메뉴 건너뛰기




Volumn 110, Issue 29, 2013, Pages

Cofactor-dependent specificity of a DEAD-box protein

Author keywords

Annealing; RNA helicases

Indexed keywords

DEAD BOX PROTEIN; RIBOSOME RNA; ROK1 PROTEIN; RRP5 PROTEIN; UNCLASSIFIED DRUG;

EID: 84880372171     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1302577110     Document Type: Article
Times cited : (35)

References (93)
  • 1
    • 78650854687 scopus 로고    scopus 로고
    • Rna helicases at work: Binding and rearranging
    • Jankowsky E (2011) RNA helicases at work: Binding and rearranging. Trends Biochem Sci 36(1)-19-29.
    • (2011) Trends Biochem Sci , vol.36 , Issue.1 , pp. 19-29
    • Jankowsky, E.1
  • 2
    • 34347385000 scopus 로고    scopus 로고
    • Rna helicases - One fold for many functions
    • Jankowsky E, Fairman ME (2007) RNA helicases - One fold for many functions. Curr Opin Struct Biol 17(3):316-324.
    • (2007) Curr Opin Struct Biol , vol.17 , Issue.3 , pp. 316-324
    • Jankowsky, E.1    Fairman, M.E.2
  • 3
    • 79956071179 scopus 로고    scopus 로고
    • Dead-box proteins as rna helicases and chaperones
    • Jarmoskaite I, Russell R (2011) DEAD-box proteins as RNA helicases and chaperones. Wiley Interdiscip Rev RNA 2(1)-135-152.
    • (2011) Wiley Interdiscip Rev RNA , vol.2 , Issue.1 , pp. 135-152
    • Jarmoskaite, I.1    Russell, R.2
  • 4
    • 33749139723 scopus 로고    scopus 로고
    • Dead-box proteins: A family affair - Active and passive players in rnpremodeling
    • Linder P (2006) Dead-box proteins: A family affair - Active and passive players in RNPremodeling. Nucleic Acids Res 34(15):4168-4180.
    • (2006) Nucleic Acids Res , vol.34 , Issue.15 , pp. 4168-4180
    • Linder, P.1
  • 5
    • 70350089113 scopus 로고    scopus 로고
    • The mechanism of atp-dependent rna unwinding by dead box proteins
    • Hilbert M, Karow AR, Klostermeier D (2009) The mechanism of ATP-dependent RNA unwinding by DEAD box proteins. Biol Chem 390(12)-1237-1250.
    • (2009) Biol Chem , vol.390 , Issue.12 , pp. 1237-1250
    • Hilbert, M.1    Karow, A.R.2    Klostermeier, D.3
  • 6
    • 0027301893 scopus 로고
    • Dbpa: A dead box protein specifically activated by 23s rrna
    • Fuller-Pace FV, Nicol SM, Reid AD, Lane DP (1993) DbpA: A DEAD box protein specifically activated by 23s rRNA. EMBO J 12(9):3619-3626.
    • (1993) EMBO J , vol.12 , Issue.9 , pp. 3619-3626
    • Fuller-Pace, F.V.1    Nicol, S.M.2    Reid, A.D.3    Lane, D.P.4
  • 7
    • 33749125440 scopus 로고    scopus 로고
    • Dead-box rna helicases in escherichia coli
    • Iost I, Dreyfus M (2006) DEAD-box RNA helicases in Escherichia coli. Nucleic Acids Res 34(15):4189-4197.
    • (2006) Nucleic Acids Res , vol.34 , Issue.15 , pp. 4189-4197
    • Iost, I.1    Dreyfus, M.2
  • 8
    • 71049181356 scopus 로고    scopus 로고
    • A dominant negative mutant of the e. Coli rna helicase dbpa blocks assembly of the 50s ribosomal subunit
    • Sharpe Elles LM, Sykes MT, Williamson JR, Uhlenbeck OC (2009) A dominant negative mutant of the E. coli RNA helicase DbpA blocks assembly of the 50S ribosomal subunit. Nucleic Acids Res 37(19):6503-6514.
    • (2009) Nucleic Acids Res , vol.37 , Issue.19 , pp. 6503-6514
    • Sharpe Elles, L.M.1    Sykes, M.T.2    Williamson, J.R.3    Uhlenbeck, O.C.4
  • 9
    • 0032387820 scopus 로고    scopus 로고
    • Kinetic analysis of the rna-dependent adenosinetriphosphatase activity of dbpa, an escherichia coli dead protein specific for 23s ribosomal rna
    • Tsu CA, Uhlenbeck OC (1998) Kinetic analysis of the RNA-dependent adenosinetriphosphatase activity of DbpA, an Escherichia coli DEAD protein specific for 23S ribosomal RNA. Biochemistry 37(48)-16989-16996.
    • (1998) Biochemistry , vol.37 , Issue.48 , pp. 16989-16996
    • Tsu, C.A.1    Uhlenbeck, O.C.2
  • 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 FV, Uhlenbeck OC (2002) The carboxy-terminal domain of the DExDH protein YxiN is sufficient to confer specificity for 23S rRNA. J Mol Biol 324(4): 625-636.
