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Volumn 108, Issue 30, 2011, Pages 12254-12259

Solution structures of DEAD-box RNA chaperones reveal conformational changes and nucleic acid tethering by a basic tail

Author keywords

Ribozyme; RNA folding; RNA helicase; RNA protein interaction

Indexed keywords

ADENOSINE; CHAPERONE; DEAD BOX PROTEIN; DNA; HELICASE; OLIGONUCLEOTIDE; RNA;

EID: 79961099216     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1109566108     Document Type: Article
Times cited : (63)

References (43)
  • 1
    • 33344473656 scopus 로고    scopus 로고
    • The DEAD-box protein family of RNA helicases
    • DOI 10.1016/j.gene.2005.10.019, PII S0378111905006359
    • Cordin O, Banroques J, Tanner NK, Linder P (2006) The DEAD-box protein family of RNA helicases. Gene 367:17-37. (Pubitemid 43286737)
    • (2006) Gene , vol.367 , Issue.1-2 , pp. 17-37
    • Cordin, O.1    Banroques, J.2    Tanner, N.K.3    Linder, P.4
  • 2
    • 34347385000 scopus 로고    scopus 로고
    • RNA helicases - one fold for many functions
    • DOI 10.1016/j.sbi.2007.05.007, PII S0959440X07000723, Nucleic acids / Sequences and topology
    • Jankowsky E, Fairman ME (2007) RNA helicases - one fold for many functions. Curr Opin Struct Biol 17:316-324. (Pubitemid 47021361)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.3 , pp. 316-324
    • Jankowsky, E.1    Fairman, M.E.2
  • 3
    • 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 390:1237-1250.
    • (2009) Biol Chem , vol.390 , pp. 1237-1250
    • Hilbert, M.1    Karow, A.R.2    Klostermeier, D.3
  • 4
    • 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. WIREs: RNA 2:135-152.
    • (2011) WIREs: RNA , vol.2 , pp. 135-152
    • Jarmoskaite, I.1    Russell, R.2
  • 5
    • 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 36:19-29.
    • (2011) Trends Biochem Sci , vol.36 , pp. 19-29
    • Jankowsky, E.1
  • 6
    • 33749139723 scopus 로고    scopus 로고
    • Dead-box proteins: A family affair - Active and passive players in RNP-remodeling
    • Linder P (2006) Dead-box proteins: A family affair - active and passive players in RNP-remodeling. Nucleic Acids Res 34:4168-4180.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4168-4180
    • Linder, P.1
  • 7
    • 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 125:287-300.
    • (2006) Cell , vol.125 , pp. 287-300
    • Sengoku, T.1    Nureki, O.2    Nakamura, A.3    Kobayashi, S.4    Yokoyama, S.5
  • 8
    • 58149503706 scopus 로고    scopus 로고
    • DEAD-box proteins can completely separate an RNA duplex using a single ATP
    • Chen Y, et al. (2008) DEAD-box proteins can completely separate an RNA duplex using a single ATP. Proc Natl Acad Sci USA 105:20203-20208.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 20203-20208
    • Chen, Y.1
  • 9
    • 58149481225 scopus 로고    scopus 로고
    • ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
    • Liu F, Putnam A, 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
  • 10
    • 35348941874 scopus 로고    scopus 로고
    • DEAD-Box Proteins Unwind Duplexes by Local Strand Separation
    • DOI 10.1016/j.molcel.2007.08.016, PII S109727650700559X
    • Yang Q, Del Campo M, Lambowitz AM, Jankowsky E (2007) DEAD-box proteins unwind duplexes by local strand separation. Mol Cell 28:253-263. (Pubitemid 47610740)
    • (2007) Molecular Cell , vol.28 , Issue.2 , pp. 253-263
    • Yang, Q.1    Del, C.M.2    Lambowitz, A.M.3    Jankowsky, E.4
  • 11
    • 77749239820 scopus 로고    scopus 로고
    • Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA
