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Volumn 33, Issue 3, 2013, Pages 514-525

Link of NTR-mediated spliceosome disassembly with DEAH-box ATpases PrP2, PrP16, and PrP22

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; NTR1 PROTEIN; NTR2 PROTEIN; PROTEIN; PRP16 PROTEIN; PRP2 PROTEIN; PRP22 PROTEIN; PRP43 PROTEIN; RNA HELICASE; UNCLASSIFIED DRUG;

EID: 84873041707     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01093-12     Document Type: Article
Times cited : (32)

References (59)
  • 1
    • 0036948420 scopus 로고    scopus 로고
    • Allosteric cascade of spliceosome activation
    • Brow DA. 2002. Allosteric cascade of spliceosome activation. Annu. Rev. Genet. 36:333-360.
    • (2002) Annu. Rev. Genet. , vol.36 , pp. 333-360
    • Brow, D.A.1
  • 2
    • 0001468848 scopus 로고    scopus 로고
    • Splicing of precursors to mRNAs by the spliceosome
    • Gesteland RF, Cech TR, Atkins JF (ed), 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Burge CB, Tuschl TH, Sharp PA. 1999. Splicing of precursors to mRNAs by the spliceosome, p 525-560. In Gesteland RF, Cech TR, Atkins JF (ed), The RNA world, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1999) The RNA world , pp. 525-560
    • Burge, C.B.1    Tuschl, T.H.2    Sharp, P.A.3
  • 3
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: design principles of a dynamic RNP machine
    • Wahl MC, Will CL, Lührmann RL. 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    Lührmann, R.L.3
  • 4
    • 33645213731 scopus 로고    scopus 로고
    • Spliceosome structure and function
    • Gesteland RF, Cech TR, Atkins JF (ed), 3rd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Will CL, Lührmann R. 2006. Spliceosome structure and function, p 369-400. In Gesteland RF, Cech TR, Atkins JF (ed), The RNA world, 3rd ed. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
    • (2006) The RNA world , pp. 369-400
    • Will, C.L.1    Lührmann, R.2
  • 5
    • 42249093677 scopus 로고    scopus 로고
    • Isolation of an active step I spliceosome and composition of its RNP core
    • Bessonov S, Anokhina M, Will CL, Urlaub H, Lührmann R. 2008. Isolation of an active step I spliceosome and composition of its RNP core. Nature 452:846-850.
    • (2008) Nature , vol.452 , pp. 846-850
    • Bessonov, S.1    Anokhina, M.2    Will, C.L.3    Urlaub, H.4    Lührmann, R.5
  • 6
    • 24744465409 scopus 로고    scopus 로고
    • The Prp19-associated complex is required for specifying interactions of U5 and U6 with pre-mRNA during spliceo-some activation
    • Chan S-P, Cheng S-C. 2005. The Prp19-associated complex is required for specifying interactions of U5 and U6 with pre-mRNA during spliceo-some activation. J. Biol. Chem. 280:31190-31199.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31190-31199
    • Chan, S.-P.1    Cheng, S.-C.2
  • 7
    • 0141924550 scopus 로고    scopus 로고
    • The Prp19p-associated complex in spliceosome activation
    • Chan S-P, Kao D-I, Tsai W-Y, Cheng S-C. 2003. The Prp19p-associated complex in spliceosome activation. Science 302:279-282.
    • (2003) Science , vol.302 , pp. 279-282
    • Chan, S.-P.1    Kao, D.-I.2    Tsai, W-Y.3    Cheng, S.-C.4
  • 9
    • 3242737496 scopus 로고    scopus 로고
    • A subset of human 35S U5 proteins, including Prp19, function prior to catalytic step 1 of splicing
    • Makarova OV, Makarov EM, Urlaub H, Will CL, Gentzel M, Wilm M, LührmannR. 2004. A subset of human 35S U5 proteins, including Prp19, function prior to catalytic step 1 of splicing. EMBO J. 23:2381-2391.