    • (2002) J Mol Biol , vol.324 , Issue.4 , pp. 625-636
    • Kossen, K.1    Karginov, F.V.2    Uhlenbeck, O.C.3
  • 11
    • 69749126977 scopus 로고    scopus 로고
    • Structure of the yeast dead box protein mss116p reveals two wedges that crimp rna
    • Del Campo M, Lambowitz AM (2009) Structure of the Yeast DEAD box protein Mss116p reveals two wedges that crimp RNA. Mol Cell 35(5):598-609.
    • (2009) Mol Cell , vol.35 , Issue.5 , pp. 598-609
    • Del Campo, M.1    Lambowitz, A.M.2
  • 12
    • 62049084648 scopus 로고    scopus 로고
    • The mrna export protein dbp5 binds rna and the cytoplasmic nucleoporin nup214 in a mutually exclusive manner
    • von Moeller H, Basquin C, Conti E (2009) The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner. Nat Struct Mol Biol 16(3):247-254.
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.3 , pp. 247-254
    • Von Moeller, H.1    Basquin, C.2    Conti, E.3
  • 13
    • 33749332762 scopus 로고    scopus 로고
    • Structure of the exon junction core complex with a trapped dead-box atpase bound to rna
    • Andersen CB, et al. (2006) Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA. Science 313(5795)-1968-1972.
    • (2006) Science , vol.313 , Issue.5795 , pp. 1968-1972
    • Andersen, C.B.1
  • 14
    • 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, 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
  • 15
    • 33747182255 scopus 로고    scopus 로고
    • The crystal structure of the exon junction complex reveals how it maintains a stable grip on mrna
    • Bono F, Ebert J, Lorentzen E, Conti E (2006) The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA. Cell 126(4):713-725.
    • (2006) Cell , vol.126 , Issue.4 , pp. 713-725
    • Bono, F.1    Ebert, J.2    Lorentzen, E.3    Conti, E.4
  • 16
    • 67449105353 scopus 로고    scopus 로고
    • The dexd/h-box rna helicase ddx19 is regulated by an alphahelical switch
    • Collins R, et al. (2009) The DEXD/H-box RNA helicase DDX19 is regulated by an alphahelical switch. J Biol Chem 284(16)-10296-10300.
    • (2009) J Biol Chem , vol.284 , Issue.16 , pp. 10296-10300
    • Collins, R.1
  • 17
    • 77958568836 scopus 로고    scopus 로고
    • Comparative structural analysis of human dead-box rna helicases
    • pii
    • Schütz P, et al. (2010) Comparative structural analysis of human DEAD-box RNA helicases. PLoS ONE 5(9):pii: e12791.
    • (2010) PLoS ONE , vol.5 , Issue.9
    • Schütz, P.1
  • 19
    • 81155154337 scopus 로고    scopus 로고
    • Gle1 is a multifunctional dead-box protein regulator that modulates ded1 in translation initiation
    • Bolger TA, Wente SR (2011) Gle1 is a multifunctional DEAD-box protein regulator that modulates Ded1 in translation initiation. J Biol Chem 286(46):39750-39759.
    • (2011) J Biol Chem , vol.286 , Issue.46 , pp. 39750-39759
    • Bolger, T.A.1    Wente, S.R.2
  • 20
    • 0042666838 scopus 로고    scopus 로고
    • Solution structure and rna interactions of the rna recognition motif from eukaryotic translation initiation factor 4b
    • Fleming K, et al. (2003) Solution structure and RNA interactions of the RNA recognition motif from eukaryotic translation initiation factor 4B. Biochemistry 42(30):8966-8975.
    • (2003) Biochemistry , vol.42 , Issue.30 , pp. 8966-8975
    • Fleming, K.1
  • 21
    • 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, et al. (2006) The nucleolar protein Esf2 interacts directly with the DExD/H box RNA helicase, Dbp8, to stimulate ATP hydrolysis. Nucleic Acids Res 34(10): 3189-3199.
    • (2006) Nucleic Acids Res , vol.34 , Issue.10 , pp. 3189-3199
    • Granneman, S.1
  • 22
    • 72449189579 scopus 로고    scopus 로고
    • The atpase and helicase activities of prp43p are stimulated by the g-patch protein pfa1p during yeast ribosome biogenesis
    • Lebaron S, et al. (2009) The ATPase and helicase activities of Prp43p are stimulated by the G-patch protein Pfa1p during yeast ribosome biogenesis. EMBO J 28(24): 3808-3819.
    • (2009) EMBO J , vol.28 , Issue.24 , pp. 3808-3819
    • Lebaron, S.1
  • 23
    • 70449656291 scopus 로고    scopus 로고
    • Rna helicase prp43 and its co-factor pfa1 promote 20 to 18 s rrna processing catalyzed by the endonuclease nob1
    • Pertschy B, et al. (2009) RNA helicase Prp43 and its co-factor Pfa1 promote 20 to 18 S rRNA processing catalyzed by the endonuclease Nob1. J Biol Chem 284(50): 35079-35091.
