메뉴 건너뛰기




Volumn 19, Issue 8, 2000, Pages 1873-1886

A dual role for BBP/ScSF1 in nuclear pre-mRNA retention and splicing

Author keywords

KH domain; Nonsense mediated decay; Saccharomyces cerevisiae; snRNP; Spliceosome

Indexed keywords

MESSENGER RNA; SPLICING FACTOR; UNCLASSIFIED DRUG;

EID: 0343729923     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/19.8.1873     Document Type: Article
Times cited : (88)

References (69)
  • 1
    • 0030911051 scopus 로고    scopus 로고
    • Cross-intron bridging and interactions in the yeast commitment complex are conserved in mammals
    • Abovich, N. and Rosbash, M. (1997) Cross-intron bridging and interactions in the yeast commitment complex are conserved in mammals. Cell, 89, 403-412.
    • (1997) Cell , vol.89 , pp. 403-412
    • Abovich, N.1    Rosbash, M.2
  • 2
    • 0025224525 scopus 로고
    • The yeast PRP6 gene encodes a U4/U6 small nuclear ribonucleoprotein particle (snRNP) protein and the PRP9 gene encodes a protein required for U2 snRNP binding
    • Abovich, N., Legrain, P. and Rosbash, M. (1990) The yeast PRP6 gene encodes a U4/U6 small nuclear ribonucleoprotein particle (snRNP) protein and the PRP9 gene encodes a protein required for U2 snRNP binding. Mol. Cell. Biol., 10, 6417-6425.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 6417-6425
    • Abovich, N.1    Legrain, P.2    Rosbash, M.3
  • 3
    • 0028273768 scopus 로고
    • The yeast MUD2 protein: An interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition
    • Abovich, N., Liao, X.C. and Rosbash, M. (1994) The yeast MUD2 protein: an interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition. Genes Dev., 8, 843-854.
    • (1994) Genes Dev. , vol.8 , pp. 843-854
    • Abovich, N.1    Liao, X.C.2    Rosbash, M.3
  • 4
    • 0029949698 scopus 로고    scopus 로고
    • Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RNA
    • Arning, S., Grüter, P., Bilbe, G. and Krämer, A. (1996) Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RNA. RNA, 2, 794-810.
    • (1996) RNA , vol.2 , pp. 794-810
    • Arning, S.1    Grüter, P.2    Bilbe, G.3    Krämer, A.4
  • 5
    • 0030696675 scopus 로고    scopus 로고
    • The splicing factor BBP interacts specifically with the pre-mRNA branch point sequence UACUAAC
    • Berglund, J.A., Chua, K., Abovich, N., Reed, R. and Rosbash, M. (1997) The splicing factor BBP interacts specifically with the pre-mRNA branch point sequence UACUAAC. Cell, 89, 781-787.
    • (1997) Cell , vol.89 , pp. 781-787
    • Berglund, J.A.1    Chua, K.2    Abovich, N.3    Reed, R.4    Rosbash, M.5
  • 6
    • 0032521186 scopus 로고    scopus 로고
    • 65 and mBBP/SF1 facilitates branchpoint region recognition
    • 65 and mBBP/SF1 facilitates branchpoint region recognition. Genes Dev., 12, 858-867.
    • (1998) Genes Dev. , vol.12 , pp. 858-867
    • Berglund, J.A.1    Abovich, N.2    Rosbash, M.3
  • 7
    • 0031823231 scopus 로고    scopus 로고
    • The KH domain of the branchpoint sequence binding protein determines specificity for the pre-mRNA branchpoint sequence
    • Berglund, J.A., Fleming, M.L. and Rosbash, M. (1998b) The KH domain of the branchpoint sequence binding protein determines specificity for the pre-mRNA branchpoint sequence. RNA, 4, 998-1006.