    • (2004) EMBO J. , vol.23 , pp. 2381-2391
    • Makarova, O.V.1    Makarov, E.M.2    Urlaub, H.3    Will, C.L.4    Gentzel, M.5    Wilm, M.6    Lührmann, R.7
  • 10
    • 0036188450 scopus 로고    scopus 로고
    • ATP-dependent remodeling of the spliceosome: intragenic suppressors of release-defective mutants of Sac-charomyces cerevisiae Prp22
    • Campodonico E, Schwer B. 2002. ATP-dependent remodeling of the spliceosome: intragenic suppressors of release-defective mutants of Sac-charomyces cerevisiae Prp22. Genetics 160:407-415.
    • (2002) Genetics , vol.160 , pp. 407-415
    • Campodonico, E.1    Schwer, B.2
  • 11
    • 0035105921 scopus 로고    scopus 로고
    • Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate the requirement of Prp28p, an essential DEAD box splicing factor
    • Chen JY-F, Stands L, Staley JP, Jackups RR, Jr, Latus LJ, Chang T-H. 2001. Specific alterations of U1-C protein or U1 small nuclear RNA can eliminate the requirement of Prp28p, an essential DEAD box splicing factor. Mol. Cell 7:227-232.
    • (2001) Mol. Cell , vol.7 , pp. 227-232
    • Chen, J.Y.-F.1    Stands, L.2    Staley, J.P.3    Jackups Jr., R.R.4    Latus, L.J.5    Chang, T.-H.6
  • 12
    • 0032537739 scopus 로고    scopus 로고
    • RNA unwinding in U4/U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2
    • Raghunathan PL, 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
  • 13
    • 0035147544 scopus 로고    scopus 로고
    • A new twist on RNA helicases: DExH/D box proteins as RNPases
    • Schwer B. 2001. A new twist on RNA helicases: DExH/D box proteins as RNPases. Nat. Struct. Biol. 8:113-116.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 113-116
    • Schwer, B.1
  • 14
    • 0027065506 scopus 로고
    • A conformational rearrangement in the spliceosome is dependent on PRP16 and ATP hydrolysis
    • Schwer B, Guthrie C. 1992. A conformational rearrangement in the spliceosome is dependent on PRP16 and ATP hydrolysis. EMBO J. 11: 5033-5040.
    • (1992) EMBO J. , vol.11 , pp. 5033-5040
    • Schwer, B.1    Guthrie, C.2
  • 15
    • 0033010430 scopus 로고    scopus 로고
    • An RNA switch at the 5= splice site requires ATP and the DEAD box protein Prp28p
    • Staley JP, Guthrie C. 1999. An RNA switch at the 5= splice site requires ATP and the DEAD box protein Prp28p. Mol. Cell 3:55-64.
    • (1999) Mol. Cell , vol.3 , pp. 55-64
    • Staley, J.P.1    Guthrie, C.2
  • 16
    • 0030611640 scopus 로고    scopus 로고
    • U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction
    • Fleckner J, Zhang M, Valcárcel J, Green MR. 1997. U2AF65 recruits a novel human DEAD box protein required for the U2 snRNP-branchpoint interaction. Genes Dev. 11:1864-1872.
    • (1997) Genes Dev. , vol.11 , pp. 1864-1872
    • Fleckner, J.1    Zhang, M.2    Valcárcel, J.3    Green, M.R.4
  • 17
    • 0035177309 scopus 로고    scopus 로고
    • Deletion of MUD2, the yeast homolog of U2AF65, can bypass the requirement for Sub2, an essential spliceosomal ATPase
    • Kistler AL, Guthrie C. 2001. Deletion of MUD2, the yeast homolog of U2AF65, can bypass the requirement for Sub2, an essential spliceosomal ATPase. Genes Dev. 15:42-49.
