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Volumn 42, Issue 16, 2014, Pages 10644-10654

DEAD-box RNA helicase domains exhibit a continuum between complete functional independence and high thermodynamic coupling in nucleotide and RNA duplex recognition

Author keywords

[No Author keywords available]

Indexed keywords

DEAD BOX PROTEIN; DOUBLE STRANDED RNA; HELICASE; HERA PROTEIN; RECA PROTEIN; UNCLASSIFIED DRUG; YXIN PROTEIN; BACTERIAL PROTEIN; NUCLEOTIDE; PROTEIN BINDING; YXIN PROTEIN, BACILLUS SUBTILIS;

EID: 84921334101     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku747     Document Type: Article
Times cited : (32)

References (57)
  • 1
    • 84863450258 scopus 로고    scopus 로고
    • RNA helicases in infection and disease
    • Steimer, L. and Klostermeier, D. (2012) RNA helicases in infection and disease. RNA Biol., 9, 751-771.
    • (2012) RNA Biol. , vol.9 , pp. 751-771
    • Steimer, L.1    Klostermeier, D.2
  • 3
    • 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, 625-636.
    • (2002) J. Mol. Biol. , vol.324 , pp. 625-636
    • Kossen, K.1    Karginov, F.V.2    Uhlenbeck, O.C.3
  • 4
    • 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, 35499-35505.
    • (2005) J. Biol. Chem. , vol.280 , pp. 35499-35505
    • Karginov, F.V.1    Caruthers, J.M.2    Hu, Y.3    McKay, D.B.4    Uhlenbeck, O.C.5
  • 5
    • 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, 2769-2776.
    • (2007) J. Bacteriol. , vol.189 , pp. 2769-2776
    • Turner, A.M.1    Love, C.F.2    Alexander, R.W.3    Jones, P.G.4
  • 6
    • 54549123661 scopus 로고    scopus 로고
    • The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity
    • Linden, M.H., Hartmann, R.K. and Klostermeier, D. (2008) The putative RNase P motif in the DEAD box helicase Hera is dispensable for efficient interaction with RNA and helicase activity. Nucleic Acids Res., 36, 5800-5811.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 5800-5811
    • Linden, M.H.1    Hartmann, R.K.2    Klostermeier, D.3
  • 7
    • 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, 5503-5512.
    • (2001) EMBO J. , vol.20 , pp. 5503-5512
    • Diges, C.M.1    Uhlenbeck, O.C.2
  • 8
    • 0027301893 scopus 로고
    • DbpA: A DEAD box protein specifically activated by 23s rRNA
    • Fuller-Pace, F.V., Nicol, S.M., Reid, A.D. and Lane, D.P. (1993) DbpA: a DEAD box protein specifically activated by 23s rRNA. EMBO J., 12, 3619-3626.
    • (1993) EMBO J. , vol.12 , pp. 3619-3626
    • Fuller-Pace, F.V.1    Nicol, S.M.2    Reid, A.D.3    Lane, D.P.4
  • 9
    • 67349117103 scopus 로고    scopus 로고
    • Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones
    • Del Campo, M., Mohr, S., Jiang, Y., Jia, H., Jankowsky, E. and Lambowitz, A.M. (2009) Unwinding by local strand separation is critical for the function of DEAD-box proteins as RNA chaperones. J. Mol. Biol., 389, 674-693.
    • (2009) J. Mol. Biol. , vol.389 , pp. 674-693
    • Del Campo, M.1    Mohr, S.2    Jiang, Y.3    Jia, H.4    Jankowsky, E.5    Lambowitz, A.M.6
  • 10
    • 84867064003 scopus 로고    scopus 로고
    • Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p
    • Mallam, A.L., Del Campo, M., Gilman, B., Sidote, D.J. and Lambowitz, A.M. (2012) Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p. Nature, 490, 121-125.
