. P., Amaratunga, M., Moore, K. J., and Lohman, T. M. (1994) Single-turnover kinetics of helicase-catalyzed DNA unwinding monitored continuously by fluorescence energy transfer. Biochemistry 33 (47), 14306-14316.
    • (1994) Biochemistry , vol.33 , Issue.47 , pp. 14306-14316
    • Bjornson, K.P.1    Amaratunga, M.2    Moore, K.J.3    Lohman, T.M.4
  • 19
    • 38349186157 scopus 로고    scopus 로고
    • Mutation of the arginine finger in the active site of Escherichia coli DbpA abolishes ATPase and helicase activity and confers a dominant slow growth phenotype
    • Elles, L. M., and Uhlenbeck, O. C. (2008) Mutation of the arginine finger in the active site of Escherichia coli DbpA abolishes ATPase and helicase activity and confers a dominant slow growth phenotype. Nucleic Acids Res. 36 (1), 41-50.
    • (2008) Nucleic Acids Res , vol.36 , Issue.1 , pp. 41-50
    • Elles, L.M.1    Uhlenbeck, O.C.2
  • 20
    • 32044449843 scopus 로고    scopus 로고
    • Comprehensive mutational analysis of yeast DEXD/H box RNA helicases involved in large ribosomal subunit biogenesis
    • Bernstein, K. A., Granneman, S., Lee, A. V., Manickam, S., and Baserga, S. J. (2006) Comprehensive mutational analysis of yeast DEXD/H box RNA helicases involved in large ribosomal subunit biogenesis. Mol. Cell. Biol. 26 (4), 1195-208.
    • (2006) Mol. Cell. Biol , vol.26 , Issue.4 , pp. 1195-1208
    • Bernstein, K.A.1    Granneman, S.2    Lee, A.V.3    Manickam, S.4    Baserga, S.J.5
  • 21
    • 32044462969 scopus 로고    scopus 로고
    • Comprehensive mutational analysis of yeast DEXD/H box RNA helicases required for small ribosomal subunit synthesis
    • Granneman, S., Bernstein, K. A., Bleichert, F., and Baserga, S. J. (2006) Comprehensive mutational analysis of yeast DEXD/H box RNA helicases required for small ribosomal subunit synthesis. Mol. Cell. Biol. 26 (4), 1183-94.
    • (2006) Mol. Cell. Biol , vol.26 , Issue.4 , pp. 1183-1194
    • Granneman, S.1    Bernstein, K.A.2    Bleichert, F.3    Baserga, S.J.4
  • 22
    • 0035282868 scopus 로고    scopus 로고
    • Characterization and mutational analysis of yeast Dbp8p, a putative RNA helicase involved in ribosome biogenesis
    • Daugeron, M. C., and Linder, P. (2001) Characterization and mutational analysis of yeast Dbp8p, a putative RNA helicase involved in ribosome biogenesis. Nucleic Acids Res. 29 (5), 1144-55.
    • (2001) Nucleic Acids Res , vol.29 , Issue.5 , pp. 1144-1155
    • Daugeron, M.C.1    Linder, P.2
  • 23
    • 34147169852 scopus 로고    scopus 로고
    • Mutational analysis of the Escherichia coli DEAD box protein CsdA
    • Turner, A. M., Love, C. F., Alexander, R. W., and Jones, P. G. (2007) Mutational analysis of the Escherichia coli DEAD box protein CsdA. J. Bacteriol. 189 (7), 2769-76.
    • (2007) J. Bacteriol , vol.189 , Issue.7 , pp. 2769-2776
    • Turner, A.M.1    Love, C.F.2    Alexander, R.W.3    Jones, P.G.4
  • 24
    • 33344464450 scopus 로고    scopus 로고
    • Mutational analysis of human eIF4AIII identifies regions necessary for exon junction complex formation and nonsense-mediated mRNA decay
    • Shibuya, T., Tange, T. O., Stroupe, M. E., and Moore, M. J. (2006) Mutational analysis of human eIF4AIII identifies regions necessary for exon junction complex formation and nonsense-mediated mRNA decay. RNA 12 (3), 360-74.