    • (2009) J Biol Chem , vol.284 , Issue.50 , pp. 35079-35091
    • Pertschy, B.1
  • 24
    • 0035903136 scopus 로고    scopus 로고
    • Modulation of the helicase activity of eif4a by eif4b, eif4h, and eif4f
    • Rogers GW, Jr., Richter NJ, Lima WF, Merrick WC (2001) Modulation of the helicase activity of eIF4A by eIF4B, eIF4H, and eIF4F. J Biol Chem 276(33):30914-30922.
    • (2001) J Biol Chem , vol.276 , Issue.33 , pp. 30914-30922
    • Rogers Jr., G.W.1    Richter, N.J.2    Lima, W.F.3    Merrick, W.C.4
  • 25
    • 36849009618 scopus 로고    scopus 로고
    • Dynamic interactions of ntr1-ntr2 with prp43 and with u5 govern the recruitment of prp43 to mediate spliceosome disassembly
    • Tsai RT, et al. (2007) Dynamic interactions of Ntr1-Ntr2 with Prp43 and with U5 govern the recruitment of Prp43 to mediate spliceosome disassembly. Mol Cell Biol 27(23): 8027-8037.
    • (2007) Mol Cell Biol , vol.27 , Issue.23 , pp. 8027-8037
    • Tsai, R.T.1
  • 26
    • 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, Linder P (1999) Ded1p, a DEAD-box protein required for translation initiation in Saccharomyces cerevisiae, is an RNA helicase. J Biol Chem 274(25): 17677-17683.
    • (1999) J Biol Chem , vol.274 , Issue.25 , pp. 17677-17683
    • Iost, I.1    Dreyfus, M.2    Linder, P.3
  • 27
    • 80052965200 scopus 로고    scopus 로고
    • Duplex unwinding and atpase activities of the dead-box helicase eif4a are coupled by eif4g and eif4b
    • Özeş AR, Feoktistova K, Avanzino BC, Fraser CS (2011) Duplex unwinding and ATPase activities of the DEAD-box helicase eIF4A are coupled by eIF4G and eIF4B. J Mol Biol 412(4):674-687.
    • (2011) J Mol Biol , vol.412 , Issue.4 , pp. 674-687
    • Özeş, A.R.1    Feoktistova, K.2    Avanzino, B.C.3    Fraser, C.S.4
  • 28
    • 47749123500 scopus 로고    scopus 로고
    • Crystal structure of the yeast eif4a-eif4g complex: An rnahelicase controlled by protein-protein interactions
    • Schütz P, et al. (2008) Crystal structure of the yeast eIF4A-eIF4G complex: An RNAhelicase controlled by protein-protein interactions. Proc Natl Acad Sci USA 105(28): 9564-9569.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.28 , pp. 9564-9569
    • Schütz, P.1
  • 29
    • 43249100378 scopus 로고    scopus 로고
    • A conserved phenylalanine of motif iv in superfamily 2 helicases is required for cooperative, atpdependent binding of rna substrates in dead-box proteins
    • Banroques J, Cordin O, Doère M, Linder P, Tanner NK (2008) A conserved phenylalanine of motif IV in superfamily 2 helicases is required for cooperative, ATPdependent binding of RNA substrates in DEAD-box proteins. Mol Cell Biol 28(10): 3359-3371.
    • (2008) Mol Cell Biol , vol.28 , Issue.10 , pp. 3359-3371
    • Banroques, J.1    Cordin, O.2    Doère, M.3    Linder, P.4    Tanner, N.K.5
  • 30
    • 33646181578 scopus 로고    scopus 로고
    • Discriminatory rnp remodeling by the dead-box protein ded1
    • Bowers HA, et al. (2006) Discriminatory RNP remodeling by the DEAD-box protein DED1. RNA 12(5):903-912.
    • (2006) RNA , vol.12 , Issue.5 , pp. 903-912
    • Bowers, H.A.1
  • 31
    • 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, et al. (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):835-855.
    • (2007) J Mol Biol , vol.365 , Issue.3 , pp. 835-855
    • Halls, C.1
  • 32
    • 26644450709 scopus 로고    scopus 로고
    • Atp- and adp-dependent modulation of rna unwinding and strand annealing activities by the dead-box protein ded1
    • Yang Q, Jankowsky E (2005) ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1. Biochemistry 44(41): 13591-13601.
    • (2005) Biochemistry , vol.44 , Issue.41 , pp. 13591-13601
    • Yang, Q.1    Jankowsky, E.2
  • 33
    • 33750593917 scopus 로고    scopus 로고
    • The dead-box protein ded1 unwinds rna duplexes by a mode distinct from translocating helicases
    • Yang Q, Jankowsky E (2006) The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases. Nat Struct Mol Biol 13(11):981-986.
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.11 , pp. 981-986
    • Yang, Q.1    Jankowsky, E.2
  • 34
    • 0033578620 scopus 로고    scopus 로고
    • Interaction of translation initiation factor eif4g with eif4a in the yeast saccharomyces cerevisiae
    • Dominguez D, Altmann M, Benz J, Baumann U, Trachsel H (1999) Interaction of translation initiation factor eIF4G with eIF4A in the yeast Saccharomyces cerevisiae. J Biol Chem 274(38):26720-26726.