    • (2001) Genes Dev. , vol.15 , pp. 42-49
    • Kistler, A.L.1    Guthrie, C.2
  • 18
    • 0027428138 scopus 로고
    • Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact to promote U2 snRNP binding to pre-mRNA
    • Ruby SW, Chang T-H, Abelson J. 1993. Four yeast spliceosomal proteins (PRP5, PRP9, PRP11, and PRP21) interact to promote U2 snRNP binding to pre-mRNA. Genes Dev. 7:1909-1925.
    • (1993) Genes Dev. , vol.7 , pp. 1909-1925
    • Ruby, S.W.1    Chang, T.-H.2    Abelson, J.3
  • 19
    • 0028799447 scopus 로고
    • Characterization and functional ordering of Slu7p and Prp17p during the second step of pre-mRNA splicing in yeast
    • Jones MH, Frank DN, Guthrie C. 1995. Characterization and functional ordering of Slu7p and Prp17p during the second step of pre-mRNA splicing in yeast. Proc. Natl. Acad. Sci. U. S. A. 92:9687-9691.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9687-9691
    • Jones, M.H.1    Frank, D.N.2    Guthrie, C.3
  • 20
    • 0029965552 scopus 로고    scopus 로고
    • Spliceosome activation by PRP2 ATPase prior to the first transesterification reaction of pre-mRNA splicing
    • Kim S-H, Lin R-J. 1996. Spliceosome activation by PRP2 ATPase prior to the first transesterification reaction of pre-mRNA splicing. Mol. Cell. Biol. 16:6810-6819.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6810-6819
    • Kim, S.-H.1    Lin, R.-J.2
  • 21
    • 77149180424 scopus 로고    scopus 로고
    • Release of SF3 from the intron branchpoint activates the first step of pre-mRNA splicing
    • Lardelli RM, Thompson JX, Yates JR, III, Stevens SW. 2010. Release of SF3 from the intron branchpoint activates the first step of pre-mRNA splicing. RNA 16:516-528.
    • (2010) RNA , vol.16 , pp. 516-528
    • Lardelli, R.M.1    Thompson, J.X.2    Yates, J.R.3    Stevens, S.W.4
  • 23
    • 78650446117 scopus 로고    scopus 로고
    • DEAH-box ATPase Prp16 has dual roles in remodeling of the spliceosome in catalytic steps
    • Tseng C-K, Liu H-L, Cheng S-C. 2011. DEAH-box ATPase Prp16 has dual roles in remodeling of the spliceosome in catalytic steps. RNA 17: 145-154.
    • (2011) RNA , vol.17 , pp. 145-154
    • Tseng, C.-K.1    Liu, H.-L.2    Cheng, S.-C.3
  • 25
    • 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. U. S. A. 94:11798-11802.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11798-11802
    • Arenas, J.E.1    Abelson, J.N.2
  • 26
    • 0026088747 scopus 로고
    • Requirement of the RNA helicase- like protein PRP22 for release of messenger RNA from spliceosomes
    • Company M, Arenas J, Abelson J. 1991. Requirement of the RNA helicase- like protein PRP22 for release of messenger RNA from spliceosomes. Nature 349:487-493.
    • (1991) Nature , vol.349 , pp. 487-493
    • Company, M.1    Arenas, J.2    Abelson, J.3
  • 27
    • 0037124096 scopus 로고    scopus 로고
    • Prp43 is an essential RNAdependent ATPase required for release of lariat-intron from the spliceosome
    • Martin A, Schneider S, Schwer B. 2002. Prp43 is an essential RNAdependent ATPase required for release of lariat-intron from the spliceosome. J. Biol. Chem. 277:17743-17750.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17743-17750
    • Martin, A.1    Schneider, S.2    Schwer, B.3
  • 28
    • 0032525149 scopus 로고    scopus 로고
    • The DEAH-box protein PRP22 is an ATPase that mediates ATPdependent mRNA release from the spliceosome and unwinds RNA duplexes
    • Wagner JD, Jankowsky E, Company M, Pyle AM, Abelson JN. 1998. The DEAH-box protein PRP22 is an ATPase that mediates ATPdependent mRNA release from the spliceosome and unwinds RNA duplexes. EMBO J. 17:2926-2937.