    • Henn A, et al. (2010) Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA. Proc Natl Acad Sci USA 107:4046-4050.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4046-4050
    • Henn, A.1
  • 12
    • 79956103194 scopus 로고    scopus 로고
    • Mechanism of Mss116 ATPase reveals functional diversity of DEAD-box proteins
    • Cao W, et al. (2011) Mechanism of Mss116 ATPase reveals functional diversity of DEAD-box proteins. J Mol Biol 409:399-414.
    • (2011) J Mol Biol , vol.409 , pp. 399-414
    • Cao, W.1
  • 13
    • 33947362880 scopus 로고    scopus 로고
    • Probing the mechanisms of DEAD-box proteins as general RNA chaperones: The C-terminal domain of CYT-19 mediates general recognition of RNA
    • DOI 10.1021/bi0619472
    • Grohman JK, et al. (2007) Probing the mechanisms of DEAD-box proteins as general RNA chaperones: The C-terminal domain of CYT-19 mediates general recognition of RNA. Biochemistry 46:3013-3022. (Pubitemid 46449125)
    • (2007) Biochemistry , vol.46 , Issue.11 , pp. 3013-3022
    • Grohman, J.K.1    Del, C.M.2    Bhaskaran, H.3    Tijerina, P.4    Lambowitz, A.M.5    Russell, R.6
  • 14
    • 37749022256 scopus 로고    scopus 로고
    • Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro
    • Mohr G, et al. (2008) Function of the C-terminal domain of the DEAD-box protein Mss116p analyzed in vivo and in vitro. J Mol Biol 375:1344-1364.
    • (2008) J Mol Biol , vol.375 , pp. 1344-1364
    • Mohr, G.1
  • 15
    • 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
    • DOI 10.1021/bi049852s
    • 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 43:7857-7866. (Pubitemid 38787694)
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7857-7866
    • Bizebard, T.1    Ferlenghi, I.2    Iost, I.3    Dreyfus, M.4
  • 16
    • 26644450709 scopus 로고    scopus 로고
    • ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1
    • DOI 10.1021/bi0508946
    • Yang Q, Jankowsky E (2005) ATP- and ADP-dependent modulation of RNA unwinding and strand annealing activities by the DEAD-box protein DED1. Biochemistry 44:13591-13601. (Pubitemid 41443687)
    • (2005) Biochemistry , vol.44 , Issue.41 , pp. 13591-13601
    • Yang, Q.1    Jankowsky, E.2
  • 17
    • 0037077127 scopus 로고    scopus 로고
    • A DEAD-Box protein functions as an ATP-dependent RNA chaperone in group I intron splicing
    • DOI 10.1016/S0092-8674(02)00771-7
    • Mohr S, Stryker JM, Lambowitz AM (2002) A DEAD-box protein functions as an ATP-dependent RNA chaperone in group I intron splicing. Cell 109:769-779. (Pubitemid 34722271)
    • (2002) Cell , vol.109 , Issue.6 , pp. 769-779
    • Mohr, S.1    Stryker, J.M.2    Lambowitz, A.M.3
  • 18
    • 35548989806 scopus 로고    scopus 로고
    • Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone
    • DOI 10.1038/nature06235, PII NATURE06235
    • Bhaskaran H, Russell R (2007) Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone. Nature 449:1014-1018. (Pubitemid 350014602)
    • (2007) Nature , vol.449 , Issue.7165 , pp. 1014-1018
    • Bhaskaran, H.1    Russell, R.2
  • 19
    • 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, et al. (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
  • 20
    • 11844297811 scopus 로고    scopus 로고
    • The splicing of yeastmitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function
    • Huang HR, et al. (2005) The splicing of yeastmitochondrial group I and group II introns requires a DEAD-box protein with RNA chaperone function. Proc Natl Acad Sci USA 102:163-168.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 163-168