    • (2012) Nature , vol.490 , pp. 121-125
    • Mallam, A.L.1    Del Campo, M.2    Gilman, B.3    Sidote, D.J.4    Lambowitz, A.M.5
  • 11
    • 84861385163 scopus 로고    scopus 로고
    • ATP utilization and RNA conformational rearrangement by DEAD-box proteins
    • Henn, A., Bradley, M.J. and De La Cruz, E.M. (2012) ATP utilization and RNA conformational rearrangement by DEAD-box proteins. Annu. Rev. Biophys., 41, 247-267.
    • (2012) Annu. Rev. Biophys. , vol.41 , pp. 247-267
    • Henn, A.1    Bradley, M.J.2    De La Cruz, E.M.3
  • 12
    • 84862975911 scopus 로고    scopus 로고
    • Conformational changes of DEAD-box helicases monitored by single molecule fluorescence resonance energy transfer
    • Andreou, A.Z. and Klostermeier, D. (2012) Conformational changes of DEAD-box helicases monitored by single molecule fluorescence resonance energy transfer. Methods Enzymol., 511, 75-109.
    • (2012) Methods Enzymol. , vol.511 , pp. 75-109
    • Andreou, A.Z.1    Klostermeier, D.2
  • 13
    • 84875171510 scopus 로고    scopus 로고
    • Toward a molecular understanding of RNA remodeling by DEAD-box proteins
    • Russell, R., Jarmoskaite, I. and Lambowitz, A.M. (2013) Toward a molecular understanding of RNA remodeling by DEAD-box proteins. RNA Biol., 10, 44-55.
    • (2013) RNA Biol. , vol.10 , pp. 44-55
    • Russell, R.1    Jarmoskaite, I.2    Lambowitz, A.M.3
  • 14
    • 38649106732 scopus 로고    scopus 로고
    • Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase
    • Theissen, B., Karow, A.R., Kohler, J., Gubaev, A. and Klostermeier, D. (2008) Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase. Proc. Natl Acad. Sci. USA, 105, 548-553.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 548-553
    • Theissen, B.1    Karow, A.R.2    Kohler, J.3    Gubaev, A.4    Klostermeier, D.5
  • 15
    • 0032562239 scopus 로고    scopus 로고
    • The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide
    • Lorsch, J.R. and Herschlag, D. (1998) The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide. Biochemistry, 37, 2180-2193.
    • (1998) Biochemistry , vol.37 , pp. 2180-2193
    • Lorsch, J.R.1    Herschlag, D.2
  • 16
    • 0033580840 scopus 로고    scopus 로고
    • Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase
    • Iost, I., Dreyfus, M. and Linder, P. (1999) Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase. J. Biol. Chem., 274, 17677-17683.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17677-17683
    • Iost, I.1    Dreyfus, M.2    Linder, P.3
  • 17
    • 43249100378 scopus 로고    scopus 로고
    • A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATP-dependent binding of RNA substrates in DEAD-box proteins
    • Banroques, J., Cordin, O., Doere, M., Linder, P. and Tanner, N.K. (2008) A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATP-dependent binding of RNA substrates in DEAD-box proteins. Mol. Cell Biol., 28, 3359-3371.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 3359-3371
    • Banroques, J.1    Cordin, O.2    Doere, M.3    Linder, P.4    Tanner, N.K.5
  • 19
    • 0035942167 scopus 로고    scopus 로고
    • Visualization of unwinding activity of duplex RNA by DbpA, a DEAD box helicase, at single-molecule resolution by atomic force microscopy
    • Henn, A., Medalia, O., Shi, S.P., Steinberg, M., Franceschi, F. and Sagi, I. (2001) Visualization of unwinding activity of duplex RNA by DbpA, a DEAD box helicase, at single-molecule resolution by atomic force microscopy. Proc. Natl. Acad. Sci. USA, 98, 5007-5012.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5007-5012
    • Henn, A.1    Medalia, O.2    Shi, S.P.3    Steinberg, M.4    Franceschi, F.5    Sagi, I.6
  • 20
    • 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, 287-300.