    • (1998) EMBO J. , vol.17 , pp. 2926-2937
    • Wagner, J.D.1    Jankowsky, E.2    Company, M.3    Pyle, A.M.4    Abelson, J.N.5
  • 29
    • 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. 16:42-48.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 42-48
    • Maeder, C.1    Kutach, A.K.2    Guthrie, C.3
  • 30
    • 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: 2312-2325.
    • (2007) Genes Dev. , vol.21 , pp. 2312-2325
    • Tanaka, N.1    Aronova, A.2    Schwer, B.3
  • 32
    • 33746441457 scopus 로고    scopus 로고
    • The EF-G-like GTPase Snu114p regulates spliceosome dynamics mediated by Brr2p, a DExD/H box ATPase
    • Small EC, Leggett SR, Winans AA, Staley JP. 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
  • 33
    • 43249119932 scopus 로고    scopus 로고
    • Modifications target spliceosome dynamics
    • Maeder C, Guthrie C. 2008. Modifications target spliceosome dynamics. Nat. Struct. Mol. Biol. 15:426-428.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 426-428
    • Maeder, C.1    Guthrie, C.2
  • 34
    • 43249109907 scopus 로고    scopus 로고
    • Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome
    • Mathew R, Hartmuth K, Möhlmann S, Urlaub H, Ficner R, Lührmann R. 2008. Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome. Nat. Struct. Mol. Biol. 15:435-443.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 435-443
    • Mathew, R.1    Hartmuth, K.2    Möhlmann, S.3    Urlaub, H.4    Ficner, R.5    Lührmann, R.6
  • 37
    • 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 R-T, Tseng C-K, Lee P-J, Chen H-C, Fu R-H, Chang K-J, Yeh F-L, Cheng S-C. 2007. Dynamic interactions of Ntr1-Ntr2 with Prp43 and with U5 govern the recruitment of Prp43 to mediate spliceosome disassembly. Mol. Cell. Biol. 27:8027-8037.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 8027-8037
    • Tsai, R.-T.1    Tseng, C.-K.2    Lee, P.-J.3    Chen, H.-C.4    Fu, R.-H.5    Chang, K.-J.6    Yeh, F.-L.7    Cheng, S.-C.8
  • 38
    • 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 JA, Staley JP. 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
  • 40
    • 0032055765 scopus 로고    scopus 로고
    • Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing
    • Schwer B, Gross CH. 1998. Prp22, a DExH-box RNA helicase, plays two distinct roles in yeast pre-mRNA splicing. EMBO J. 17:2086-2094.
    • (1998) EMBO J. , vol.17 , pp. 2086-2094
    • Schwer, B.1    Gross, C.H.2
  • 41
    • 34547155595 scopus 로고    scopus 로고
    • A novel splicing factor, Yju2, is associated with NTC and acts after Prp2 in promoting the first catalytic reaction of pre-mRNA splicing
    • Liu Y-C, Chen H-C, Wu N-Y, Cheng S-C. 2007. A novel splicing factor, Yju2, is associated with NTC and acts after Prp2 in promoting the first catalytic reaction of pre-mRNA splicing. Mol. Cell. Biol. 27:5403-5413.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5403-5413
    • Liu, Y.-C.1    Chen, H.-C.2    Wu, N.-Y.3    Cheng, S.-C.4
  • 42
    • 46449086933 scopus 로고    scopus 로고
    • Both catalytic steps of nuclear pre-mRNA splicing are reversible
    • Tseng C-K, Cheng S-C. 2008. Both catalytic steps of nuclear pre-mRNA splicing are reversible. Science 320:1782-1784.