    • (1999) J Biol Chem , vol.274 , Issue.38 , pp. 26720-26726
    • Dominguez, D.1    Altmann, M.2    Benz, J.3    Baumann, U.4    Trachsel, H.5
  • 35
    • 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, Klostermeier D (2011) eIF4G stimulates the activity of the DEAD box protein eIF4A by a conformational guidance mechanism. Nucleic Acids Res 39(6):2260-2270.
    • (2011) Nucleic Acids Res , vol.39 , Issue.6 , pp. 2260-2270
    • Hilbert, M.1    Kebbel, F.2    Gubaev, A.3    Klostermeier, D.4
  • 36
    • 0032562221 scopus 로고    scopus 로고
    • The dead box protein eif4a. 2. A cycle of nucleotide and rna-dependent conformational changes
    • Lorsch JR, Herschlag D (1998) The DEAD box protein eIF4A. 2. A cycle of nucleotide and RNA-dependent conformational changes. Biochemistry 37(8):2194-2206.
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2194-2206
    • Lorsch, J.R.1    Herschlag, D.2
  • 37
    • 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 JR, Herschlag D (1998) The DEAD box protein eIF4A. 1. A minimal kinetic and thermodynamic framework reveals coupled binding of RNA and nucleotide. Biochemistry 37(8):2180-2193.
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2180-2193
    • Lorsch, J.R.1    Herschlag, D.2
  • 38
    • 0040142238 scopus 로고    scopus 로고
    • Biochemical and kinetic characterization of the rna helicase activity of eukaryotic initiation factor 4a
    • Rogers GW, Jr., Richter NJ, Merrick WC (1999) Biochemical and kinetic characterization of the RNA helicase activity of eukaryotic initiation factor 4A. J Biol Chem 274(18): 12236-12244.
    • (1999) J Biol Chem , vol.274 , Issue.18 , pp. 12236-12244
    • Rogers Jr., G.W.1    Richter, N.J.2    Merrick, W.C.3
  • 39
    • 79951545973 scopus 로고    scopus 로고
    • The roles of s1 rna-binding domains in rrp5's interactions with pre-rrna
    • Young CL, Karbstein K (2011) The roles of S1 RNA-binding domains in Rrp5's interactions with pre-rRNA. RNA 17(3):512-521.
    • (2011) RNA , vol.17 , Issue.3 , pp. 512-521
    • Young, C.L.1    Karbstein, K.2
  • 41
    • 0029853905 scopus 로고    scopus 로고
    • Rrp5 is required for formation of both 18s and 5.8s rrna in yeast
    • Venema J, Tollervey D (1996) RRP5 is required for formation of both 18S and 5.8S rRNA in yeast. EMBO J 15(20):5701-5714.
    • (1996) EMBO J , vol.15 , Issue.20 , pp. 5701-5714
    • Venema, J.1    Tollervey, D.2
  • 42
    • 0031761922 scopus 로고    scopus 로고
    • Two mutant forms of the s1/tprcontaining protein rrp5p affect the 18s rrna synthesis in saccharomyces cerevisiae
    • Torchet C, Jacq C, Hermann-Le Denmat S (1998) Two mutant forms of the S1/TPRcontaining protein Rrp5p affect the 18S rRNA synthesis in Saccharomyces cerevisiae. RNA 4(12)-1636-1652.
    • (1998) RNA , vol.4 , Issue.12 , pp. 1636-1652
    • Torchet, C.1    Jacq, C.2    Hermann-Le Denmat, S.3
  • 43
    • 78650413785 scopus 로고    scopus 로고
    • An rna conformational switch regulates pre-18s rrna cleavage
    • Lamanna AC, Karbstein K (2011) An RNA conformational switch regulates pre-18S rRNA cleavage. J Mol Biol 405(1):3-17.
    • (2011) J Mol Biol , vol.405 , Issue.1 , pp. 3-17
    • Lamanna, A.C.1    Karbstein, K.2
  • 44
    • 0028998441 scopus 로고
    • Tetratrico peptide repeat interactions: To tpr or not to tpr?
    • Lamb JR, Tugendreich S, Hieter P (1995) Tetratrico peptide repeat interactions: To TPR or not to TPR? Trends Biochem Sci 20(7):257-259.
    • (1995) Trends Biochem Sci , vol.20 , Issue.7 , pp. 257-259
    • Lamb, J.R.1    Tugendreich, S.2    Hieter, P.3
  • 45
    • 10244245450 scopus 로고    scopus 로고
    • U3 snornp and rrp5p associate independently with saccharomyces cerevisiae 35s pre-rrna, but rrp5p is essential for association of rok1p
    • Vos HR, Bax R, Faber AW, Vos JC, Raué HA (2004) U3 snoRNP and Rrp5p associate independently with Saccharomyces cerevisiae 35S pre-rRNA, but Rrp5p is essential for association of Rok1p. Nucleic Acids Res 32(19):5827-5833.
    • (2004) Nucleic Acids Res , vol.32 , Issue.19 , pp. 5827-5833
    • Vos, H.R.1    Bax, R.2    Faber, A.W.3    Vos, J.C.4    Raué, H.A.5
  • 46
    • 0032983093 scopus 로고    scopus 로고
    • The roles of rrp5p in the synthesis of yeast 18s and 5.8s rrna can be functionally and physically separated
    • Eppens NA, Rensen S, Granneman S, Raué HA, Venema J (1999) The roles of Rrp5p in the synthesis of yeast 18S and 5.8S rRNA can be functionally and physically separated. RNA 5(6):779-793.