    • (1998) RNA , vol.4 , pp. 998-1006
    • Berglund, J.A.1    Fleming, M.L.2    Rosbash, M.3
  • 8
    • 0029897488 scopus 로고    scopus 로고
    • PairWise and SearchWise: Finding the optimal alignment in a simultaneous comparison of a protein profile against all DNA translation frames
    • Birney, E., Thompson, J.D. and Gibson, T.J. (1996) PairWise and SearchWise: finding the optimal alignment in a simultaneous comparison of a protein profile against all DNA translation frames. Nucliec Acids Res., 24, 2730-2739.
    • (1996) Nucliec Acids Res. , vol.24 , pp. 2730-2739
    • Birney, E.1    Thompson, J.D.2    Gibson, T.J.3
  • 10
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell, R.C. and Joyce, G.F. (1992) Randomization of genes by PCR mutagenesis. PCR Methods Appl., 2. 28-33.
    • (1992) PCR Methods Appl. , vol.2 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 11
    • 0032476603 scopus 로고    scopus 로고
    • The yeast U2A′/U2B″ complex is required for pre-spliceosome formation
    • Caspary, F. and Séraphin, B. (1998) The yeast U2A′/U2B″ complex is required for pre-spliceosome formation. EMBO J., 17, 6348-6358.
    • (1998) EMBO J. , vol.17 , pp. 6348-6358
    • Caspary, F.1    Séraphin, B.2
  • 12
    • 0033564206 scopus 로고    scopus 로고
    • Partial purification of the yeast U2 snRNP reveals a novel yeast pre-mRNA splicing factor required for pre-spliceosome assembly
    • Caspary, F., Shevchenko, A., Wilm, M. and Séraphin, B. (1999) Partial purification of the yeast U2 snRNP reveals a novel yeast pre-mRNA splicing factor required for pre-spliceosome assembly. EMBO J., 18, 3463-3474.
    • (1999) EMBO J. , vol.18 , pp. 3463-3474
    • Caspary, F.1    Shevchenko, A.2    Wilm, M.3    Séraphin, B.4
  • 14
    • 0029894931 scopus 로고    scopus 로고
    • Identification of proteins that interact with exon sequences, splice sites and the branchpoint sequence during each stage of spliceosome assembly
    • Chiara, M.D., Gozani, O., Bennett, M., Champion, A.P., Palandjian, L. and Reed, R. (1996) Identification of proteins that interact with exon sequences, splice sites and the branchpoint sequence during each stage of spliceosome assembly. Mol. Cell. Biol., 16, 3317-3326.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3317-3326
    • Chiara, M.D.1    Gozani, O.2    Bennett, M.3    Champion, A.P.4    Palandjian, L.5    Reed, R.6
  • 15
    • 0029775561 scopus 로고    scopus 로고
    • The yeast splicing factor Mud13p is a commitment complex component and corresponds to CBP20, the small subunit of the nuclear cap-binding complex
    • Colot, H.V., Stutz, F. and Rosbash, M. (1996) The yeast splicing factor Mud13p is a commitment complex component and corresponds to CBP20, the small subunit of the nuclear cap-binding complex. Genes Dev., 10, 1699-1708.
    • (1996) Genes Dev. , vol.10 , pp. 1699-1708
    • Colot, H.V.1    Stutz, F.2    Rosbash, M.3
  • 16
    • 0033180278 scopus 로고    scopus 로고
    • Should we kill the messenger? The role of the surveillance complex in translation termination and mRNA turnover
    • Czaplinski, K., Ruiz-Echevarria, M.J., Gonzalez, C.I. and Peltz, S.W. (1999) Should we kill the messenger? The role of the surveillance complex in translation termination and mRNA turnover. BioEssays, 21, 685-696.