    • (2008) Science , vol.320 , pp. 1782-1784
    • Tseng, C.-K.1    Cheng, S.-C.2
  • 43
    • 0035808487 scopus 로고    scopus 로고
    • Identification and characterization of two novel components of the Prp19passociated complex, Ntc30p and Ntc20p
    • Chen C-H, Tsai W-Y, Chen H-R, Wang C-H, Cheng S-C. 2001. Identification and characterization of two novel components of the Prp19passociated complex, Ntc30p and Ntc20p. J. Biol. Chem. 276:488-494.
    • (2001) J. Biol. Chem. , vol.276 , pp. 488-494
    • Chen, C.-H.1    Tsai, W.-Y.2    Chen, H.-R.3    Wang, C.-H.4    Cheng, S.-C.5
  • 44
    • 0034423411 scopus 로고    scopus 로고
    • RNA helicase dynamics in pre-mRNA splicing
    • Schwer B, Meszaros T. 2000. RNA helicase dynamics in pre-mRNA splicing. EMBO J. 19:6582-6591.
    • (2000) EMBO J. , vol.19 , pp. 6582-6591
    • Schwer, B.1    Meszaros, T.2
  • 45
    • 0022747370 scopus 로고
    • Mutations in conserved intron sequences affect multiple steps in the yeast splicing pathway, particularly assembly of the spliceosome
    • Vijayraghavan U, Parker R, Tamm J, Iimura Y, Rossi J, Abelson J, Guthrie C. 1986. Mutations in conserved intron sequences affect multiple steps in the yeast splicing pathway, particularly assembly of the spliceosome. EMBO J. 5:1683-1695.
    • (1986) EMBO J. , vol.5 , pp. 1683-1695
    • Vijayraghavan, U.1    Parker, R.2    Tamm, J.3    Iimura, Y.4    Rossi, J.5    Abelson, J.6    Guthrie, C.7
  • 46
    • 0036674909 scopus 로고    scopus 로고
    • How Slu7 and Prp18 cooperate in the second step of yeast pre-mRNA splicing
    • James S, Tirmer W, Schwer B. 2002. How Slu7 and Prp18 cooperate in the second step of yeast pre-mRNA splicing. RNA 8:1068-1077.
    • (2002) RNA , vol.8 , pp. 1068-1077
    • James, S.1    Tirmer, W.2    Schwer, B.3
  • 47
    • 70350532246 scopus 로고    scopus 로고
    • Cwc25 is a novel splicing factor required after Prp2 and Yju2 to facilitate the first catalytic reaction
    • Chiu Y-F, Liu Y-C, Chiang T-W, Yeh T-C, Tseng C-K, Wu NY, Cheng S-C. 2009. Cwc25 is a novel splicing factor required after Prp2 and Yju2 to facilitate the first catalytic reaction. Mol. Cell. Biol. 29:5671-5678.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5671-5678
    • Chiu, Y.-F.1    Liu, Y.-C.2    Chiang, T.-W.3    Yeh, T.-C.4    Tseng, C.-K.5    Wu, N.Y.6    Cheng, S.-C.7
  • 48
    • 0027404721 scopus 로고
    • Stages in the second reaction of premRNAsplicing: the final step is ATP independent
    • Horowitz DS, Abelson J. 1993. Stages in the second reaction of premRNAsplicing: the final step is ATP independent. Genes Dev. 7:320-329.
    • (1993) Genes Dev. , vol.7 , pp. 320-329
    • Horowitz, D.S.1    Abelson, J.2
  • 49
    • 0031800746 scopus 로고    scopus 로고
    • Mutational analysis of the yeast DEAH-box splicing factor Prp16
    • Hotz H-R, 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
  • 50
    • 0027955630 scopus 로고
    • A dominant negative mutation in the conserved RNA helicase motif 'SAT' causes splicing factor PRP2 to stall in spliceosomes
    • Plumpton M, McGarvey M, Beggs JD. 1994. A dominant negative mutation in the conserved RNA helicase motif 'SAT' causes splicing factor PRP2 to stall in spliceosomes. EMBO J. 13:879-887.
