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Volumn 60, Issue 3, 2015, Pages 487-499

Structure of the RNA Helicase MLE Reveals the Molecular Mechanisms for Uridine Specificity and RNA-ATP Coupling

Author keywords

DEAH; Dosage compensation; Helicase; MLE; RoX RNA; Structure

Indexed keywords

ADENOSINE TRIPHOSPHATE; RNA; RNA HELICASE; RNA HELICASE MLE; UNCLASSIFIED DRUG; URIDINE; DNA HELICASE; DROSOPHILA PROTEIN; MLE PROTEIN, DROSOPHILA; NONHISTONE PROTEIN; RNA BINDING PROTEIN; ROX2 PROTEIN, DROSOPHILA; TRANSCRIPTION FACTOR;

EID: 84947750104     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2015.10.011     Document Type: Article
Times cited : (59)

References (51)
  • 2
    • 34447132375 scopus 로고    scopus 로고
    • Structural basis for DNA duplex separation by a superfamily-2 helicase
    • Büttner K., Nehring S., Hopfner K.-P. Structural basis for DNA duplex separation by a superfamily-2 helicase. Nat. Struct. Mol. Biol. 2007, 14:647-652.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 647-652
    • Büttner, K.1    Nehring, S.2    Hopfner, K.-P.3
  • 3
    • 84897128298 scopus 로고    scopus 로고
    • The noncoding RNA revolution-trashing old rules to forge new ones
    • Cech T.R., Steitz J.A. The noncoding RNA revolution-trashing old rules to forge new ones. Cell 2014, 157:77-94.
    • (2014) Cell , vol.157 , pp. 77-94
    • Cech, T.R.1    Steitz, J.A.2
  • 5
    • 84875174459 scopus 로고    scopus 로고
    • RNA helicases in splicing
    • Cordin O., Beggs J.D. RNA helicases in splicing. RNA Biol. 2013, 10:83-95.
    • (2013) RNA Biol. , vol.10 , pp. 83-95
    • Cordin, O.1    Beggs, J.D.2
  • 8
    • 0033166348 scopus 로고    scopus 로고
    • The rox1 and rox2 RNAs are essential components of the compensasome, which mediates dosage compensation in Drosophila
    • Franke A., Baker B.S. The rox1 and rox2 RNAs are essential components of the compensasome, which mediates dosage compensation in Drosophila. Mol. Cell 1999, 4:117-122.
    • (1999) Mol. Cell , vol.4 , pp. 117-122
    • Franke, A.1    Baker, B.S.2
  • 9
    • 84876374789 scopus 로고    scopus 로고
    • Structural insights into RISC assembly facilitated by dsRNA-binding domains of human RNA helicase A (DHX9)
    • Fu Q., Yuan Y.A. Structural insights into RISC assembly facilitated by dsRNA-binding domains of human RNA helicase A (DHX9). Nucleic Acids Res. 2013, 41:3457-3470.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 3457-3470
    • Fu, Q.1    Yuan, Y.A.2
  • 10
    • 76249111702 scopus 로고    scopus 로고
    • Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism
    • Gu M., Rice C.M. Three conformational snapshots of the hepatitis C virus NS3 helicase reveal a ratchet translocation mechanism. Proc. Natl. Acad. Sci. USA 2010, 107:521-528.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 521-528
    • Gu, M.1    Rice, C.M.2
  • 11
    • 0034597001 scopus 로고    scopus 로고
    • Targeting the chromatin-remodeling MSL complex of Drosophila to its sites of action on the X chromosome requires both acetyl transferase and ATPase activities
    • Gu W., Wei X., Pannuti A., Lucchesi J.C. Targeting the chromatin-remodeling MSL complex of Drosophila to its sites of action on the X chromosome requires both acetyl transferase and ATPase activities. EMBO J. 2000, 19:5202-5211.
    • (2000) EMBO J. , vol.19 , pp. 5202-5211
    • Gu, W.1    Wei, X.2    Pannuti, A.3    Lucchesi, J.C.4
  • 12
    • 84055217962 scopus 로고    scopus 로고
    • The crystal structure of S. cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome
    • Halbach F., Rode M., Conti E. The crystal structure of S. cerevisiae Ski2, a DExH helicase associated with the cytoplasmic functions of the exosome. RNA 2012, 18:124-134.
    • (2012) RNA , vol.18 , pp. 124-134