    • (1999) BioEssays , vol.21 , pp. 685-696
    • Czaplinski, K.1    Ruiz-Echevarria, M.J.2    Gonzalez, C.I.3    Peltz, S.W.4
  • 17
    • 0032880119 scopus 로고    scopus 로고
    • Characterization of a protein complex containing spliceosomal proteins SAPs 49, 130, 145, and 155
    • Das, B.K., Xia, L., Palandjian, L., Gozani, O., Chyung, Y. and Reed, R. (1999) Characterization of a protein complex containing spliceosomal proteins SAPs 49, 130, 145, and 155. Mol. Cell. Biol., 19, 6796-6802.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6796-6802
    • Das, B.K.1    Xia, L.2    Palandjian, L.3    Gozani, O.4    Chyung, Y.5    Reed, R.6
  • 18
    • 0032708815 scopus 로고    scopus 로고
    • Resolution of the mammalian E complex and the ATP-dependent spliceosomal complexes on native agarose minigels
    • Das, R. and Reed, R. (1999) Resolution of the mammalian E complex and the ATP-dependent spliceosomal complexes on native agarose minigels. RNA, 5, 1504-1508.
    • (1999) RNA , vol.5 , pp. 1504-1508
    • Das, R.1    Reed, R.2
  • 19
    • 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. Nature Genet., 16, 277-282.
    • (1997) Nature Genet. , vol.16 , pp. 277-282
    • Fromont-Racine, M.1    Rain, J.-C.2    Legrain, P.3
  • 20
    • 0031878108 scopus 로고    scopus 로고
    • A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site
    • Gozani, O., Potashkin, J. and Reed, R. (1998) A potential role for U2AF-SAP 155 interactions in recruiting U2 snRNP to the branch site. Mol. Cell. Biol., 18, 4752-4760.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4752-4760
    • Gozani, O.1    Potashkin, J.2    Reed, R.3
  • 21
    • 0027242173 scopus 로고
    • Stabilization and ribosome association of unspliced pre-mRNAs in a yeast upf1-mutant
    • He, F., Peltz, S.W., Donahue, J.L., Rosbash, M. and Jacobson, A. (1993) Stabilization and ribosome association of unspliced pre-mRNAs in a yeast upf1-mutant. Proc. Natl Acad. Sci. USA, 90, 7034-7038.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 7034-7038
    • He, F.1    Peltz, S.W.2    Donahue, J.L.3    Rosbash, M.4    Jacobson, A.5
  • 22
    • 0033016753 scopus 로고    scopus 로고
    • mRNA surveillance in eukaryotes: Kinetic proofreading of proper translation termination as assessed by mRNP domain organization?
    • Hilleren, P. and Parker, R. (1999) mRNA surveillance in eukaryotes: kinetic proofreading of proper translation termination as assessed by mRNP domain organization? RNA, 5, 711-719.
    • (1999) RNA , vol.5 , pp. 711-719
    • Hilleren, P.1    Parker, R.2
  • 23
    • 0014565169 scopus 로고
    • Temperature-sensitive yeast mutant defective in rihonucleic acid production
    • Hutchison, H.T., Hartwell, L.H. and McLaughlin, C.S. (1969) Temperature-sensitive yeast mutant defective in rihonucleic acid production. J. Bacteriol., 99, 807-814.
    • (1969) J. Bacteriol. , vol.99 , pp. 807-814
    • Hutchison, H.T.1    Hartwell, L.H.2    McLaughlin, C.S.3
  • 24
    • 0020529962 scopus 로고
    • Transformation of intact yeast cells treated with alkali cations
    • Ito, H., Fukada, Y., Murata, K. and Kimura, A. (1983) Transformation of intact yeast cells treated with alkali cations. J. Bacteriol., 153, 163-168.
    • (1983) J. Bacteriol. , vol.153 , pp. 163-168
    • Ito, H.1    Fukada, Y.2    Murata, K.3    Kimura, A.4
  • 25
    • 0022348855 scopus 로고
    • A quantitative analysis of the effects of 5′ junction and TACTAAC box mutants and mutant combinations on yeast mRNA splicing
    • Jacquier, A., Rodriguez, J.R. and Rosbash, M. (1985) A quantitative analysis of the effects of 5′ junction and TACTAAC box mutants and mutant combinations on yeast mRNA splicing. Cell, 43, 423-430.