    • (2006) RNA 12 , Issue.3 , pp. 360-374
    • Shibuya, T.1    Tange, T.O.2    Stroupe, M.E.3    Moore, M.J.4
  • 25
    • 0037124096 scopus 로고    scopus 로고
    • Prp43 is an essential RNA-dependent ATPase required for release of lariatintron from the spliceosome
    • Martin, A., Schneider, S., and Schwer, B. (2002) Prp43 is an essential RNA-dependent ATPase required for release of lariatintron from the spliceosome. J. Biol. Chem. 277 (20), 17743-50.
    • (2002) J. Biol. Chem , vol.277 , Issue.20 , pp. 17743-17750
    • Martin, A.1    Schneider, S.2    Schwer, B.3
  • 26
    • 14244260321 scopus 로고    scopus 로고
    • Characterization of the ATPase and unwinding activities of the yeast DEAD-box protein Has1p and the analysis of the roles of the conserved motifs
    • Rocak, S., Emery, B., Tanner, N. K., and Linder, P. (2005) Characterization of the ATPase and unwinding activities of the yeast DEAD-box protein Has1p and the analysis of the roles of the conserved motifs. Nucleic Acids Res. 33 (3), 999-1009.
    • (2005) Nucleic Acids Res , vol.33 , Issue.3 , pp. 999-1009
    • Rocak, S.1    Emery, B.2    Tanner, N.K.3    Linder, P.4
  • 27
    • 0033168965 scopus 로고    scopus 로고
    • ATP hydrolysis activity of the DEAD box protein Rok1p is required for in vivo ROK1 function
    • Oh, J., and Kim, J. (1999) ATP hydrolysis activity of the DEAD box protein Rok1p is required for in vivo ROK1 function. Nucleic Acids Res. 27, 2753-2759.
    • (1999) Nucleic Acids Res , vol.27 , pp. 2753-2759
    • Oh, J.1    Kim, J.2
  • 28
    • 0033509092 scopus 로고    scopus 로고
    • Protein transacting factors involved in ribosome biogenesis
    • Kressler, D., Linder, P., and de la Cruz, J. (1999) Protein transacting factors involved in ribosome biogenesis. Mol. Cell. Biol. 19, 7897-7912.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 7897-7912
    • Kressler, D.1    Linder, P.2    de la Cruz, J.3
  • 29
    • 12244283992 scopus 로고    scopus 로고
    • Economics of Ribosome Biosynthesis
    • Stillman, B, Ed, pp, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Warner, J. R., Vilardell, J., and Sohn, J. H. (2001) Economics of Ribosome Biosynthesis, in The Ribosome: Proceedings of 2001 Symposium LXVI (Stillman, B., Ed.) pp 567-74, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2001) The Ribosome: Proceedings of 2001 Symposium LXVI , pp. 567-574
    • Warner, J.R.1    Vilardell, J.2    Sohn, J.H.3
  • 30
    • 0033367325 scopus 로고    scopus 로고
    • Ribosome synthesis in Saccharomyces cerevisiae
    • Venema, J., and Tollervey, D. (1999) Ribosome synthesis in Saccharomyces cerevisiae. Annu. Rev. Genet. 33, 261-311.
    • (1999) Annu. Rev. Genet , vol.33 , pp. 261-311
    • Venema, J.1    Tollervey, D.2
  • 31
    • 0033133863 scopus 로고    scopus 로고
    • Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families
    • de la Cruz, J., Kressler, D., and Linder, P. (1999) Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families. Trends Biochem. Sci. 24, 192-198.
    • (1999) Trends Biochem. Sci , vol.24 , pp. 192-198
    • de la Cruz, J.1    Kressler, D.2    Linder, P.3
  • 32
    • 0038738334 scopus 로고    scopus 로고
    • Pre-ribosomes on the road from the nucleolus to the cytoplasm
    • Tschochner, H., and Hurt, E. (2003) Pre-ribosomes on the road from the nucleolus to the cytoplasm. Trends Cell Biol 13 (5), 255-63.