    • (1999) RNA , vol.5 , Issue.6 , pp. 779-793
    • Eppens, N.A.1    Rensen, S.2    Granneman, S.3    Raué, H.A.4    Venema, J.5
  • 47
    • 0036800015 scopus 로고    scopus 로고
    • Deletions in the s1 domain of rrp5p cause processing at a novel site in its1 of yeast pre-rrna that depends on rex4p
    • Eppens NA, et al. (2002) Deletions in the S1 domain of Rrp5p cause processing at a novel site in ITS1 of yeast pre-rRNA that depends on Rex4p. Nucleic Acids Res 30(19): 4222-4231.
    • (2002) Nucleic Acids Res , vol.30 , Issue.19 , pp. 4222-4231
    • Eppens, N.A.1
  • 48
    • 33745742173 scopus 로고    scopus 로고
    • Activation of the dexd/h-box protein dbp5 by the nuclearpore protein gle1 and its coactivator insp6 is required for mrna export
    • Weirich CS, et al. (2006) Activation of the DExD/H-box protein Dbp5 by the nuclearpore protein Gle1 and its coactivator InsP6 is required for mRNA export. Nat Cell Biol 8(7):668-676.
    • (2006) Nat Cell Biol , vol.8 , Issue.7 , pp. 668-676
    • Weirich, C.S.1
  • 49
    • 2442708866 scopus 로고    scopus 로고
    • Dbp9p, a member of the dead box protein family, exhibits dna helicase activity
    • Kikuma T, et al. (2004) Dbp9p, a member of the DEAD box protein family, exhibits DNA helicase activity. J Biol Chem 279(20):20692-20698.
    • (2004) J Biol Chem , vol.279 , Issue.20 , pp. 20692-20698
    • Kikuma, T.1
  • 50
    • 0024356599 scopus 로고
    • Dissociation of double-stranded polynucleotide helical structures by eukaryotic initiation factors, as revealed by a novel assay
    • Lawson TG, et al. (1989) Dissociation of double-stranded polynucleotide helical structures by eukaryotic initiation factors, as revealed by a novel assay. Biochemistry 28(11):4729-4734.
    • (1989) Biochemistry , vol.28 , Issue.11 , pp. 4729-4734
    • Lawson, T.G.1
  • 51
    • 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, 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):7857-7866.
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7857-7866
    • Bizebard, T.1    Ferlenghi, I.2    Iost, I.3    Dreyfus, M.4
  • 52
    • 0037066739 scopus 로고    scopus 로고
    • The atpase, rna unwinding, and rna binding activities of recombinant p68 rna helicase
    • Huang Y, Liu ZR (2002) The ATPase, RNA unwinding, and RNA binding activities of recombinant p68 RNA helicase. J Biol Chem 277(15)-12810-12815.
    • (2002) J Biol Chem , vol.277 , Issue.15 , pp. 12810-12815
    • Huang, Y.1    Liu, Z.R.2
  • 53
    • 2542510120 scopus 로고    scopus 로고
    • Rearrangement of structured rna via branch migration structures catalysed by the highly related dead-box proteins p68 and p72
    • Rössler OG, Straka A, Stahl H (2001) Rearrangement of structured RNA via branch migration structures catalysed by the highly related DEAD-box proteins p68 and p72. Nucleic Acids Res 29(10):2088-2096.
    • (2001) Nucleic Acids Res , vol.29 , Issue.10 , pp. 2088-2096
    • Rössler, O.G.1    Straka, A.2    Stahl, H.3
  • 54
    • 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 NK, 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
  • 55
    • 84871267065 scopus 로고    scopus 로고
    • Duplex destabilization by four ribosomal dead-box proteins
    • Garcia I, Albring MJ, Uhlenbeck OC (2012) Duplex destabilization by four ribosomal DEAD-box proteins. Biochemistry 51(50)-10109-10118.
    • (2012) Biochemistry , vol.51 , Issue.50 , pp. 10109-10118
    • Garcia, I.1    Albring, M.J.2    Uhlenbeck, O.C.3
  • 56
    • 33749130843 scopus 로고    scopus 로고
    • Remodeling of ribonucleoprotein complexes with dexh/d rna helicases
    • Jankowsky E, Bowers H (2006) Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases. Nucleic Acids Res 34(15):4181-4188.
    • (2006) Nucleic Acids Res , vol.34 , Issue.15 , pp. 4181-4188
    • Jankowsky, E.1    Bowers, H.2
  • 57
    • 0035808566 scopus 로고    scopus 로고
    • Active disruption of an rnaprotein interaction by a dexh/d rna helicase
    • Jankowsky E, Gross CH, Shuman S, Pyle AM (2001) Active disruption of an RNAprotein interaction by a DExH/D RNA helicase. Science 291(5501)-121-125.
    • (2001) Science , vol.291 , Issue.5501 , pp. 121-125
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 58
    • 39149089317 scopus 로고    scopus 로고
    • Structural insights into the exon junction complex
    • Le Hir H, Andersen GR (2008) Structural insights into the exon junction complex. Curr Opin Struct Biol 18(1)-112-119.
