메뉴 건너뛰기




Volumn 42, Issue 22, 2014, Pages 13897-13910

Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CARBOXY TERMINAL SEC63 DOMAIN PROTEIN; MUTANT PROTEIN; NUCLEIC ACID BINDING PROTEIN; PROTEIN BRR2P; RNA HELICASE; RNA HELICASE PRP16P; UNCLASSIFIED DRUG; BRR2 PROTEIN, S CEREVISIAE; DEAD BOX PROTEIN; PRP16 PROTEIN, S CEREVISIAE; PRP2 PROTEIN, S CEREVISIAE; RNA; SACCHAROMYCES CEREVISIAE PROTEIN; SMALL NUCLEAR RIBONUCLEOPROTEIN; SNRNP200 PROTEIN, HUMAN;

EID: 84927665216     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku1238     Document Type: Article
Times cited : (12)

References (44)
  • 2
    • 84875174459 scopus 로고    scopus 로고
    • RNA helicases in splicing
    • Cordin, O. and Beggs, J. D. (2013) RNA helicases in splicing. RNA Biol., 10, 83-95.
    • (2013) RNA Biol. , vol.10 , pp. 83-95
    • Cordin, O.1    Beggs, J.D.2
  • 3
    • 84861984263 scopus 로고    scopus 로고
    • Structure, function and regulation of spliceosomal RNA helicases
    • Cordin, O., Hahn, D. and Beggs, J. D. (2012) Structure, function and regulation of spliceosomal RNA helicases. Curr. Opin. Cell Biol., 24, 431-438.
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 431-438
    • Cordin, O.1    Hahn, D.2    Beggs, J.D.3
  • 4
    • 0034857262 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: From generic motors to specific dissociation functions
    • Tanner, N. K. and Linder, P. (2001) DExD/H box RNA helicases: from generic motors to specific dissociation functions. Mol. Cell, 8, 251-262.
    • (2001) Mol. Cell , vol.8 , pp. 251-262
    • Tanner, N.K.1    Linder, P.2
  • 5
    • 0032537739 scopus 로고    scopus 로고
    • RNA unwinding in U4/U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2
    • Raghunathan, P. L. and Guthrie, C. (1998) RNA unwinding in U4/U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2. Curr. Biol., 8, 847-855.
    • (1998) Curr. Biol. , vol.8 , pp. 847-855
    • Raghunathan, P.L.1    Guthrie, C.2
  • 6
    • 84868592766 scopus 로고    scopus 로고
    • Brr2p-mediated conformational rearrangements in the spliceosome during activation and substrate repositioning
    • Hahn, D., Kudla, G., Tollervey, D. and Beggs, J. D. (2012) Brr2p-mediated conformational rearrangements in the spliceosome during activation and substrate repositioning. Genes Dev., 26, 2408-2421.
    • (2012) Genes Dev. , vol.26 , pp. 2408-2421
    • Hahn, D.1    Kudla, G.2    Tollervey, D.3    Beggs, J.D.4
  • 7
    • 33746441457 scopus 로고    scopus 로고
    • The EF-G-like GTPase Snu114p regulates spliceosome dynamics mediated by Brr2p, a DExD/H box ATPase
    • Small, E. C, Leggett, S. R., Winans, A. A. and Staley, J. P. (2006) The EF-G-like GTPase Snu114p regulates spliceosome dynamics mediated by Brr2p, a DExD/H box ATPase. Mol. Cell, 23, 389-399.
    • (2006) Mol. Cell , vol.23 , pp. 389-399
    • Small, E.C.1    Leggett, S.R.2    Winans, A.A.3    Staley, J.P.4
  • 8
    • 84874268195 scopus 로고    scopus 로고
    • Dissection of the factor requirements for spliceosome disassembly and the elucidation of its dissociation products using a purified splicing system
    • Fourmann, J. B., Schmitzova, J., Christian, H., Urlaub, H., Ficner, R., Boon, K. L., Fabrizio, P. and Luhrmann, R. (2013) Dissection of the factor requirements for spliceosome disassembly and the elucidation of its dissociation products using a purified splicing system. Genes Dev., 27, 413-428.
    • (2013) Genes Dev. , vol.27 , pp. 413-428
    • Fourmann, J.B.1    Schmitzova, J.2    Christian, H.3    Urlaub, H.4    Ficner, R.5    Boon, K.L.6    Fabrizio, P.7    Luhrmann, R.8
  • 9
    • 84901464971 scopus 로고    scopus 로고
    • Novel regulatory principles of the spliceosomal Brr2 RNA helicase and links to retinal disease in humans
    • Mozaffari-Jovin, S., Wandersleben, T., Santos, K. F., Will, C. L., Lührmann, R. and Wahl, M. C. (2014) Novel regulatory principles of the spliceosomal Brr2 RNA helicase and links to retinal disease in humans. RNA Biol, 11, 298-312.