    • (2003) Trends Cell Biol , vol.13 , Issue.5 , pp. 255-263
    • Tschochner, H.1    Hurt, E.2
  • 33
    • 0031016682 scopus 로고    scopus 로고
    • Dbp3p, a putative RNA helicase in Saccharomyces cerevisiae is required for efficient pre-rRNA processing predominantly at site A3
    • Weaver, P. L., Sun, C., and Chang, T. (1997) Dbp3p, a putative RNA helicase in Saccharomyces cerevisiae is required for efficient pre-rRNA processing predominantly at site A3. Mol. Cell. Biol. 17, 1354-1365.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 1354-1365
    • Weaver, P.L.1    Sun, C.2    Chang, T.3
  • 34
    • 0028983910 scopus 로고
    • Birth of the snoRNPs: The evolution of RNase MRP and the eukaryotic pre-rRNA-processing system
    • Morrissey, J. P., and Tollervey, D. (1995) Birth of the snoRNPs: The evolution of RNase MRP and the eukaryotic pre-rRNA-processing system. Trends Biochem. Sci. 20 (2), 78-82.
    • (1995) Trends Biochem. Sci , vol.20 , Issue.2 , pp. 78-82
    • Morrissey, J.P.1    Tollervey, D.2
  • 35
    • 0028054796 scopus 로고
    • The RNA of RNase MRP is required for normal processing of ribosomal RNA
    • Chu, S., Archer, R. H., Zengel, J. M., and Lindahl, L. (1994) The RNA of RNase MRP is required for normal processing of ribosomal RNA. Proc. Natl. Acad. Sci. U.S.A. 91 (2), 659-63.
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , Issue.2 , pp. 659-663
    • Chu, S.1    Archer, R.H.2    Zengel, J.M.3    Lindahl, L.4
  • 36
    • 0029981894 scopus 로고    scopus 로고
    • Accurate processing of a eukaryotic precursor ribosomal RNA by ribonuclease MRP in vitro
    • Lygerou, Z., Allmang, C., Tollervey, D, and Seraphin, B. (1996) Accurate processing of a eukaryotic precursor ribosomal RNA by ribonuclease MRP in vitro. Science 272 (5259), 268-70.
    • (1996) Science , vol.272 , Issue.5259 , pp. 268-270
    • Lygerou, Z.1    Allmang, C.2    Tollervey, D.3    Seraphin, B.4
  • 37
    • 0023152084 scopus 로고
    • A mammalian mitochondrial RNA processing activity contains nucleus-encoded RNA
    • Chang, D. D., and Clayton, D. A. (1987) A mammalian mitochondrial RNA processing activity contains nucleus-encoded RNA. Science 235 (4793), 1178-84.
    • (1987) Science , vol.235 , Issue.4793 , pp. 1178-1184
    • Chang, D.D.1    Clayton, D.A.2
  • 38
    • 0030929129 scopus 로고    scopus 로고
    • The rRNA-processing function of the yeast U14 small nucleolar RNA can be rescued by a conserved RNA helicase-like protein
    • Liang, W. Q., Clark, J. A., and Fournier, M. J. (1997) The rRNA-processing function of the yeast U14 small nucleolar RNA can be rescued by a conserved RNA helicase-like protein. Mol. Cell. Biol. 17, 4124-4132.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 4124-4132
    • Liang, W.Q.1    Clark, J.A.2    Fournier, M.J.3
  • 39
    • 0031942702 scopus 로고    scopus 로고
    • The U14 snoRNA is required for 2′-O-methylation of the pre-18S rRNA in Xenopus oocytes
    • Dunbar, D. A., and Baserga, S. J. (1998) The U14 snoRNA is required for 2′-O-methylation of the pre-18S rRNA in Xenopus oocytes. RNA 4 (2), 195-204.