    • (2008) Curr Opin Struct Biol , vol.18 , Issue.1 , pp. 112-119
    • Le Hir, H.1    Andersen, G.R.2
  • 59
    • 79956300418 scopus 로고    scopus 로고
    • The dbp5 cycle at the nuclear pore complex during mrna export ii: Nucleotide cycling and mrnp remodeling by dbp5 are controlled by nup159 and gle1
    • Noble KN, et al. (2011) The Dbp5 cycle at the nuclear pore complex during mRNA export II: Nucleotide cycling and mRNP remodeling by Dbp5 are controlled by Nup159 and Gle1. Genes Dev 25(10)-1065-1077.
    • (2011) Genes Dev , vol.25 , Issue.10 , pp. 1065-1077
    • Noble, K.N.1
  • 60
    • 84867064003 scopus 로고    scopus 로고
    • Structural basis for rna-duplex recognition and unwinding by the dead-box helicase mss116p
    • Mallam AL, Del Campo M, Gilman B, Sidote DJ, Lambowitz AM (2012) Structural basis for RNA-duplex recognition and unwinding by the DEAD-box helicase Mss116p. Nature 490(7418)-121-125.
    • (2012) Nature , vol.490 , Issue.7418 , pp. 121-125
    • Mallam, A.L.1    Del Campo, M.2    Gilman, B.3    Sidote, D.J.4    Lambowitz, A.M.5
  • 61
    • 33750936780 scopus 로고    scopus 로고
    • Nonspecific binding to structured rna and preferential unwinding of an exposed helix by the cyt-19 protein, a dead-box rna chaperone
    • Tijerina P, Bhaskaran H, Russell R (2006) Nonspecific binding to structured RNA and preferential unwinding of an exposed helix by the CYT-19 protein, a DEAD-box RNA chaperone. Proc Natl Acad Sci USA 103(45)-16698-16703.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.45 , pp. 16698-16703
    • Tijerina, P.1    Bhaskaran, H.2    Russell, R.3
  • 62
    • 78549252106 scopus 로고    scopus 로고
    • Time-resolved measurements of intracellular atp in the yeast saccharomyces cerevisiae using a new type of nanobiosensor
    • Ozalp VC, Pedersen TR, Nielsen LJ, Olsen LF (2010) Time-resolved measurements of intracellular ATP in the yeast Saccharomyces cerevisiae using a new type of nanobiosensor. J Biol Chem 285(48):37579-37588.
    • (2010) J Biol Chem , vol.285 , Issue.48 , pp. 37579-37588
    • Ozalp, V.C.1    Pedersen, T.R.2    Nielsen, L.J.3    Olsen, L.F.4
  • 63
    • 0035282868 scopus 로고    scopus 로고
    • Characterization and mutational analysis of yeast dbp8p, a putative rna helicase involved in ribosome biogenesis
    • Daugeron MC, Linder P (2001) Characterization and mutational analysis of yeast Dbp8p, a putative RNA helicase involved in ribosome biogenesis. Nucleic Acids Res 29(5)-1144-1155.
    • (2001) Nucleic Acids Res , vol.29 , Issue.5 , pp. 1144-1155
    • Daugeron, M.C.1    Linder, P.2
  • 64
    • 84869845792 scopus 로고    scopus 로고
    • A structure-based model of rig-i activation
    • Kolakofsky D, Kowalinski E, Cusack S (2012) A structure-based model of RIG-I activation. RNA 18(12):2118-2127.
    • (2012) RNA , vol.18 , Issue.12 , pp. 2118-2127
    • Kolakofsky, D.1    Kowalinski, E.2    Cusack, S.3
  • 65
    • 79956302113 scopus 로고    scopus 로고
    • Human eif4aiii interacts with an eif4glike partner nom1 revealing an evolutionarily conserved function outside the exon junction complex
    • Alexandrov A, Colognori D, Steitz JA (2011) Human eIF4AIII interacts with an eIF4Glike partner, NOM1, revealing an evolutionarily conserved function outside the exon junction complex. Genes Dev 25(10)-1078-1090.
    • (2011) Genes Dev , vol.25 , Issue.10 , pp. 1078-1090
    • Alexandrov, A.1    Colognori, D.2    Steitz, J.A.3
  • 66
    • 79954598438 scopus 로고    scopus 로고
    • A conserved mechanism of dead-box atpase activation by nucleoporins and insp6 in mrna export
    • Montpetit B, et al. (2011) A conserved mechanism of DEAD-box ATPase activation by nucleoporins and InsP6 in mRNA export. Nature 472(7342):238-242.
    • (2011) Nature , vol.472 , Issue.7342 , pp. 238-242
    • Montpetit, B.1
  • 67
    • 0033569797 scopus 로고    scopus 로고
    • The rna export factor gle1p is located on the cytoplasmic fibrils of the npc and physically interacts with the fg-nucleoporin rip1p, the deadbox protein rat8p/dbp5p and a new protein ymr 255p
    • Strahm Y, et al. (1999) The RNA export factor Gle1p is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Rip1p, the DEADbox protein Rat8p/Dbp5p and a new protein Ymr 255p. EMBO J 18(20):5761-5777.