    • (2014) RNA Biol , vol.11 , pp. 298-312
    • Mozaffari-Jovin, S.1    Wandersleben, T.2    Santos, K.F.3    Will, C.L.4    Lührmann, R.5    Wahl, M.C.6
  • 10
    • 0032515969 scopus 로고    scopus 로고
    • The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro
    • Laggerbauer, B., Achsel, T. and Luhrmann, R. (1998) The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro. Proc. Natl. Acad. Sci. U. S. A., 95, 4188-4192.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 4188-4192
    • Laggerbauer, B.1    Achsel, T.2    Luhrmann, R.3
  • 13
    • 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, A. K. and 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, 42-48.
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 42-48
    • Maeder, C.1    Kutach, A.K.2    Guthrie, C.3
  • 14
    • 84868583242 scopus 로고    scopus 로고
    • The Prp8 RNase H-like domain inhibits Brr2-mediated U4/U6 snRNA unwinding by blocking Brr2 loading onto the U4 snRNA
    • Mozaffari-Jovin, S., Santos, K. F., Hsiao, H. H., Will, C. L., Urlaub, H., Wahl, M. C. and Luhrmann, R. (2012) The Prp8 RNase H-like domain inhibits Brr2-mediated U4/U6 snRNA unwinding by blocking Brr2 loading onto the U4 snRNA. Genes Dev., 26, 2422-2434.
    • (2012) Genes Dev. , vol.26 , pp. 2422-2434
    • Mozaffari-Jovin, S.1    Santos, K.F.2    Hsiao, H.H.3    Will, C.L.4    Urlaub, H.5    Wahl, M.C.6    Luhrmann, R.7
  • 15
    • 84879797997 scopus 로고    scopus 로고
    • Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8
    • Mozaffari-Jovin, S., Wandersleben, T, Santos, K. F., Will, C. L., Luhrmann, R. and Wahl, M. C. (2013) Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8. Science, 341, 80-84.
    • (2013) Science , vol.341 , pp. 80-84
    • Mozaffari-Jovin, S.1    Wandersleben, T.2    Santos, K.F.3    Will, C.L.4    Luhrmann, R.5    Wahl, M.C.6
  • 16
    • 84878849387 scopus 로고    scopus 로고
    • Structural basis of Brr2-Prp8 interactions and implications for U5 snRNP biogenesis and the spliceosome active site
    • Nguyen, TH. D., Li, J., Galej, W. P, Oshikane, H., Newman, A. J. and Nagai, K. (2013) Structural basis of Brr2-Prp8 interactions and implications for U5 snRNP biogenesis and the spliceosome active site. Structure, 21, 910-919.
    • (2013) Structure , vol.21 , pp. 910-919
    • Nguyen, T.H.D.1    Li, J.2    Galej, W.P.3    Oshikane, H.4    Newman, A.J.5    Nagai, K.6
  • 17
    • 69149090973 scopus 로고    scopus 로고
    • Common design principles in the spliceosomal RNA helicase Brr2 and in the Hel308 DNA helicase
    • Pena, V., Jovin, S. M., Fabrizio, P, Orlowski, J., Bujnicki, J. M., Luhrmann, R. and Wahl, M. C. (2009) Common design principles in the spliceosomal RNA helicase Brr2 and in the Hel308 DNA helicase. Mol. Cell, 35, 454-466.
    • (2009) Mol. Cell , vol.35 , pp. 454-466
    • Pena, V.1    Jovin, S.M.2    Fabrizio, P.3    Orlowski, J.4    Bujnicki, J.M.5    Luhrmann, R.6    Wahl, M.C.7
  • 18
    • 84867913431 scopus 로고    scopus 로고
    • Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome
    • Santos, K. F., Jovin, S. M., Weber, G, Pena, V, Luhrmann, R. and Wahl, M. C. (2012) Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome. Proc. Natl. Acad. Sci. U. S. A., 109, 17418-17423.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 17418-17423
    • Santos, K.F.1    Jovin, S.M.2    Weber, G.3    Pena, V.4    Luhrmann, R.5    Wahl, M.C.6
  • 20
    • 0033056712 scopus 로고    scopus 로고
    • The first ATPase domain of the yeast 246-kDa protein is required for in vivo unwinding of the U4/U6 duplex
    • Kim, D. H. and Rossi, J. J. (1999) The first ATPase domain of the yeast 246-kDa protein is required for in vivo unwinding of the U4/U6 duplex. RNA, 5, 959-971.