    • (1998) RNA , vol.4 , Issue.2 , pp. 195-204
    • Dunbar, D.A.1    Baserga, S.J.2
  • 40
    • 0028818298 scopus 로고
    • U14 base-pairs with 18S rRNA: A novel snoRNA interaction required for rRNA processing
    • Liang, W. Q., and Fournier, M. J. (1995) U14 base-pairs with 18S rRNA: a novel snoRNA interaction required for rRNA processing. Genes Dev. 9 (19), 2433-43.
    • (1995) Genes Dev , vol.9 , Issue.19 , pp. 2433-2443
    • Liang, W.Q.1    Fournier, M.J.2
  • 41
    • 0030738552 scopus 로고    scopus 로고
    • U14 small nucleolar RNA makes multiple contacts with the pre-ribosomal RNA
    • Morrissey, J. P., and Tollervey, D. (1997) U14 small nucleolar RNA makes multiple contacts with the pre-ribosomal RNA. Chromosoma 105 (7-8), 515-22.
    • (1997) Chromosoma , vol.105 , Issue.7-8 , pp. 515-522
    • Morrissey, J.P.1    Tollervey, D.2
  • 42
    • 25844432236 scopus 로고    scopus 로고
    • The Putative RNA Helicase Dbp4p Is Required for Release of the U14 snoRNA from Preribosomes in Saccharomyces cerevisiae
    • Kos, M., and Tollervey, D. (2005) The Putative RNA Helicase Dbp4p Is Required for Release of the U14 snoRNA from Preribosomes in Saccharomyces cerevisiae. Mol. Cell 20 (1), 53-64.
    • (2005) Mol. Cell , vol.20 , Issue.1 , pp. 53-64
    • Kos, M.1    Tollervey, D.2
  • 44
    • 0030771087 scopus 로고    scopus 로고
    • Small nucleolar RNAs direct site-specific synthesis of pseudouridine in ribosomal RNA
    • Ni, J., Tien, A. L., and Fournier, M. J. (1997) Small nucleolar RNAs direct site-specific synthesis of pseudouridine in ribosomal RNA. Cell 89 (4), 565-73.
    • (1997) Cell , vol.89 , Issue.4 , pp. 565-573
    • Ni, J.1    Tien, A.L.2    Fournier, M.J.3
  • 45
    • 0032894591 scopus 로고    scopus 로고
    • A comprehensive database for the small nucleolar RNAs from Saccharomyces cerevisiae
    • Samarsky, D. A., and Fournier, M. J. (1999) A comprehensive database for the small nucleolar RNAs from Saccharomyces cerevisiae. Nucleic Acids Res. 27 (1), 161-4.
    • (1999) Nucleic Acids Res , vol.27 , Issue.1 , pp. 161-164
    • Samarsky, D.A.1    Fournier, M.J.2
  • 46
    • 0023661309 scopus 로고
    • A yeast small nuclear RNA is required for normal processing of pre-ribosomal RNA
    • Tollervey, D. (1987) A yeast small nuclear RNA is required for normal processing of pre-ribosomal RNA. EMBO J. 6 (13), 4169-75.
    • (1987) EMBO J , vol.6 , Issue.13 , pp. 4169-4175
    • Tollervey, D.1
  • 47
    • 0029736818 scopus 로고    scopus 로고
    • 18S rRNA processing requires the RNA helicase-like protein Rrp3
    • O'Day, C., Chavanikamannil, F., and Abelson, J. (1996) 18S rRNA processing requires the RNA helicase-like protein Rrp3. Nucleic Acids Res. 24, 3201-3207.
    • (1996) Nucleic Acids Res , vol.24 , pp. 3201-3207
    • O'Day, C.1    Chavanikamannil, F.2    Abelson, J.3
  • 48
    • 0032387820 scopus 로고    scopus 로고
    • Kinetic analysis of the RNA-dependent adenosine triphosphatase activity of DbpA, an Escherichia coli DEAD protein specific for 23S ribosomal RNA
    • Tsu, C. A., and Uhlenbeck, O. C. (1998) Kinetic analysis of the RNA-dependent adenosine triphosphatase activity of DbpA, an Escherichia coli DEAD protein specific for 23S ribosomal RNA. Biochemistry 37, 16989-16996.