    • Halbach, F.1    Rode, M.2    Conti, E.3
  • 13
    • 84882796823 scopus 로고    scopus 로고
    • The yeast ski complex: crystal structure and RNA channeling to the exosome complex
    • Halbach F., Reichelt P., Rode M., Conti E. The yeast ski complex: crystal structure and RNA channeling to the exosome complex. Cell 2013, 154:814-826.
    • (2013) Cell , vol.154 , pp. 814-826
    • Halbach, F.1    Reichelt, P.2    Rode, M.3    Conti, E.4
  • 14
    • 77649269768 scopus 로고    scopus 로고
    • Structural basis for the function of DEAH helicases
    • He Y., Andersen G.R., Nielsen K.H. Structural basis for the function of DEAH helicases. EMBO Rep. 2010, 11:180-186.
    • (2010) EMBO Rep. , vol.11 , pp. 180-186
    • He, Y.1    Andersen, G.R.2    Nielsen, K.H.3
  • 18
    • 77954952539 scopus 로고    scopus 로고
    • The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing
    • Jackson R.N., Klauer A.A., Hintze B.J., Robinson H., van Hoof A., Johnson S.J. The crystal structure of Mtr4 reveals a novel arch domain required for rRNA processing. EMBO J. 2010, 29:2205-2216.
    • (2010) EMBO J. , vol.29 , pp. 2205-2216
    • Jackson, R.N.1    Klauer, A.A.2    Hintze, B.J.3    Robinson, H.4    van Hoof, A.5    Johnson, S.J.6
  • 19
    • 78650854687 scopus 로고    scopus 로고
    • RNA helicases at work: binding and rearranging
    • Jankowsky E. RNA helicases at work: binding and rearranging. Trends Biochem. Sci. 2011, 36:19-29.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 19-29
    • Jankowsky, E.1
  • 21
    • 84927755520 scopus 로고    scopus 로고
    • The MSL complex: juggling RNA-protein interactions for dosage compensation and beyond
    • Keller C.I., Akhtar A. The MSL complex: juggling RNA-protein interactions for dosage compensation and beyond. Curr. Opin. Genet. Dev. 2015, 31:1-11.
    • (2015) Curr. Opin. Genet. Dev. , vol.31 , pp. 1-11
    • Keller, C.I.1    Akhtar, A.2
  • 22
    • 55249112898 scopus 로고    scopus 로고
    • Transcription rate of noncoding roX1 RNA controls local spreading of the Drosophila MSL chromatin remodeling complex
    • Kelley R.L., Lee O.K., Shim Y.K. Transcription rate of noncoding roX1 RNA controls local spreading of the Drosophila MSL chromatin remodeling complex. Mech. Dev. 2008, 125:1009-1019.
    • (2008) Mech. Dev. , vol.125 , pp. 1009-1019
    • Kelley, R.L.1    Lee, O.K.2    Shim, Y.K.3
  • 23
    • 0030949009 scopus 로고    scopus 로고
    • The NTPase/helicase activities of Drosophila maleless, an essential factor in dosage compensation
    • Lee C.G., Chang K.A., Kuroda M.I., Hurwitz J. The NTPase/helicase activities of Drosophila maleless, an essential factor in dosage compensation. EMBO J. 1997, 16:2671-2681.
    • (1997) EMBO J. , vol.16 , pp. 2671-2681
    • Lee, C.G.1    Chang, K.A.2    Kuroda, M.I.3    Hurwitz, J.4
  • 25
    • 84863396955 scopus 로고    scopus 로고
    • Roles of long, non-coding RNA in chromosome-wide transcription regulation: lessons from two dosage compensation systems
    • Maenner S., Müller M., Becker P.B. Roles of long, non-coding RNA in chromosome-wide transcription regulation: lessons from two dosage compensation systems. Biochimie 2012, 94:1490-1498.
    • (2012) Biochimie , vol.94 , pp. 1490-1498
    • Maenner, S.1    Müller, M.2    Becker, P.B.3
  • 26
    • 84880421665 scopus 로고    scopus 로고
    • ATP-dependent roX RNA remodeling by the helicase maleless enables specific association of MSL proteins
    • Maenner S., Müller M., Fröhlich J., Langer D., Becker P.B. ATP-dependent roX RNA remodeling by the helicase maleless enables specific association of MSL proteins. Mol. Cell 2013, 51:174-184.
    • (2013) Mol. Cell , vol.51 , pp. 174-184
    • Maenner, S.1    Müller, M.2    Fröhlich, J.3    Langer, D.4    Becker, P.B.5
  • 27
    • 84878270899 scopus 로고    scopus 로고