    • (1985) Cell , vol.43 , pp. 423-430
    • Jacquier, A.1    Rodriguez, J.R.2    Rosbash, M.3
  • 26
    • 0026668641 scopus 로고
    • Purification of splicing factor SF1, a heat stable protein that functions in the assembly of a presplicing complex
    • Krämer, A. (1992) Purification of splicing factor SF1, a heat stable protein that functions in the assembly of a presplicing complex. Mol. Cell. Biol. 12, 4545-4552.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4545-4552
    • Krämer, A.1
  • 27
    • 0029891101 scopus 로고    scopus 로고
    • The structure and function of proteins involved in mammalian pre-mRNA splicing
    • Krämer, A. (1996) The structure and function of proteins involved in mammalian pre-mRNA splicing. Annu. Rev. Biochem., 65, 367-409.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 367-409
    • Krämer, A.1
  • 28
    • 0025897155 scopus 로고
    • Three protein factors (SF1, SF3 and U2AF) function in pre-splicing complex formation in addition to snRNPs
    • Krämer, A. and Utans, U. (1991) Three protein factors (SF1, SF3 and U2AF) function in pre-splicing complex formation in addition to snRNPs. EMBO J., 10, 1503-1509.
    • (1991) EMBO J. , vol.10 , pp. 1503-1509
    • Krämer, A.1    Utans, U.2
  • 29
    • 0033612569 scopus 로고    scopus 로고
    • Combined biochemical and electron microscopic analyses reveal the architecture of the mammalian U2 snRNP
    • Krämer, A., Grüter, P., Groning, K. and Kastner, B. (1999) Combined biochemical and electron microscopic analyses reveal the architecture of the mammalian U2 snRNP. J. Cell Biol., 145, 1355-1368.
    • (1999) J. Cell Biol. , vol.145 , pp. 1355-1368
    • Krämer, A.1    Grüter, P.2    Groning, K.3    Kastner, B.4
  • 30
    • 0025786141 scopus 로고
    • The product of the yeast UPF1 gene is required for rapid turnover of mRNAs containing a premature translational termination codon
    • Leeds, P., Peltz, S.W., Jacobson, A. and Culbertson, M.R. (1991) The product of the yeast UPF1 gene is required for rapid turnover of mRNAs containing a premature translational termination codon. Genes Dev., 5, 2303-2314.
    • (1991) Genes Dev. , vol.5 , pp. 2303-2314
    • Leeds, P.1    Peltz, S.W.2    Jacobson, A.3    Culbertson, M.R.4
  • 31
    • 0024973850 scopus 로고
    • Some cis-and trans-acting mutants for splicing target pre-mRNA to the cytoplasm
    • Legrain, P. and Rosbash, M. (1989) Some cis-and trans-acting mutants for splicing target pre-mRNA to the cytoplasm. Cell, 57, 573-583.
    • (1989) Cell , vol.57 , pp. 573-583
    • Legrain, P.1    Rosbash, M.2
  • 33
    • 0034603208 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by a Nova KH domain: Implications for paraneoplastic disease and the fragile X syndrome
    • Lewis, H.A., Musunuru, K., Jensen, K.B., Edo, C., Chen, H., Darnell, R.B. and Burley, S.K. (2000) Sequence-specific RNA binding by a Nova KH domain: implications for paraneoplastic disease and the fragile X syndrome. Cell, 100, 323-332.