    • Huang, H.R.1
  • 22
    • 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 35:598-609.
    • (2009) Mol Cell , vol.35 , pp. 598-609
    • Del Campo, M.1    Lambowitz, A.M.2
  • 23
    • 0242571958 scopus 로고    scopus 로고
    • Small-angle scattering studies of biological macromolecules in solution
    • DOI 10.1088/0034-4885/66/10/R05, PII S0034488503126887
    • Svergun DI, Koch MHJ (2003) Small-angle scattering studies of biological macromolecules in solution. Rep Prog Phys 66:1735-1782. (Pubitemid 37365734)
    • (2003) Reports on Progress in Physics , vol.66 , Issue.10 , pp. 1735-1782
    • Svergun, D.I.1    Koch, M.H.J.2
  • 24
    • 0033001996 scopus 로고    scopus 로고
    • Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing
    • Svergun DI (1999) Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys J 76:2879-2886.
    • (1999) Biophys J , vol.76 , pp. 2879-2886
    • Svergun, D.I.1
  • 25
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from x-ray solution scattering
    • Svergun DI, Petoukhov MV, Koch MH (2001) Determination of domain structure of proteins from X-ray solution scattering. Biophys J 80:2946-2953. (Pubitemid 32521666)
    • (2001) Biophysical Journal , vol.80 , Issue.6 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 26
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • DOI 10.1529/biophysj.105.064154
    • Petoukhov MV, Svergun DI (2005) Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89:1237-1250. (Pubitemid 41099005)
    • (2005) Biophysical Journal , vol.89 , Issue.2 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 27
    • 34248359067 scopus 로고    scopus 로고
    • ATSAS 2.1 - Towards automated and web-supported small-angle scattering data analysis
    • DOI 10.1107/S0021889807002853, PII S0021889807002853
    • Petoukhov MV, Konarev PV, Kikhney AG, Svergun DI (2007) ATSAS 2.1-towards automated and web-supported small-angle scattering data analysis. J Appl Crystallogr 40:S223-S228. (Pubitemid 46732692)
    • (2007) Journal of Applied Crystallography , vol.40 , Issue.SUPPL. 1
    • Petoukhov, M.V.1    Konarev, P.V.2    Kikhney, A.G.3    Svergun, D.I.4
  • 29
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • DOI 10.1107/S0021889895007047
    • Svergun D, Barberato C, Koch MHJ (1995) CRYSOL-A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates. J Appl Crystallogr 28:768-773. (Pubitemid 3014671)
    • (1995) Journal of Applied Crystallography , vol.28 , Issue.6 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.3
  • 31
    • 0034640267 scopus 로고    scopus 로고
    • A map of protein-rRNA distribution in the 70 S Escherichia coli ribosome
    • DOI 10.1074/jbc.275.19.14432
    • Svergun DI, Nierhaus KH (2000) A map of protein-rRNA distribution in the 70 S Escherichia coli ribosome. J Biol Chem 275:14432-14439. (Pubitemid 30339729)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.19 , pp. 14432-14439
    • Svergun, D.I.1    Nierhaus, K.H.2
  • 32
    • 70349237510 scopus 로고    scopus 로고
    • Identification of proteins associated with the yeastmitochondrial RNA polymerase by tandem affinity purification
    • Markov DA, et al. (2009) Identification of proteins associated with the yeastmitochondrial RNA polymerase by tandem affinity purification. Yeast 26:423-440.
    • (2009) Yeast , vol.26 , pp. 423-440
    • Markov, D.A.1
  • 33
    • 33750593917 scopus 로고    scopus 로고
    • The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases
    • DOI 10.1038/nsmb1165, PII NSMB1165