    • (1998) Biochemistry , vol.37 , pp. 16989-16996
    • Tsu, C.A.1    Uhlenbeck, O.C.2
  • 50
    • 0030475009 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Prp5 protein has RNA-dependent ATPase activity with specificity for U2 small nuclear RNA
    • O'Day, C. L., Dalbadie-McFarland, G., and Abelson, J. (1996) The Saccharomyces cerevisiae Prp5 protein has RNA-dependent ATPase activity with specificity for U2 small nuclear RNA. J. Biol. Chem. 271 (52), 33261-7.
    • (1996) J. Biol. Chem , vol.271 , Issue.52 , pp. 33261-33267
    • O'Day, C.L.1    Dalbadie-McFarland, G.2    Abelson, J.3
  • 51
    • 0027905034 scopus 로고
    • Molecular mechanism of transcription-repair coupling
    • Selby, C. P., and Sancar, A. (1993) Molecular mechanism of transcription-repair coupling. Science 260 (5104), 53-8.
    • (1993) Science , vol.260 , Issue.5104 , pp. 53-58
    • Selby, C.P.1    Sancar, A.2
  • 52
    • 0029809505 scopus 로고    scopus 로고
    • Functional analysis of the DNA-stimulated ATPase domain of yeast SWI2/SNF2
    • Richmond, E., and Peterson, C. L. (1996) Functional analysis of the DNA-stimulated ATPase domain of yeast SWI2/SNF2. Nucleic Acids Res. 24 (19), 3685-92.
    • (1996) Nucleic Acids Res , vol.24 , Issue.19 , pp. 3685-3692
    • Richmond, E.1    Peterson, C.L.2
  • 53
    • 0033428970 scopus 로고    scopus 로고
    • Helicase motifs: The engine that powers DNA unwinding
    • Hall, M. C., and Matson, S. W. (1999) Helicase motifs: the engine that powers DNA unwinding. Mol. Microbiol. 34, 867-877.
    • (1999) Mol. Microbiol , vol.34 , pp. 867-877
    • Hall, M.C.1    Matson, S.W.2
  • 54
    • 0035854827 scopus 로고    scopus 로고
    • Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis
    • Dunn, R., and Hicke, L. (2001) Multiple roles for Rsp5p-dependent ubiquitination at the internalization step of endocytosis. J. Biol. Chem. 276 (28), 25974-81.
    • (2001) J. Biol. Chem , vol.276 , Issue.28 , pp. 25974-25981
    • Dunn, R.1    Hicke, L.2
  • 55
    • 0025014583 scopus 로고
    • Yeast precursor ribosomal RNA. Molecular cloning and probing the higher-order structure of the internal transcribed spacer I by kethoxal and dimethylsulfate modification
    • Thweatt, R., and Lee, J. C. (1990) Yeast precursor ribosomal RNA. Molecular cloning and probing the higher-order structure of the internal transcribed spacer I by kethoxal and dimethylsulfate modification. J. Mol. Biol. 211 (2), 305-20.
    • (1990) J. Mol. Biol , vol.211 , Issue.2 , pp. 305-320
    • Thweatt, R.1    Lee, J.C.2
  • 56
    • 0033214805 scopus 로고    scopus 로고
    • Cloning and biochemical characterization of Bacillus subtilis YxiN, a DEAD protein specifically activated by 23S rRNA: Delineation of a novel subfamily of bacterial DEAD proteins
    • Kossen, K., and Uhlenbeck, O. C. (1999) Cloning and biochemical characterization of Bacillus subtilis YxiN, a DEAD protein specifically activated by 23S rRNA: delineation of a novel subfamily of bacterial DEAD proteins. Nucleic Acids Res. 27, 3811-3820.
    • (1999) Nucleic Acids Res , vol.27 , pp. 3811-3820
    • Kossen, K.1    Uhlenbeck, O.C.2
  • 57
    • 33745406566 scopus 로고    scopus 로고
    • The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis
    • Granneman, S., Lin, C., Champion, E. A., Nandineni, M. R., Zorca, C., and Baserga, S. J. (2006) The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis. Nucleic Acids Res. 34 (10), 3189-99.