    • RNA recognition by double-stranded RNA binding domains: a matter of shape and sequence
    • Masliah G., Barraud P., Allain F.H.-T. RNA recognition by double-stranded RNA binding domains: a matter of shape and sequence. Cell. Mol. Life Sci. 2013, 70:1875-1895.
    • (2013) Cell. Mol. Life Sci. , vol.70 , pp. 1875-1895
    • Masliah, G.1    Barraud, P.2    Allain, F.H.-T.3
  • 29
    • 0033953362 scopus 로고    scopus 로고
    • Dosage compensation: making 1X equal 2X
    • Meller V.H. Dosage compensation: making 1X equal 2X. Trends Cell Biol. 2000, 10:54-59.
    • (2000) Trends Cell Biol. , vol.10 , pp. 54-59
    • Meller, V.H.1
  • 30
    • 0036500632 scopus 로고    scopus 로고
    • The roX genes encode redundant male-specific lethal transcripts required for targeting of the MSL complex
    • Meller V.H., Rattner B.P. The roX genes encode redundant male-specific lethal transcripts required for targeting of the MSL complex. EMBO J. 2002, 21:1084-1091.
    • (2002) EMBO J. , vol.21 , pp. 1084-1091
    • Meller, V.H.1    Rattner, B.P.2
  • 31
    • 84907321145 scopus 로고    scopus 로고
    • UNR facilitates the interaction of MLE with the lncRNA roX2 during Drosophila dosage compensation
    • Militti C., Maenner S., Becker P.B., Gebauer F. UNR facilitates the interaction of MLE with the lncRNA roX2 during Drosophila dosage compensation. Nat. Commun. 2014, 5:4762.
    • (2014) Nat. Commun. , vol.5 , pp. 4762
    • Militti, C.1    Maenner, S.2    Becker, P.B.3    Gebauer, F.4
  • 32
    • 38549116197 scopus 로고    scopus 로고
    • The MLE subunit of the Drosophila MSL complex uses its ATPase activity for dosage compensation and its helicase activity for targeting
    • Morra R., Smith E.R., Yokoyama R., Lucchesi J.C. The MLE subunit of the Drosophila MSL complex uses its ATPase activity for dosage compensation and its helicase activity for targeting. Mol. Cell. Biol. 2008, 28:958-966.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 958-966
    • Morra, R.1    Smith, E.R.2    Yokoyama, R.3    Lucchesi, J.C.4
  • 33
    • 79953895523 scopus 로고    scopus 로고
    • Role of the ATPase/helicase maleless (MLE) in the assembly, targeting, spreading and function of the male-specific lethal (MSL) complex of Drosophila
    • Morra R., Yokoyama R., Ling H., Lucchesi J.C. Role of the ATPase/helicase maleless (MLE) in the assembly, targeting, spreading and function of the male-specific lethal (MSL) complex of Drosophila. Epigenetics Chromatin 2011, 4:6.
    • (2011) Epigenetics Chromatin , vol.4 , pp. 6
    • Morra, R.1    Yokoyama, R.2    Ling, H.3    Lucchesi, J.C.4
  • 34
    • 77749322591 scopus 로고    scopus 로고
    • Stepwise translocation of nucleic acid motors
    • Myong S., Ha T. Stepwise translocation of nucleic acid motors. Curr. Opin. Struct. Biol. 2010, 20:121-127.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 121-127
    • Myong, S.1    Ha, T.2
  • 36
    • 37249042122 scopus 로고    scopus 로고
    • An evolutionarily conserved domain of roX2 RNA is sufficient for induction of H4-Lys16 acetylation on the Drosophila X chromosome
    • Park S.W., Kang Y.Ie., Sypula J.G., Choi J., Oh H., Park Y. An evolutionarily conserved domain of roX2 RNA is sufficient for induction of H4-Lys16 acetylation on the Drosophila X chromosome. Genetics 2007, 177:1429-1437.
    • (2007) Genetics , vol.177 , pp. 1429-1437
    • Park, S.W.1    Kang, Y.2    Sypula, J.G.3    Choi, J.4    Oh, H.5    Park, Y.6
  • 37
    • 49449085856 scopus 로고    scopus 로고
    • Regulation of histone H4 Lys16 acetylation by predicted alternative secondary structures in roX noncoding RNAs
    • Park S.W., Kuroda M.I., Park Y. Regulation of histone H4 Lys16 acetylation by predicted alternative secondary structures in roX noncoding RNAs. Mol. Cell. Biol. 2008, 28:4952-4962.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4952-4962