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 21
    • 70350089113 scopus 로고    scopus 로고
    • The mechanism of ATP-dependent RNA unwinding by DEAD box proteins
    • Hilbert, M., Karow, A.R. and Klostermeier, D. (2009) The mechanism of ATP-dependent RNA unwinding by DEAD box proteins. Biol. Chem., 390, 1237-1250.
    • (2009) Biol. Chem. , vol.390 , pp. 1237-1250
    • Hilbert, M.1    Karow, A.R.2    Klostermeier, D.3
  • 22
    • 69749126977 scopus 로고    scopus 로고
    • Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA
    • Del Campo, M. and Lambowitz, A.M. (2009) Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. Mol. Cell, 35, 598-609.
    • (2009) Mol. Cell , vol.35 , pp. 598-609
    • Del Campo, M.1    Lambowitz, A.M.2
  • 23
    • 39649096274 scopus 로고    scopus 로고
    • The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA
    • Henn, A., Cao, W., Hackney, D.D. and De La Cruz, E.M. (2008) The ATPase cycle mechanism of the DEAD-box rRNA helicase, DbpA. J. Mol. Biol., 377, 193-205.
    • (2008) J. Mol. Biol. , vol.377 , pp. 193-205
    • Henn, A.1    Cao, W.2    Hackney, D.D.3    De La Cruz, E.M.4
  • 25
    • 58149481225 scopus 로고    scopus 로고
    • ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
    • Liu, F., Putnam, A. and Jankowsky, E. (2008) ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding. Proc. Natl. Acad. Sci. USA, 105, 20209-20214.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 20209-20214
    • Liu, F.1    Putnam, A.2    Jankowsky, E.3
  • 26
    • 79953675393 scopus 로고    scopus 로고
    • EIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism
    • Hilbert, M., Kebbel, F., Gubaev, A. and Klostermeier, D. (2011) eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism. Nucleic Acids Res., 39, 2260-2270.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2260-2270
    • Hilbert, M.1    Kebbel, F.2    Gubaev, A.3    Klostermeier, D.4
  • 27
    • 70449584733 scopus 로고    scopus 로고
    • The DEAD box helicase YxiN maintains a closed conformation during ATP hydrolysis
    • Aregger, R. and Klostermeier, D. (2009) The DEAD box helicase YxiN maintains a closed conformation during ATP hydrolysis. Biochemistry, 48, 10679-10681.
    • (2009) Biochemistry , vol.48 , pp. 10679-10681
    • Aregger, R.1    Klostermeier, D.2
  • 28
    • 84903974069 scopus 로고    scopus 로고
    • EIF4B, eIF4G and RNA regulate eIF4A activity in translation initiation by modulating the eIF4A conformational cycle
    • Harms, U., Andreou, A.Z., Gubaev, A. and Klostermeier, D. (2014) eIF4B, eIF4G and RNA regulate eIF4A activity in translation initiation by modulating the eIF4A conformational cycle. Nucleic Acids Res., 42, 7911-7922.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 7911-7922
    • Harms, U.1    Andreou, A.Z.2    Gubaev, A.3    Klostermeier, D.4
  • 29
    • 0344129033 scopus 로고    scopus 로고
    • Hera from Thermus thermophilus: The first thermostable DEAD-box helicase with an RNase P protein motif
    • Morlang, S., Weglohner, W. and Franceschi, F. (1999) Hera from Thermus thermophilus: the first thermostable DEAD-box helicase with an RNase P protein motif. J. Mol. Biol., 294, 795-805.