    • (2000) Cell , vol.100 , pp. 323-332
    • Lewis, H.A.1    Musunuru, K.2    Jensen, K.B.3    Edo, C.4    Chen, H.5    Darnell, R.B.6    Burley, S.K.7
  • 34
    • 0029790606 scopus 로고    scopus 로고
    • A yeast cap binding protein complex (yCBC) acts at an early step in prE-mRNA splicing
    • Lewis, J.D., Görlich, D. and Mattaj, I.W. (1996) A yeast cap binding protein complex (yCBC) acts at an early step in prE-mRNA splicing. Nucleic Acids Res., 24, 3332-3336.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3332-3336
    • Lewis, J.D.1    Görlich, D.2    Mattaj, I.W.3
  • 35
    • 0026657735 scopus 로고
    • Requirements for U2 snRNP addition to yeast pre-mRNA
    • Liao, X.C., Colot, H.V., Wang, Y. and Rosbash, M. (1992) Requirements for U2 snRNP addition to yeast pre-mRNA. Nucleic Acids Res., 20, 4237-4245.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4237-4245
    • Liao, X.C.1    Colot, H.V.2    Wang, Y.3    Rosbash, M.4
  • 36
    • 0029448034 scopus 로고
    • Spatial consequences of defective processing of specific yeast mRNAs revealed by fluorescent in situ hybridization
    • Long, R.M., Elliott, D.J., Stutz, F., Rosbash, M. and Singer, R.H. (1995) Spatial consequences of defective processing of specific yeast mRNAs revealed by fluorescent in situ hybridization. RNA, 1, 1071-1078.
    • (1995) RNA , vol.1 , pp. 1071-1078
    • Long, R.M.1    Elliott, D.J.2    Stutz, F.3    Rosbash, M.4    Singer, R.H.5
  • 37
    • 0032865541 scopus 로고    scopus 로고
    • Genomic-scale quantitative analysis of yeast pre-mRNA splicing: Implications for splice-site recognition
    • Lopez, P.J. and Séraphin, B. (1999) Genomic-scale quantitative analysis of yeast pre-mRNA splicing: implications for splice-site recognition. RNA, 5, 1135-1137.
    • (1999) RNA , vol.5 , pp. 1135-1137
    • Lopez, P.J.1    Séraphin, B.2
  • 38
    • 1842330298 scopus 로고    scopus 로고
    • The role of branchpoint-3′ splice site spacing and interaction between intron terminal nucleotides in 3′ splice site selection in Saccharomyces cerevisiae
    • Luukkonen, B. and Séraphin, B. (1997) The role of branchpoint-3′ splice site spacing and interaction between intron terminal nucleotides in 3′ splice site selection in Saccharomyces cerevisiae. EMBO J., 16, 779-792.
    • (1997) EMBO J. , vol.16 , pp. 779-792
    • Luukkonen, B.1    Séraphin, B.2
  • 40
    • 0028556367 scopus 로고
    • Dynamic RNA-RNA interactions in the spliceosome
    • Madhani, H. and Guthrie, C. (1994) Dynamic RNA-RNA interactions in the spliceosome. Annu. Rev. Genet., 28, 1-26.
    • (1994) Annu. Rev. Genet. , vol.28 , pp. 1-26
    • Madhani, H.1    Guthrie, C.2
  • 41
    • 0032796427 scopus 로고    scopus 로고
    • Splicing factor SF1 from Drosophila and Caenorhabditis: Presence of an N-terminal RS domain and requirement for viability
    • Mazroui, R., Puoti, A. and Kramer, A. (1999) Splicing factor SF1 from Drosophila and Caenorhabditis: presence of an N-terminal RS domain and requirement for viability. RNA, 5, 1615-1631.
    • (1999) RNA , vol.5 , pp. 1615-1631
    • Mazroui, R.1    Puoti, A.2    Kramer, A.3
  • 42
    • 0027215924 scopus 로고
    • A functional association between the 5′ and 3′ splice site is established in the earliest prespliceosome complex (E) in mammals
    • Michaud, S. and Reed, R. (1993) A functional association between the 5′ and 3′ splice site is established in the earliest prespliceosome complex (E) in mammals. Genes Dev., 7, 1008-1020.
    • (1993) Genes Dev. , vol.7 , pp. 1008-1020
    • Michaud, S.1    Reed, R.2
  • 43
    • 0001877802 scopus 로고
    • Splicing of precursors to mRNA by the spliceosome
    • Gesteland, R. and Atkins, J. (eds), Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY
    • Moore, M., Query, C. and Sharp, P. (1993) Splicing of precursors to mRNA by the spliceosome. In Gesteland, R. and Atkins, J. (eds), The RNA World. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, NY, pp. 303-357.