    • (1999) EMBO J , vol.18 , Issue.20 , pp. 5761-5777
    • Strahm, Y.1
  • 68
    • 79958267118 scopus 로고    scopus 로고
    • The rna helicase mtr4p modulates polyadenylation in the tramp complex
    • Jia H, et al. (2011) The RNA helicase Mtr4p modulates polyadenylation in the TRAMP complex. Cell 145(6):890-901.
    • (2011) Cell , vol.145 , Issue.6 , pp. 890-901
    • Jia, H.1
  • 69
    • 58149231008 scopus 로고    scopus 로고
    • Atp-dependent unwinding of u4/u6 snrnas by the brr2 helicase requires the c terminus of prp8
    • Maeder C, Kutach AK, Guthrie C (2009) ATP-dependent unwinding of U4/U6 snRNAs by the Brr2 helicase requires the C terminus of Prp8. Nat Struct Mol Biol 16(1):42-48.
    • (2009) Nat Struct Mol Biol , vol.16 , Issue.1 , pp. 42-48
    • Maeder, C.1    Kutach, A.K.2    Guthrie, C.3
  • 70
    • 69149090973 scopus 로고    scopus 로고
    • Common design principles in the spliceosomal rna helicase brr2 and in the hel308 dna helicase
    • Pena V, et al. (2009) Common design principles in the spliceosomal RNA helicase Brr2 and in the Hel308 DNA helicase. Mol Cell 35(4):454-466.
    • (2009) Mol Cell , vol.35 , Issue.4 , pp. 454-466
    • Pena, V.1
  • 71
    • 34548842257 scopus 로고    scopus 로고
    • Ntr1 activates the prp43 helicase to trigger release of lariat-intron from the spliceosome
    • Tanaka N, Aronova A, Schwer B (2007) Ntr1 activates the Prp43 helicase to trigger release of lariat-intron from the spliceosome. Genes Dev 21(18):2312-2325.
    • (2007) Genes Dev , vol.21 , Issue.18 , pp. 2312-2325
    • Tanaka, N.1    Aronova, A.2    Schwer, B.3
  • 72
    • 84857590342 scopus 로고    scopus 로고
    • Dbp5, gle1-ip6 and nup159: A working model for mrnp export
    • Folkmann AW, Noble KN, Cole CN, Wente SR (2011) Dbp5, Gle1-IP6 and Nup159: A working model for mRNP export. Nucleus 2(6):540-548.
    • (2011) Nucleus , vol.2 , Issue.6 , pp. 540-548
    • Folkmann, A.W.1    Noble, K.N.2    Cole, C.N.3    Wente, S.R.4
  • 73
    • 24944469031 scopus 로고    scopus 로고
    • Structural basis for the enhancement of eif4a helicase activity by eif4g
    • Oberer M, Marintchev A, Wagner G (2005) Structural basis for the enhancement of eIF4A helicase activity by eIF4G. Genes Dev 19(18):2212-2223.
    • (2005) Genes Dev , vol.19 , Issue.18 , pp. 2212-2223
    • Oberer, M.1    Marintchev, A.2    Wagner, G.3
  • 74
    • 79952686670 scopus 로고    scopus 로고
    • Molecular mechanisms for the rna-dependent atpase activity of upf1 and its regulation by upf2
    • Chakrabarti S, et al. (2011) Molecular mechanisms for the RNA-dependent ATPase activity of Upf1 and its regulation by Upf2. Mol Cell 41(6):693-703.
    • (2011) Mol Cell , vol.41 , Issue.6 , pp. 693-703
    • Chakrabarti, S.1
  • 75
    • 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 EH, Hinnebusch AG, Lorsch JR (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(24):20301-20312.
    • (2012) J Biol Chem , vol.287 , Issue.24 , pp. 20301-20312
    • Rajagopal, V.1    Park, E.H.2    Hinnebusch, A.G.3    Lorsch, J.R.4
  • 76
    • 0030671163 scopus 로고    scopus 로고
    • Prp43: An rna helicase-like factor involved in spliceosome disassembly
    • Arenas JE, Abelson JN (1997) Prp43: An RNA helicase-like factor involved in spliceosome disassembly. Proc Natl Acad Sci USA 94(22)-11798-11802.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.22 , pp. 11798-11802
    • Arenas, J.E.1    Abelson, J.N.2
  • 77
    • 30644465812 scopus 로고    scopus 로고
    • Prp43p is a deah-box spliceosome disassembly factor essential for ribosome biogenesis
    • Combs DJ, Nagel RJ, Ares M, Jr., Stevens SW (2006) Prp43p is a DEAH-box spliceosome disassembly factor essential for ribosome biogenesis. Mol Cell Biol 26(2):523-534.
    • (2006) Mol Cell Biol , vol.26 , Issue.2 , pp. 523-534
    • Combs, D.J.1    Nagel, R.J.2    Ares Jr., M.3    Stevens, S.W.4
  • 78
    • 30644478744 scopus 로고    scopus 로고
    • The splicing factor prp43p, a deah box atpase, functions in ribosome biogenesis
    • Leeds NB, Small EC, Hiley SL, Hughes TR, Staley JP (2006) The splicing factor Prp43p, a DEAH box ATPase, functions in ribosome biogenesis. Mol Cell Biol 26(2):513-522.