    • (1994) EMBO J. , vol.13 , pp. 879-887
    • Plumpton, M.1    McGarvey, M.2    Beggs, J.D.3
  • 51
    • 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 RW, Beggs JD. 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
  • 52
    • 0032525135 scopus 로고    scopus 로고
    • Progression through the spliceosome cycle requires Prp38p function for U4/U6 snRNA dissociation
    • Xie J, Beickman K, Otte E, Rymond BC. 1998. Progression through the spliceosome cycle requires Prp38p function for U4/U6 snRNA dissociation. EMBO J. 17:2938-2946.
    • (1998) EMBO J. , vol.17 , pp. 2938-2946
    • Xie, J.1    Beickman, K.2    Otte, E.3    Rymond, B.C.4
  • 53
    • 33748766359 scopus 로고    scopus 로고
    • Inhibition of a spliceosome turnover pathway suppresses splicing defects
    • Pandit S, Lynn B, Rymond BC. 2006. Inhibition of a spliceosome turnover pathway suppresses splicing defects. Proc. Natl. Acad. Sci. U. S. A. 103:13700-13705.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 13700-13705
    • Pandit, S.1    Lynn, B.2    Rymond, B.C.3
  • 54
    • 0027287852 scopus 로고
    • A mechanism to enhance mRNA splicing fidelity: the RNA-dependent ATPase Prp16 governs usage of a discard pathway for aberrant lariat intermediates
    • Burgess SM, Guthrie C. 1993. A mechanism to enhance mRNA splicing fidelity: the RNA-dependent ATPase Prp16 governs usage of a discard pathway for aberrant lariat intermediates. Cell 73:1377-1392.
    • (1993) Cell , vol.73 , pp. 1377-1392
    • Burgess, S.M.1    Guthrie, C.2
  • 55
    • 33744937919 scopus 로고    scopus 로고
    • Exon ligation is proofread by the DExD/H-box ATPase Prp22p
    • Mayas RM, Maita H, Staley JP. 2006. Exon ligation is proofread by the DExD/H-box ATPase Prp22p. Nat. Struct. Mol. Biol. 13:482-490.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 482-490
    • Mayas, R.M.1    Maita, H.2    Staley, J.P.3
  • 56
    • 36749080450 scopus 로고    scopus 로고
    • Competition between the ATPase Prp5 and branch region-U2 snRNA pairing modulates the fidelity of spliceosome assembly
    • Xu Y-Z, Query CC. 2007. Competition between the ATPase Prp5 and branch region-U2 snRNA pairing modulates the fidelity of spliceosome assembly. Mol. Cell 28:838-849.
    • (2007) Mol. Cell , vol.28 , pp. 838-849
    • Xu, Y.-Z.1    Query, C.C.2
  • 57
    • 0027361712 scopus 로고
    • Beat the clock: paradigms for NTPases in the maintenance of biological fidelity
    • Burgess SM, Guthrie C. 1993. Beat the clock: paradigms for NTPases in the maintenance of biological fidelity. Trends Biochem. Sci. 18:381-384.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 381-384
    • Burgess, S.M.1    Guthrie, C.2
  • 58
    • 79953014376 scopus 로고    scopus 로고
    • The splice is right: guarantors of fidelity in premRNA splicing
    • Horowitz DS. 2011. The splice is right: guarantors of fidelity in premRNA splicing. RNA 17:551-554.
    • (2011) RNA , vol.17 , pp. 551-554
    • Horowitz, D.S.1
  • 59
    • 0034649666 scopus 로고    scopus 로고
    • Metalion coordination by U6 small nuclear RNA contributes to catalysis in the spliceosome
    • Yean S-L, Wuenschell G, Termini J, Lin R-J. 2000. Metal-ion coordination by U6 small nuclear RNA contributes to catalysis in the spliceosome. Nature 408:881-884.
    • (2000) Nature , vol.408 , pp. 881-884
    • Yean, S.-L.1    Wuenschell, G.2    Termini, J.3    Lin, R.-J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.