    • (1993) The RNA World , pp. 303-357
    • Moore, M.1    Query, C.2    Sharp, P.3
  • 44
    • 0029988528 scopus 로고    scopus 로고
    • Three-dimensional structure and stability of the KH domain: Molecular insights into the fragile X syndrome
    • Musco, G., Stier, G., Joseph, C., Castiglione Morelli, M.A., Nilges, M., Gibson, T.J. and Pastore, A. (1996) Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome. Cell, 85, 237-245.
    • (1996) Cell , vol.85 , pp. 237-245
    • Musco, G.1    Stier, G.2    Joseph, C.3    Castiglione Morelli, M.A.4    Nilges, M.5    Gibson, T.J.6    Pastore, A.7
  • 45
    • 0031230806 scopus 로고    scopus 로고
    • The solution structure of the first KH domain of FMRI, the protein responsible for the fragile X syndrome
    • published erratum appears in Nature Struct. Biol., 1997, 4, 840
    • Musco, G., Kharrat, A., Stier, G., Fraternali, F., Gibson, T.J., Nilges, M. and Pastore, A. (1997) The solution structure of the first KH domain of FMRI, the protein responsible for the fragile X syndrome [published erratum appears in Nature Struct. Biol., 1997, 4, 840]. Nature Struct. Biol., 4, 712-716.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 712-716
    • Musco, G.1    Kharrat, A.2    Stier, G.3    Fraternali, F.4    Gibson, T.J.5    Nilges, M.6    Pastore, A.7
  • 46
    • 0033598989 scopus 로고    scopus 로고
    • Transport of proteins and RNAs in and out of the nucleus
    • Nakielny, S. and Dreyfuss, G. (1999) Transport of proteins and RNAs in and out of the nucleus. Cell, 99, 677-690.
    • (1999) Cell , vol.99 , pp. 677-690
    • Nakielny, S.1    Dreyfuss, G.2
  • 47
    • 0006479273 scopus 로고
    • Analysis of pre-mRNA splicing in yeast
    • Higgins, S. and Hames, B. (eds), Oxford University Press, Oxford. UK
    • Newman, A. (1994) Analysis of pre-mRNA splicing in yeast. In Higgins, S. and Hames, B. (eds), RNA Processing: A Practical Approach. Oxford University Press, Oxford. UK. pp. 179-195.
    • (1994) RNA Processing: A Practical Approach , pp. 179-195
    • Newman, A.1
  • 48
    • 0029871680 scopus 로고    scopus 로고
    • Identification of novel genes required for yeast pre-mRNA splicing by means of cold-sensitive mutations
    • Noble, S.M. and Guthrie, C. (1996) Identification of novel genes required for yeast pre-mRNA splicing by means of cold-sensitive mutations. Genetics, 143, 67-80.
    • (1996) Genetics , vol.143 , pp. 67-80
    • Noble, S.M.1    Guthrie, C.2
  • 49
    • 0021832962 scopus 로고
    • mRNA splicing efficiency in yeast and the contribution of nonconserved sequences
    • Pikielny, C.W. and Rosbash, M. (1985) mRNA splicing efficiency in yeast and the contribution of nonconserved sequences. Cell, 41, 119-126.
    • (1985) Cell , vol.41 , pp. 119-126
    • Pikielny, C.W.1    Rosbash, M.2
  • 51
    • 0033105003 scopus 로고    scopus 로고
    • Interaction of the U1 snRNP with nonconserved intronic sequences affects 5′ splice site selection
    • Puig, O., Gottschalk, A., Fabrizio, P. and Séraphin, B. (1999) Interaction of the U1 snRNP with nonconserved intronic sequences affects 5′ splice site selection. Genes Dev., 13, 569-580.