    • Park, S.W.1    Kuroda, M.I.2    Park, Y.3
  • 38
    • 64549117893 scopus 로고    scopus 로고
    • Dual sex-specific functions of Drosophila upstream of N-ras in the control of X chromosome dosage compensation
    • Patalano S., Mihailovich M., Belacortu Y., Paricio N., Gebauer F. Dual sex-specific functions of Drosophila upstream of N-ras in the control of X chromosome dosage compensation. Development 2009, 136:689-698.
    • (2009) Development , vol.136 , pp. 689-698
    • Patalano, S.1    Mihailovich, M.2    Belacortu, Y.3    Paricio, N.4    Gebauer, F.5
  • 39
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle A.M. Translocation and unwinding mechanisms of RNA and DNA helicases. Annu. Rev. Biophys. 2008, 37:317-336.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 40
    • 0034101060 scopus 로고    scopus 로고
    • The mle(napts) RNA helicase mutation in Drosophila results in a splicing catastrophe of the para Na+ channel transcript in a region of RNA editing
    • Reenan R.A., Hanrahan C.J., Ganetzky B. The mle(napts) RNA helicase mutation in Drosophila results in a splicing catastrophe of the para Na+ channel transcript in a region of RNA editing. Neuron 2000, 25:139-149.
    • (2000) Neuron , vol.25 , pp. 139-149
    • Reenan, R.A.1    Hanrahan, C.J.2    Ganetzky, B.3
  • 41
    • 0030089613 scopus 로고    scopus 로고
    • RNA-dependent association of the Drosophila maleless protein with the male X chromosome
    • Richter L., Bone J.R., Kuroda M.I. RNA-dependent association of the Drosophila maleless protein with the male X chromosome. Genes Cells 1996, 1:325-336.
    • (1996) Genes Cells , vol.1 , pp. 325-336
    • Richter, L.1    Bone, J.R.2    Kuroda, M.I.3
  • 43
    • 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. Structural basis for RNA unwinding by the DEAD-box protein Drosophila Vasa. Cell 2006, 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
  • 45
    • 33845768982 scopus 로고    scopus 로고
    • Dosage compensation: the beginning and end of generalization
    • Straub T., Becker P.B. Dosage compensation: the beginning and end of generalization. Nat. Rev. Genet. 2007, 8:47-57.
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 47-57
    • Straub, T.1    Becker, P.B.2
  • 47
    • 0042208405 scopus 로고    scopus 로고
    • Functional redundancy within roX1, a noncoding RNA involved in dosage compensation in Drosophila melanogaster
    • Stuckenholz C., Meller V.H., Kuroda M.I. Functional redundancy within roX1, a noncoding RNA involved in dosage compensation in Drosophila melanogaster. Genetics 2003, 164:1003-1014.
    • (2003) Genetics , vol.164 , pp. 1003-1014
    • Stuckenholz, C.1    Meller, V.H.2    Kuroda, M.I.3
  • 49
    • 84884849501 scopus 로고    scopus 로고
    • Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins
    • von Moeller H., Lerner R., Ricciardi A., Basquin C., Marzluff W.F., Conti E. Structural and biochemical studies of SLIP1-SLBP identify DBP5 and eIF3g as SLIP1-binding proteins. Nucleic Acids Res. 2013, 41:7960-7971.
    • (2013) Nucleic Acids Res. , vol.41 , pp. 7960-7971
    • von Moeller, H.1    Lerner, R.2    Ricciardi, A.3    Basquin, C.4    Marzluff, W.F.5    Conti, E.6
  • 51
    • 77955453339 scopus 로고    scopus 로고
    • Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance
    • Weir J.R., Bonneau F., Hentschel J., Conti E. Structural analysis reveals the characteristic features of Mtr4, a DExH helicase involved in nuclear RNA processing and surveillance. Proc. Natl. Acad. Sci. USA 2010, 107:12139-12144.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12139-12144
    • Weir, J.R.1    Bonneau, F.2    Hentschel, J.3    Conti, E.4


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