    • (1999) J. Mol. Biol. , vol.294 , pp. 795-805
    • Morlang, S.1    Weglohner, W.2    Franceschi, F.3
  • 30
    • 84884915205 scopus 로고    scopus 로고
    • Rearranging RNA structures at 75 degrees C? Towards the molecular mechanism and physiological function of the Thermus thermophilus DEAD-box helicase hera
    • Klostermeier, D. (2013) Rearranging RNA structures at 75 degrees C? towards the molecular mechanism and physiological function of the Thermus thermophilus DEAD-box helicase hera. Biopolymers. 99, 1137-1146
    • (2013) Biopolymers , vol.99 , pp. 1137-1146
    • Klostermeier, D.1
  • 31
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F.W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif., 41, 207-234.
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 32
    • 33845967782 scopus 로고    scopus 로고
    • Authentic interdomain communication in an RNA helicase reconstituted by expressed protein ligation of two helicase domains
    • Karow, A.R., Theissen, B. and Klostermeier, D. (2007) Authentic interdomain communication in an RNA helicase reconstituted by expressed protein ligation of two helicase domains. FEBS J., 274, 463-473.
    • (2007) FEBS J. , vol.274 , pp. 463-473
    • Karow, A.R.1    Theissen, B.2    Klostermeier, D.3
  • 33
    • 33746853440 scopus 로고    scopus 로고
    • Crystal structure and nucleotide binding of the Thermus thermophilus RNA helicase Hera N-terminal domain
    • Rudolph, M.G., Heissmann, R., Wittmann, J.G. and Klostermeier, D. (2006) Crystal structure and nucleotide binding of the Thermus thermophilus RNA helicase Hera N-terminal domain. J. Mol. Biol., 361, 731-743.
    • (2006) J. Mol. Biol. , vol.361 , pp. 731-743
    • Rudolph, M.G.1    Heissmann, R.2    Wittmann, J.G.3    Klostermeier, D.4
  • 34
    • 61849172406 scopus 로고    scopus 로고
    • Crystallization and preliminary characterization of the Thermus thermophilus RNA helicase Hera C-terminal domain
    • Rudolph, M.G., Wittmann, J.G. and Klostermeier, D. (2009) Crystallization and preliminary characterization of the Thermus thermophilus RNA helicase Hera C-terminal domain. Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun., 65, 248-252.
    • (2009) Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. , vol.65 , pp. 248-252
    • Rudolph, M.G.1    Wittmann, J.G.2    Klostermeier, D.3
  • 35
    • 84884915205 scopus 로고    scopus 로고
    • Rearranging RNA structures at 75 degrees C? Toward the molecular mechanism and physiological function of the thermus thermophilus DEAD-box helicase hera
    • Klostermeier, D. (2013) Rearranging RNA structures at 75 degrees C? toward the molecular mechanism and physiological function of the thermus thermophilus DEAD-box helicase hera. Biopolymers, 99, 1137-1146.
    • (2013) Biopolymers , vol.99 , pp. 1137-1146
    • Klostermeier, D.1
  • 37
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill, S.C. and von Hippel, P.H. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem., 182, 319-326.
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 38
    • 12244255727 scopus 로고    scopus 로고
    • Constrained analysis of fluorescence anisotropy decay: Application to experimental protein dynamics
    • Feinstein, E., Deikus, G., Rusinova, E., Rachofsky, E.L., Ross, J.B. and Laws, W.R. (2003) Constrained analysis of fluorescence anisotropy decay: application to experimental protein dynamics. Biophys. J., 84, 599-611.
    • (2003) Biophys. J. , vol.84 , pp. 599-611
    • Feinstein, E.1    Deikus, G.2    Rusinova, E.3    Rachofsky, E.L.4    Ross, J.B.5    Laws, W.R.6
  • 39
    • 84859413642 scopus 로고    scopus 로고
    • Mean fluorescence lifetime and its error
    • Fiserova, E. and Kubala, M. (2012) Mean fluorescence lifetime and its error. J. Lumin., 132, 2059-2064.