    • (1999) Genes Dev. , vol.13 , pp. 569-580
    • Puig, O.1    Gottschalk, A.2    Fabrizio, P.3    Séraphin, B.4
  • 52
    • 0030934772 scopus 로고    scopus 로고
    • In vivo commitment to splicing in yeast involves the nucleotide upstream from the branch site conserved sequence and the Mud2 protein
    • Rain, J.C. and Legrain, P. (1997) In vivo commitment to splicing in yeast involves the nucleotide upstream from the branch site conserved sequence and the Mud2 protein. EMBO J., 16, 1759-1771.
    • (1997) EMBO J. , vol.16 , pp. 1759-1771
    • Rain, J.C.1    Legrain, P.2
  • 53
    • 0031958545 scopus 로고    scopus 로고
    • Conservation of functional domains involved in RNA binding and protein-protein interactions in human and Saccharomycess cerevisiae pre-mRNA splicing factor SF1
    • Rain, J.C., Rafi, Z., Rhani, Z., Legrain, P. and Krämer, A. (1998) Conservation of functional domains involved in RNA binding and protein-protein interactions in human and Saccharomycess cerevisiae pre-mRNA splicing factor SF1. RNA, 4, 551-565.
    • (1998) RNA , vol.4 , pp. 551-565
    • Rain, J.C.1    Rafi, Z.2    Rhani, Z.3    Legrain, P.4    Krämer, A.5
  • 54
    • 0025876808 scopus 로고
    • Who's on first? The U1 snRNP-5′ splice site interaction and splicing
    • Rosbash, M. and Séraphin, B. (1991) Who's on first? The U1 snRNP-5′ splice site interaction and splicing. Trends Biochem. Sci., 16, 187-190.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 187-190
    • Rosbash, M.1    Séraphin, B.2
  • 55
    • 0345593813 scopus 로고    scopus 로고
    • Transient interaction of BBP/ScSF1 and Mud2 with the splicing machinery affects the kinetics of spliceosome assembly
    • Rutz, B. and Séraphin, B. (1999) Transient interaction of BBP/ScSF1 and Mud2 with the splicing machinery affects the kinetics of spliceosome assembly. RNA, 5, 819-831.
    • (1999) RNA , vol.5 , pp. 819-831
    • Rutz, B.1    Séraphin, B.2
  • 56
    • 0027231486 scopus 로고
    • 3′ splice site recognition in S.cerevisiae does not require base pairing with U1 snRNA
    • Séraphin, B. and Kandels-Lewis, S. (1993) 3′ splice site recognition in S.cerevisiae does not require base pairing with U1 snRNA. Cell, 73, 803-812.
    • (1993) Cell , vol.73 , pp. 803-812
    • Séraphin, B.1    Kandels-Lewis, S.2
  • 57
    • 0024325159 scopus 로고
    • Identification of functional U1 snRNA - Pre-mRNA complexes committed to spliceosome assembly and splicing
    • Séraphin, B. and Rosbash, M. (1989a) Identification of functional U1 snRNA - pre-mRNA complexes committed to spliceosome assembly and splicing. Cell, 59, 349-358.
    • (1989) Cell , vol.59 , pp. 349-358
    • Séraphin, B.1    Rosbash, M.2
  • 58
    • 0024434426 scopus 로고
    • Mutational analysis of the interactions between U1 small nuclear RNA and pre-mRNA of yeast
    • Séraphin, B. and Rosbash, M. (1989b) Mutational analysis of the interactions between U1 small nuclear RNA and pre-mRNA of yeast. Gene, 82, 145-151.
    • (1989) Gene , vol.82 , pp. 145-151
    • Séraphin, B.1    Rosbash, M.2
  • 59
    • 0025733098 scopus 로고
    • The yeast branchpoint sequence is not required for the formation of a stable U1 snRNA-pre-mRNA complex and is recognized in the absence of U2 snRNA
    • Séraphin, B. and Rosbash, M. (1991) The yeast branchpoint sequence is not required for the formation of a stable U1 snRNA-pre-mRNA complex and is recognized in the absence of U2 snRNA, EMBO J., 10, 1209-1216.