    • (2006) Mol Cell Biol , vol.26 , Issue.2 , pp. 513-522
    • Leeds, N.B.1    Small, E.C.2    Hiley, S.L.3    Hughes, T.R.4    Staley, J.P.5
  • 79
    • 29144515824 scopus 로고    scopus 로고
    • Spliceosome disassembly catalyzed by prp43 and its associated components ntr1 and ntr2
    • Tsai RT, et al. (2005) Spliceosome disassembly catalyzed by Prp43 and its associated components Ntr1 and Ntr2. Genes Dev 19(24):2991-3003.
    • (2005) Genes Dev , vol.19 , Issue.24 , pp. 2991-3003
    • Tsai, R.T.1
  • 80
    • 70449686545 scopus 로고    scopus 로고
    • Prp43 bound at different sites on the pre-rrna performs distinct functions in ribosome synthesis
    • Bohnsack MT, et al. (2009) Prp43 bound at different sites on the pre-rRNA performs distinct functions in ribosome synthesis. Mol Cell 36(4):583-592.
    • (2009) Mol Cell , vol.36 , Issue.4 , pp. 583-592
    • Bohnsack, M.T.1
  • 81
    • 77954958169 scopus 로고    scopus 로고
    • Prp43p contains a processive helicase structural architecture with a specific regulatory domain
    • Walbott H, et al. (2010) Prp43p contains a processive helicase structural architecture with a specific regulatory domain. EMBO J 29(13):2194-2204.
    • (2010) EMBO J , vol.29 , Issue.13 , pp. 2194-2204
    • Walbott, H.1
  • 82
    • 0029040719 scopus 로고
    • Antisense snornas: A family of nucleolar rnas with long complementarities to rrna
    • Bachellerie JP, et al. (1995) Antisense snoRNAs: A family of nucleolar RNAs with long complementarities to rRNA. Trends Biochem Sci 20(7):261-264.
    • (1995) Trends Biochem Sci , vol.20 , Issue.7 , pp. 261-264
    • Bachellerie, J.P.1
  • 83
    • 2942610793 scopus 로고    scopus 로고
    • Rna structure and function in c/d and h/aca s (no)rnps
    • Henras AK, Dez C, Henry Y (2004) RNA structure and function in C/D and H/ACA s (no)RNPs. Curr Opin Struct Biol 14(3):335-343.
    • (2004) Curr Opin Struct Biol , vol.14 , Issue.3 , pp. 335-343
    • Henras, A.K.1    Dez, C.2    Henry, Y.3
  • 85
    • 0032498230 scopus 로고    scopus 로고
    • The enhanceosome and transcriptional synergy
    • Carey M (1998) The enhanceosome and transcriptional synergy. Cell 92(1):5-8.
    • (1998) Cell , vol.92 , Issue.1 , pp. 5-8
    • Carey, M.1
  • 87
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks, and microprocessors
    • Morgan DO (1997) Cyclin-dependent kinases: Engines, clocks, and microprocessors. Annu Rev Cell Dev Biol 13:261-291.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 261-291
    • Morgan, D.O.1
  • 89
    • 27944487604 scopus 로고    scopus 로고
    • An essential gtpase promotes assembly of preribosomal rna processing complexes
    • Karbstein K, Jonas S, Doudna JA (2005) An essential GTPase promotes assembly of preribosomal RNA processing complexes. Mol Cell 20(4):633-643.
    • (2005) Mol Cell , vol.20 , Issue.4 , pp. 633-643
    • Karbstein, K.1    Jonas, S.2    Doudna, J.A.3
  • 90
    • 70149120737 scopus 로고    scopus 로고
    • Nob1 binds the single-stranded cleavage site d at the 3′-end of 18s rrna with its pin domain
    • Lamanna AC, Karbstein K (2009) Nob1 binds the single-stranded cleavage site D at the 3′-end of 18S rRNA with its PIN domain. Proc Natl Acad Sci USA 106(34)-14259-14264.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.34 , pp. 14259-14264
    • Lamanna, A.C.1    Karbstein, K.2
  • 91
    • 0037125926 scopus 로고    scopus 로고
    • Probing the tetrahymena group i ribozyme reaction in both directions
    • Karbstein K, Carroll KS, Herschlag D (2002) Probing the Tetrahymena group I ribozyme reaction in both directions. Biochemistry 41(37)-11171-11183.
    • (2002) Biochemistry , vol.41 , Issue.37 , pp. 11171-11183
    • Karbstein, K.1    Carroll, K.S.2    Herschlag, D.3
  • 93
    • 81155159831 scopus 로고    scopus 로고
    • Ribosome assembly factors prevent premature translation initiation by 40s assembly intermediates
    • Strunk BS, et al. (2011) Ribosome assembly factors prevent premature translation initiation by 40S assembly intermediates. Science 333(6048)-1449-1453.
    • (2011) Science , vol.333 , Issue.6048 , pp. 1449-1453
    • Strunk, B.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.