    • (2006) Nucleic Acids Res , vol.34 , Issue.10 , pp. 3189-3199
    • Granneman, S.1    Lin, C.2    Champion, E.A.3    Nandineni, M.R.4    Zorca, C.5    Baserga, S.J.6
  • 58
    • 34248513074 scopus 로고    scopus 로고
    • Human DEAD-box ATPase DDX3 shows a relaxed nucleoside substrate specificity
    • Franca, R., Belfiore, A., Spadari, S., and Maga, G. (2007) Human DEAD-box ATPase DDX3 shows a relaxed nucleoside substrate specificity. Proteins 67 (4), 1128-37.
    • (2007) Proteins , vol.67 , Issue.4 , pp. 1128-1137
    • Franca, R.1    Belfiore, A.2    Spadari, S.3    Maga, G.4
  • 59
    • 0026546001 scopus 로고
    • Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding
    • Wong, I., and Lohman, T. M. (1992) Allosteric effects of nucleotide cofactors on Escherichia coli Rep helicase-DNA binding. Science 256 (5055), 350-5.
    • (1992) Science , vol.256 , Issue.5055 , pp. 350-355
    • Wong, I.1    Lohman, T.M.2
  • 60
    • 10044240394 scopus 로고    scopus 로고
    • Structural basis for the self-chaperoning function of an RNA collapsed state
    • Garcia, I, and Weeks, K. M. (2004) Structural basis for the self-chaperoning function of an RNA collapsed state. Biochemistry 43 (48), 15179-86.
    • (2004) Biochemistry , vol.43 , Issue.48 , pp. 15179-15186
    • Garcia, I.1    Weeks, K.M.2
  • 61
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice
    • McGhee, J. D., and von Hippel, P. H. (1974) Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice. J. Mol. Biol. 86 (2), 469-89.
    • (1974) J. Mol. Biol , vol.86 , Issue.2 , pp. 469-489
    • McGhee, J.D.1    von Hippel, P.H.2
  • 62
    • 0034625396 scopus 로고    scopus 로고
    • Wheat germ poly(A)-binding protein increases the ATPase and the RNA helicase activity of translation initiation factors eIF4A, eIF4B, and eIF-iso4F
    • Bi, X., and Goss, D. J. (2000) Wheat germ poly(A)-binding protein increases the ATPase and the RNA helicase activity of translation initiation factors eIF4A, eIF4B, and eIF-iso4F. J. Biol. Chem. 275 (23), 17740-6.
    • (2000) J. Biol. Chem , vol.275 , Issue.23 , pp. 17740-17746
    • Bi, X.1    Goss, D.J.2
  • 63
    • 56749113879 scopus 로고    scopus 로고
    • RNA helicases from the baker's yeast
    • accessed July 2008
    • Linder, P. (1999) RNA helicases from the baker's yeast Saccharomyces cerevisiae, http://medweb2.unige.ch/~linder/RNA_helicases.html (accessed July 2008).
    • (1999) Saccharomyces cerevisiae
    • Linder, P.1
  • 64
    • 0034525575 scopus 로고    scopus 로고
    • PhyloDraw: A phylogenetic tree drawing system
    • Choi, J. H., Jung, H. Y., Kim, H. S., and Cho, H. G. (2000) PhyloDraw: a phylogenetic tree drawing system. Bioinformatics 16 (11), 1056-8.
    • (2000) Bioinformatics , vol.16 , Issue.11 , pp. 1056-1058
    • Choi, J.H.1    Jung, H.Y.2    Kim, H.S.3    Cho, H.G.4
  • 65
    • 3342957251 scopus 로고    scopus 로고
    • The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity
    • Cordin, O., Tanner, N. K., Doere, M., Linder, P., and Banroquez, J. (2004) The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity. EMBO J. 23 (13), 2478-87.