    • Yang Q, Jankowsky E (2006) The DEAD-box protein Ded1 unwinds RNA duplexes by a mode distinct from translocating helicases. Nat Struct Mol Biol 13:981-986. (Pubitemid 44684849)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.11 , pp. 981-986
    • Yang, Q.1    Jankowsky, E.2
  • 34
    • 78049234242 scopus 로고    scopus 로고
    • Single-molecule analysis of Mss116-mediated group II intron folding
    • Karunatilaka KS, Solem A, Pyle AM, Rueda D (2010) Single-molecule analysis of Mss116-mediated group II intron folding. Nature 467:935-939.
    • (2010) Nature , vol.467 , pp. 935-939
    • Karunatilaka, K.S.1    Solem, A.2    Pyle, A.M.3    Rueda, D.4
  • 35
    • 77956715760 scopus 로고    scopus 로고
    • Structure of the RNA binding domain of a DEAD-box helicase bound to its ribosomal RNA target reveals a novel mode of recognition by an RNA recognition motif
    • Hardin JW, Hu YX, McKay DB (2010) Structure of the RNA binding domain of a DEAD-box helicase bound to its ribosomal RNA target reveals a novel mode of recognition by an RNA recognition motif. J Mol Biol 402:412-427.
    • (2010) J Mol Biol , vol.402 , pp. 412-427
    • Hardin, J.W.1    Hu, Y.X.2    McKay, D.B.3
  • 36
    • 77956926253 scopus 로고    scopus 로고
    • A structural model for the DEAD box helicase YxiN in solution: Localization of the RNA binding domain
    • Karow AR, Klostermeier D (2010) A structural model for the DEAD box helicase YxiN in solution: Localization of the RNA binding domain. J Mol Biol 402:629-637.
    • (2010) J Mol Biol , vol.402 , pp. 629-637
    • Karow, A.R.1    Klostermeier, D.2
  • 37
    • 37749032415 scopus 로고    scopus 로고
    • The Bacillus subtilis RNA helicase YxiN is distended in solution
    • Wang S, Overgaard MT, Hu Y, McKay DB (2008) The Bacillus subtilis RNA helicase YxiN is distended in solution. Biophys J 94:L01-03.
    • (2008) Biophys J , vol.94
    • Wang, S.1    Overgaard, M.T.2    Hu, Y.3    McKay, D.B.4
  • 38
    • 33646883060 scopus 로고    scopus 로고
    • The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold
    • DOI 10.1261/rna.5906
    • Wang S, et al. (2006) The domain of the Bacillus subtilis DEAD-box helicase YxiN that is responsible for specific binding of 23S rRNA has an RNA recognition motif fold. RNA 12:959-967. (Pubitemid 43788114)
    • (2006) RNA , vol.12 , Issue.6 , pp. 959-967
    • Wang, S.1    Hu, Y.2    Overgaard, M.T.3    Karginov, F.V.4    Uhlenbeck, O.C.5    McKay, D.B.6
  • 39
    • 39049131090 scopus 로고    scopus 로고
    • RNA chaperones, RNA annealers, and RNA helicases
    • Rajkowitsch L, et al. (2007) RNA chaperones, RNA annealers, and RNA helicases. RNA Biol 4:118-130.
    • (2007) RNA Biol , vol.4 , pp. 118-130
    • Rajkowitsch, L.1
  • 42
    • 79952539053 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling: Genetics, genomics, and mechanisms
    • Hargreaves DC, Crabtree GR (2011) ATP-dependent chromatin remodeling: Genetics, genomics, and mechanisms. Cell Res 21:396-420.
    • (2011) Cell Res , vol.21 , pp. 396-420
    • Hargreaves, D.C.1    Crabtree, G.R.2
  • 43
    • 79952182929 scopus 로고    scopus 로고
    • An intrinsically disordered C terminus allows the La protein to assist the biogenesis of diverse noncoding RNA precursors
    • Kucera NJ, Hodsdon ME, Wolin SL (2011) An intrinsically disordered C terminus allows the La protein to assist the biogenesis of diverse noncoding RNA precursors. Proc Natl Acad Sci USA 108:1308-1313.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 1308-1313
    • Kucera, N.J.1    Hodsdon, M.E.2    Wolin, S.L.3


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