    • (2012) J. Lumin. , vol.132 , pp. 2059-2064
    • Fiserova, E.1    Kubala, M.2
  • 40
    • 77956213053 scopus 로고    scopus 로고
    • Dynamic fluorescence depolarization: A powerful tool to explore protein folding on the ribosome
    • Weinreis, S.A., Ellis, J.P. and Cavagnero, S. (2010) Dynamic fluorescence depolarization: a powerful tool to explore protein folding on the ribosome. Methods, 52, 57-73.
    • (2010) Methods , vol.52 , pp. 57-73
    • Weinreis, S.A.1    Ellis, J.P.2    Cavagnero, S.3
  • 42
    • 0035964283 scopus 로고    scopus 로고
    • DNA binding induces dissociation of the multimeric form of HIV-1 integrase: A time-resolved fluorescence anisotropy study
    • Deprez, E., Tauc, P., Leh, H., Mouscadet, J.F., Auclair, C., Hawkins, M.E. and Brochon, J.C. (2001) DNA binding induces dissociation of the multimeric form of HIV-1 integrase: a time-resolved fluorescence anisotropy study. Proc. Natl. Acad. Sci. USA, 98, 10090-10095.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10090-10095
    • Deprez, E.1    Tauc, P.2    Leh, H.3    Mouscadet, J.F.4    Auclair, C.5    Hawkins, M.E.6    Brochon, J.C.7
  • 43
    • 0031723406 scopus 로고    scopus 로고
    • Dynamics of biomolecules: Assignment of local motions by fluorescence anisotropy decay
    • Bialik, C.N., Wolf, B., Rachofsky, E.L., Ross, J.B. and Laws, W.R. (1998) Dynamics of biomolecules: assignment of local motions by fluorescence anisotropy decay. Biophys. J., 75, 2564-2573.
    • (1998) Biophys. J. , vol.75 , pp. 2564-2573
    • Bialik, C.N.1    Wolf, B.2    Rachofsky, E.L.3    Ross, J.B.4    Laws, W.R.5
  • 44
    • 0343732186 scopus 로고
    • Theory of fluorescence depolarization by anisotropic rotational diffusion
    • Chuang, T.J. and Eisenthal, K.B. (1972) Theory of fluorescence depolarization by anisotropic rotational diffusion. J. Chem. Phys., 57, 5094-5097.
    • (1972) J. Chem. Phys. , vol.57 , pp. 5094-5097
    • Chuang, T.J.1    Eisenthal, K.B.2
  • 45
    • 0022494584 scopus 로고
    • Methionyl-tRNA synthetase induced 3′-terminal and delocalized conformational transition in tRNAfMet: Steady-state fluorescence of tRNA with a single fluorophore
    • Ferguson, B.Q. and Yang, D.C. (1986) Methionyl-tRNA synthetase induced 3′-terminal and delocalized conformational transition in tRNAfMet: steady-state fluorescence of tRNA with a single fluorophore. Biochemistry, 25, 529-539.
    • (1986) Biochemistry , vol.25 , pp. 529-539
    • Ferguson, B.Q.1    Yang, D.C.2
  • 46
    • 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
  • 47
    • 34547211817 scopus 로고    scopus 로고
    • The long unwinding road of RNA helicases
    • Bleichert, F. and Baserga, S.J. (2007) The long unwinding road of RNA helicases. Mol. Cell, 27, 339-352.