    • (2004) EMBO J , vol.23 , Issue.13 , pp. 2478-2487
    • Cordin, O.1    Tanner, N.K.2    Doere, M.3    Linder, P.4    Banroquez, J.5
  • 66
    • 0033580840 scopus 로고    scopus 로고
    • Dedlp, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase
    • Iost, I., Dreyfus, M., and Linder, P. (1999) Dedlp, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase. J. Biol. Chem. 274 (25), 17677-83.
    • (1999) J. Biol. Chem , vol.274 , Issue.25 , pp. 17677-17683
    • Iost, I.1    Dreyfus, M.2    Linder, P.3
  • 67
    • 0023925795 scopus 로고
    • Interactions of Escherichia coli transcription termination factor rho with RNA. I. Binding stoichiometries and free energies
    • McSwiggen, J. A., Bear, D. G., and von Hippel, P. H. (1988) Interactions of Escherichia coli transcription termination factor rho with RNA. I. Binding stoichiometries and free energies. J. Mol. Biol. 199 (4), 609-22.
    • (1988) J. Mol. Biol , vol.199 , Issue.4 , pp. 609-622
    • McSwiggen, J.A.1    Bear, D.G.2    von Hippel, P.H.3
  • 68
    • 0023146671 scopus 로고
    • A fluorescence study of the binding of eucaryotic initiation factors to messenger RNA and messenger RNA analogues
    • Goss, D. J., Woodley, C. L., and Wahba, A. J. (1987) A fluorescence study of the binding of eucaryotic initiation factors to messenger RNA and messenger RNA analogues. Biochemistry 26 (6), 1551-6.
    • (1987) Biochemistry , vol.26 , Issue.6 , pp. 1551-1556
    • Goss, D.J.1    Woodley, C.L.2    Wahba, A.J.3
  • 69
    • 0023654283 scopus 로고
    • The ATP-dependent interaction of eukaryotic initiation factors with mRNA
    • Abramson, R. D., Dever, T. E., Lawson, T. G., Ray, B. K., Thach, R. E., and Merrick, W. C. (1987) The ATP-dependent interaction of eukaryotic initiation factors with mRNA. J. Biol. Chem. 262 (8), 3826-32.
    • (1987) J. Biol. Chem , vol.262 , Issue.8 , pp. 3826-3832
    • Abramson, R.D.1    Dever, T.E.2    Lawson, T.G.3    Ray, B.K.4    Thach, R.E.5    Merrick, W.C.6
  • 70
    • 2942754127 scopus 로고    scopus 로고
    • Studies on three E. coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases
    • Bizebard, T., Ferlenghi, I., Iost, I., and Dreyfus, M. (2004) Studies on three E. coli DEAD-box helicases point to an unwinding mechanism different from that of model DNA helicases. Biochemistry 43 (24), 7857-66.
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7857-7866
    • Bizebard, T.1    Ferlenghi, I.2    Iost, I.3    Dreyfus, M.4
  • 71
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev, S., Hsieh, J., Gauss, G. H., Lohman, T. M., and Waksman, G. (1997) Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 90 (4), 635-47.
    • (1997) Cell , vol.90 , Issue.4 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 72
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar, S. S., Soultanas, P., Dillingham, M. S., Subramanya, H. S., and Wigley, D. B. (1999) Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97 (1), 75-84.
    • (1999) Cell , vol.97 , Issue.1 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 73
    • 0034623050 scopus 로고    scopus 로고
    • Escherichia coli replicative helicase PriA protein-single-stranded DNA complex. Stoichiometries, free energy of binding, and cooperativities
    • Jezewska, M. J., Rajendran, S., and Bujalowski, W. (2000) Escherichia coli replicative helicase PriA protein-single-stranded DNA complex. Stoichiometries, free energy of binding, and cooperativities. J. Biol. Chem. 275 (36), 27865-73.