    • (1991) EMBO J. , vol.10 , pp. 1209-1216
    • Séraphin, B.1    Rosbash, M.2
  • 60
    • 0024062611 scopus 로고
    • A U1 snRNA:Pre-mRNA base pairing interaction is required early in yeast spliceosome assembly but does not uniquely define the 5′ cleavage site
    • Séraphin, B., Kretzner, L. and Rosbash, M. (1988) A U1 snRNA:pre-mRNA base pairing interaction is required early in yeast spliceosome assembly but does not uniquely define the 5′ cleavage site. EMBO J., 7, 2533-2538.
    • (1988) EMBO J. , vol.7 , pp. 2533-2538
    • Séraphin, B.1    Kretzner, L.2    Rosbash, M.3
  • 61
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.1    Hieter, P.2
  • 62
    • 0009359622 scopus 로고
    • Expression of a β-galactosidase gene containing the ribosomal protein 51 intron is sensitive to the rna2 mutation of yeast
    • Teem, J.L. and Rosbash, M. (1983) Expression of a β-galactosidase gene containing the ribosomal protein 51 intron is sensitive to the rna2 mutation of yeast. Proc. Natl Acad. Sci. USA, 80, 4403-4407.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 4403-4407
    • Teem, J.L.1    Rosbash, M.2
  • 63
    • 0028013177 scopus 로고
    • Improved sensitivity of profile searches through the use of sequence weights and gap excision
    • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) Improved sensitivity of profile searches through the use of sequence weights and gap excision. Comput. Appl. Biosci., 10, 19-29.
    • (1994) Comput. Appl. Biosci. , vol.10 , pp. 19-29
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 64
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTALX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F. and Higgins, D.G. (1997) The CLUSTALX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res., 25, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 65
    • 0030595187 scopus 로고    scopus 로고
    • 65 RS region with pre-mRNA of branch point and promotion of base pairing with U2 snRNA
    • 65 RS region with pre-mRNA of branch point and promotion of base pairing with U2 snRNA. Science, 273, 1706-1709.
    • (1996) Science , vol.273 , pp. 1706-1709
    • Valcárcel, J.1    Gaur, R.2    Singh, R.3    Green, M.4
  • 66
    • 0031451912 scopus 로고    scopus 로고
    • STAR, a gene family involved in signal transduction and activation of RNA
    • Vernet, C. and Artzt, K. (1997) STAR, a gene family involved in signal transduction and activation of RNA. Trends Genet., 13, 479-484.
    • (1997) Trends Genet. , vol.13 , pp. 479-484
    • Vernet, C.1    Artzt, K.2
  • 67
    • 0024710729 scopus 로고
    • Isolation and characterization of pre-mRNA splicing mutants of Saccharomyces cerevisiae
    • Vijayraghavan, U., Company, M. and Abelson, J. (1989) Isolation and characterization of pre-mRNA splicing mutants of Saccharomyces cerevisiae. Genes Dev., 3, 1206-1216.
    • (1989) Genes Dev. , vol.3 , pp. 1206-1216
    • Vijayraghavan, U.1    Company, M.2    Abelson, J.3
  • 68
    • 0024408832 scopus 로고
    • Identification, purification and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor
    • Zamore, P.D. and Green, M.R. (1989) Identification, purification and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor. Proc. Natl Acad. Sci. USA, 86, 9243-9247.
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 9243-9247
    • Zamore, P.D.1    Green, M.R.2
  • 69
    • 0033106323 scopus 로고    scopus 로고
    • Identification of eight proteins that cross-link to pre-mRNA in the yeast commitment complex
    • Zhang, D. and Rosbash, M. (1999) Identification of eight proteins that cross-link to pre-mRNA in the yeast commitment complex. Genes Dev., 13, 581-592.
    • (1999) Genes Dev. , vol.13 , pp. 581-592
    • Zhang, D.1    Rosbash, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.