    • (2007) Mol. Cell , vol.27 , pp. 339-352
    • Bleichert, F.1    Baserga, S.J.2
  • 49
    • 0034700086 scopus 로고    scopus 로고
    • Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
    • Caruthers, J.M., Johnson, E.R. and McKay, D.B. (2000) Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. Proc. Natl. Acad. Sci. USA, 97, 13080-13085.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13080-13085
    • Caruthers, J.M.1    Johnson, E.R.2    McKay, D.B.3
  • 50
    • 0027494565 scopus 로고
    • The HRIGRXXR region of the Dead box RNA helicase eukaryotic translation initiation factor-4a is required for RNA-binding and ATP hydrolysis
    • Pause, A., Methot, N. and Sonenberg, N. (1993) The HRIGRXXR region of the Dead box RNA helicase eukaryotic translation initiation factor-4a is required for RNA-binding and ATP hydrolysis. Mol. Cell. Biol., 13, 6789-6798.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6789-6798
    • Pause, A.1    Methot, N.2    Sonenberg, N.3
  • 51
    • 0037133527 scopus 로고    scopus 로고
    • Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA
    • Polach, K.J. and Uhlenbeck, O.C. (2002) Cooperative binding of ATP and RNA substrates to the DEAD/H protein DbpA. Biochemistry, 41, 3693-3702.
    • (2002) Biochemistry , vol.41 , pp. 3693-3702
    • Polach, K.J.1    Uhlenbeck, O.C.2
  • 52
    • 84867064003 scopus 로고    scopus 로고
    • Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p
    • Mallam, A.L., Del Campo, M., Gilman, B., Sidote, D.J. and Lambowitz, A.M. (2012) Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p. Nature, 490, 121-125.
    • (2012) Nature , vol.490 , pp. 121-125
    • Mallam, A.L.1    Del Campo, M.2    Gilman, B.3    Sidote, D.J.4    Lambowitz, A.M.5
  • 54
    • 38649106732 scopus 로고    scopus 로고
    • Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase
    • Theissen, B., Karow, A.R., Kohler, J., Gubaev, A. and Klostermeier, D. (2008) Cooperative binding of ATP and RNA induces a closed conformation in a DEAD box RNA helicase. Proc. Natl. Acad. Sci. USA, 105, 548-553.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 548-553
    • Theissen, B.1    Karow, A.R.2    Kohler, J.3    Gubaev, A.4    Klostermeier, D.5
  • 55
    • 84862000545 scopus 로고    scopus 로고
    • Specific domains in yeast translation initiation factor eIF4G strongly bias RNA unwinding activity of the eIF4F complex toward duplexes with 5′-overhangs
    • Rajagopal, V., Park, E.H., Hinnebusch, A.G. and Lorsch, J.R. (2012) Specific domains in yeast translation initiation factor eIF4G strongly bias RNA unwinding activity of the eIF4F complex toward duplexes with 5′-overhangs. J. Biol. Chem., 287, 20301-20312.
    • (2012) J. Biol. Chem. , vol.287 , pp. 20301-20312
    • Rajagopal, V.1    Park, E.H.2    Hinnebusch, A.G.3    Lorsch, J.R.4
  • 56
    • 80053335564 scopus 로고    scopus 로고
    • Probing conformational variations at the ATPase site of the RNA helicase DbpA by high-field electron-nuclear double resonance spectroscopy
    • Kaminker, I., Sushenko, A., Potapov, A., Daube, S., Akabayov, B., Sagi, I. and Goldfarb, D. (2011) Probing conformational variations at the ATPase site of the RNA helicase DbpA by high-field electron-nuclear double resonance spectroscopy. J. Am. Chem. Soc., 133, 15514-15523.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15514-15523
    • Kaminker, I.1    Sushenko, A.2    Potapov, A.3    Daube, S.4    Akabayov, B.5    Sagi, I.6    Goldfarb, D.7
  • 57
    • 84904631841 scopus 로고    scopus 로고
    • DEAD-box protein Cyt-19 is activated by exposed helicase in group i intron RNA
    • Jarmoskaite, I., Bhaskarann, H., Seifert, S. and Russell, R. (2014) DEAD-box protein Cyt-19 is activated by exposed helicase in group I intron RNA. Proc. Natl. Acad. Sci. USA, 111, E2928-E2936 .
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E2928-E2936
    • Jarmoskaite, I.1    Bhaskarann, H.2    Seifert, S.3    Russell, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.