    • (2000) J. Biol. Chem , vol.275 , Issue.36 , pp. 27865-27873
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 74
    • 0030052444 scopus 로고    scopus 로고
    • Binding of Escherichia coli primary replicative helicase DnaB protein to single-stranded DNA. Long-range allosteric conformational changes within the protein hexamer
    • Jezewska, M. J., Kim, U. S., and Bujalowski, W. (1996) Binding of Escherichia coli primary replicative helicase DnaB protein to single-stranded DNA. Long-range allosteric conformational changes within the protein hexamer. Biochemistry 35 (7), 2129-45.
    • (1996) Biochemistry , vol.35 , Issue.7 , pp. 2129-2145
    • Jezewska, M.J.1    Kim, U.S.2    Bujalowski, W.3
  • 75
    • 0035918241 scopus 로고    scopus 로고
    • Further characterization of the helicase activity of eIF4A. Substrate specificity
    • Rogers, G. W., Jr., Lima, W. F., and Merrick, W. C. (2001) Further characterization of the helicase activity of eIF4A. Substrate specificity. J. Biol. Chem. 276 (16), 12598-608.
    • (2001) J. Biol. Chem , vol.276 , Issue.16 , pp. 12598-12608
    • Rogers Jr., G.W.1    Lima, W.F.2    Merrick, W.C.3
  • 76
    • 0037077127 scopus 로고    scopus 로고
    • A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
    • Mohr, S., Stryker, J. M., and Lambowitz, A. M. (2002) A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing. Cell 109 (6), 769-79.
    • (2002) Cell , vol.109 , Issue.6 , pp. 769-779
    • Mohr, S.1    Stryker, J.M.2    Lambowitz, A.M.3
  • 77
    • 33845738802 scopus 로고    scopus 로고
    • Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity
    • Halls, C., Mohr, S., Del Campo, M., Yang, Q., Jankowsky, E., and Lambowitz, A. M. (2007) Involvement of DEAD-box proteins in group I and group II intron splicing. Biochemical characterization of Mss116p, ATP hydrolysis-dependent and -independent mechanisms, and general RNA chaperone activity. J. Mol. Biol. 365 (3), 835-55.
    • (2007) J. Mol. Biol , vol.365 , Issue.3 , pp. 835-855
    • Halls, C.1    Mohr, S.2    Del Campo, M.3    Yang, Q.4    Jankowsky, E.5    Lambowitz, A.M.6
  • 78
    • 31044454357 scopus 로고    scopus 로고
    • Rrp5p, a trans-acting factor in yeast ribosome biogenesis, is an RNA-binding protein with a pronounced preference for U-rich sequences
    • de Boer, P., Vos, H. R., Faber, A. W., Vos, J. C., and Raue, H. A. (2006) Rrp5p, a trans-acting factor in yeast ribosome biogenesis, is an RNA-binding protein with a pronounced preference for U-rich sequences. RNA 12, 263-271.
    • (2006) RNA 12 , pp. 263-271
    • de Boer, P.1    Vos, H.R.2    Faber, A.W.3    Vos, J.C.4    Raue, H.A.5
  • 79
    • 0031761922 scopus 로고    scopus 로고
    • Two mutant forms of the S1/TPR-containing protein Rrp5p affect the 18S rRNA synthesis in Saccharomyces cerevisiae
    • Torchet, C., Jacq, C., and Hermann-Le Denmat, S. (1998) Two mutant forms of the S1/TPR-containing protein Rrp5p affect the 18S rRNA synthesis in Saccharomyces cerevisiae. RNA 4, 1636-1652.
    • (1998) RNA , vol.4 , pp. 1636-1652
    • Torchet, C.1    Jacq, C.2    Hermann-Le Denmat, S.3
  • 80
    • 0029853905 scopus 로고    scopus 로고
    • RRP5 is required for formation of both 18S and 5.8S rRNA in yeast
    • Venema, J., and Tollervey, D. (1996) RRP5 is required for formation of both 18S and 5.8S rRNA in yeast. EMBO J. 15, 5701-5714.
    • (1996) EMBO J , vol.15 , pp. 5701-5714
    • Venema, J.1    Tollervey, D.2


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