    • (1999) RNA , vol.5 , pp. 959-971
    • Kim, D.H.1    Rossi, J.J.2
  • 21
    • 0035053295 scopus 로고    scopus 로고
    • Functional contacts with a range of splicing proteins suggest a central role for Brr2p in the dynamic control of the order of events in spliceosomes of Saccharomyces cerevisiae
    • van Nues, R. W. and Beggs, J. D. (2001) Functional contacts with a range of splicing proteins suggest a central role for Brr2p in the dynamic control of the order of events in spliceosomes of Saccharomyces cerevisiae. Genetics, 157, 1451-1467.
    • (2001) Genetics , vol.157 , pp. 1451-1467
    • Van Nues, R.W.1    Beggs, J.D.2
  • 22
    • 84873041707 scopus 로고    scopus 로고
    • Link of NTR-Mediated Spliceosome Disassembly with DEAH-Box ATPases Prp2, Prp16, and Prp22
    • Chen, H. C, Tseng, C. K., Tsai, R. T, Chung, C. S. and Cheng, S. C. (2013) Link of NTR-Mediated Spliceosome Disassembly with DEAH-Box ATPases Prp2, Prp16, and Prp22. Mol. Cell. Biol, 33, 514-525.
    • (2013) Mol. Cell. Biol , vol.33 , pp. 514-525
    • Chen, H.C.1    Tseng, C.K.2    Tsai, R.T.3    Chung, C.S.4    Cheng, S.C.5
  • 23
    • 84871880170 scopus 로고    scopus 로고
    • The interaction of Prp2 with a defined region of the intron is required for the first splicing reaction
    • Liu, H. L. and Cheng, S. C. (2012) The interaction of Prp2 with a defined region of the intron is required for the first splicing reaction. Mol. Cell. Biol, 32, 5056-5066.
    • (2012) Mol. Cell. Biol , vol.32 , pp. 5056-5066
    • Liu, H.L.1    Cheng, S.C.2
  • 24
    • 0030963019 scopus 로고    scopus 로고
    • Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens
    • Fromont-Racine, M., Rain, J. C. and Legrain, P (1997) Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nat. Genet., 16, 277-282.
    • (1997) Nat. Genet. , vol.16 , pp. 277-282
    • Fromont-Racine, M.1    Rain, J.C.2    Legrain, P.3
  • 25
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M. S., McKenzie, A. 3rd, Demarini, D. J., Shah, NG, Wach, A., Brachat, A., Philippsen, P and Pringle, J. R. (1998) Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast, 14, 953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 26
    • 0021668558 scopus 로고
    • A positive selection for mutants lacking orotidine-5'-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance
    • Boeke, J. D, LaCroute, F. and Fink, GR. (1984) A positive selection for mutants lacking orotidine-5'-phosphate decarboxylase activity in yeast: 5-fluoro-orotic acid resistance. Mol. Gen. Genet., 197, 345-346.
    • (1984) Mol. Gen. Genet. , vol.197 , pp. 345-346
    • Boeke, J.D.1    LaCroute, F.2    Fink, G.R.3
  • 27
    • 4444271170 scopus 로고    scopus 로고
    • A versatile toolbox for PCR-based tagging of yeast genes: New fluorescent proteins, more markers and promoter substitution cassettes
    • Janke, C., Magiera, M. M., Rathfelder, N., Taxis, C., Reber, S., Maekawa, H., Moreno-Borchart, A., Doenges, G., Schwob, E., Schiebel, E. et al. (2004) A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast, 21, 947-962.
    • (2004) Yeast , vol.21 , pp. 947-962
    • Janke, C.1    Magiera, M.M.2    Rathfelder, N.3    Taxis, C.4    Reber, S.5    Maekawa, H.6    Moreno-Borchart, A.7    Doenges, G.8    Schwob, E.9    Schiebel, E.10
  • 29
    • 3342957251 scopus 로고    scopus 로고
    • The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity
    • Cordin, O., Tanner, N. K., Doere, M., Linder, P. and Banroques, J. (2004) The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity. EMBO J., 23, 2478-2487.
    • (2004) EMBO J. , vol.23 , pp. 2478-2487
    • Cordin, O.1    Tanner, N.K.2    Doere, M.3    Linder, P.4    Banroques, J.5
  • 30
    • 84869469029 scopus 로고    scopus 로고
    • Structural analysis of the C-terminal domain of the spliceosomal helicase Prp22
    • Kudlinzki, D., Schmitt, A., Christian, H. and Ficner, R. (2012) Structural analysis of the C-terminal domain of the spliceosomal helicase Prp22. Biol. Chem., 393, 1131-1140.
    • (2012) Biol. Chem. , vol.393 , pp. 1131-1140
    • Kudlinzki, D.1    Schmitt, A.2    Christian, H.3    Ficner, R.4
  • 32
    • 23944469448 scopus 로고    scopus 로고
    • The Isy1p component of the NineTeen complex interacts with the ATPase Prp16p to regulate the fidelity of pre-mRNA splicing
    • Villa, T. and Guthrie, C. (2005) The Isy1p component of the NineTeen complex interacts with the ATPase Prp16p to regulate the fidelity of pre-mRNA splicing. Genes Dev., 19, 1894-1904.
    • (2005) Genes Dev. , vol.19 , pp. 1894-1904
    • Villa, T.1    Guthrie, C.2
  • 33
    • 0026656540 scopus 로고
    • A dominant negative mutation in a spliceosomal ATPase affects ATP hydrolysis but not binding to the spliceosome
    • Schwer, B. and Guthrie, C. (1992) A dominant negative mutation in a spliceosomal ATPase affects ATP hydrolysis but not binding to the spliceosome. Mol. Cell. Biol., 12, 3540-3547.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3540-3547
    • Schwer, B.1    Guthrie, C.2
  • 34
    • 0031800746 scopus 로고    scopus 로고
    • Mutational analysis of the yeast DEAH-box splicing factor Prp16
    • Hotz, H. R. and Schwer, B. (1998) Mutational analysis of the yeast DEAH-box splicing factor Prp16. Genetics, 149, 807-815.
    • (1998) Genetics , vol.149 , pp. 807-815
    • Hotz, H.R.1    Schwer, B.2
  • 35
    • 0026019713 scopus 로고
    • PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome
    • Schwer, B. and Guthrie, C. (1991) PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome. Nature, 349, 494-499.
    • (1991) Nature , vol.349 , pp. 494-499
    • Schwer, B.1    Guthrie, C.2
  • 36
    • 80053567694 scopus 로고    scopus 로고
    • RNAhelicases and remodeling proteins
    • Pyle, A. M. (2011) RNAhelicases and remodeling proteins. Curr. Opin. Chem. Biol., 15, 636-642.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 636-642
    • Pyle, A.M.1
  • 37
    • 0028276521 scopus 로고
    • Genetic interactions between the yeast RNA helicase homolog Prp16 and spliceosomal snRNAs identify candidate ligands for the Prp16 RNA-dependent ATPase
    • Madhani, H. D. and Guthrie, C. (1994) Genetic interactions between the yeast RNA helicase homolog Prp16 and spliceosomal snRNAs identify candidate ligands for the Prp16 RNA-dependent ATPase. Genetics, 137, 677-687.
    • (1994) Genetics , vol.137 , pp. 677-687
    • Madhani, H.D.1    Guthrie, C.2
  • 38
    • 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
  • 39
    • 62549144414 scopus 로고    scopus 로고
    • The current understanding of Ded1p/DDX3 homologs from yeast to human
    • Tarn, W. Y. and Chang, T. H. (2009) The current understanding of Ded1p/DDX3 homologs from yeast to human. RNA Biol, 6, 17-20.
    • (2009) RNA Biol , vol.6 , pp. 17-20
    • Tarn, W.Y.1    Chang, T.H.2
  • 40
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: Design principles of a dynamic RNP machine
    • Wahl, M. C, Will, C. L. and Luhrmann, R. (2009) The spliceosome: design principles of a dynamic RNP machine. Cell, 136, 701-718.
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Luhrmann, R.3
  • 41
    • 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
  • 42
    • 77649269768 scopus 로고    scopus 로고
    • Structural basis for the function of DEAH helicases
    • He, Y, Andersen, G. R. and Nielsen, K. H. (2010) Structural basis for the function of DEAH helicases. EMBO Rep., 11, 180-186.
    • (2010) EMBO Rep. , vol.11 , pp. 180-186
    • He, Y.1    Andersen, G.R.2    Nielsen, K.H.3
  • 44
    • 77955488349 scopus 로고    scopus 로고
    • The DEAH box ATPases Prp16 and Prp43 cooperate to proofread 5' splice site cleavage during Pre-mRNA splicing
    • Koodathingal, P, Novak, T, Piccirilli, J. A. and Staley, J. P (2010) The DEAH box ATPases Prp16 and Prp43 cooperate to proofread 5' splice site cleavage during Pre-mRNA splicing. Mol. Cell, 39, 385-395.
    • (2010) Mol. Cell , vol.39 , pp. 385-395
    • Koodathingal, P.1    Novak, T.2    Piccirilli, J.A.3    Staley, J.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.