Interaction between the Human Nuclear Cap-Binding Protein Complex and hnRNP F

REFERENCES

• Abovich, N., X. C. Liao, and M. Rosbash. 1994. The yeast MUD2 protein: an interaction with PRP11 defines a bridge between commitment complexes and U2 snRNP addition. Genes Dev. 8:843–854.
   PubMed Web of Science ®Google Scholar
• Bennett, M., R. S. Pinol, D. Staknis, G. Dreyfuss, and R. Reed. 1992. Differential binding of heterogeneous nuclear ribonucleoproteins to mRNA precursors prior to spliceosome assembly in vitro. Mol. Cell. Biol. 12:3165–3175.
   PubMedGoogle Scholar
• Black, D. L. 1991. Does steric interference between splice sites block the splicing of a short c-src neuron-specific exon in non-neuronal cells? Genes Dev. 5:389–402.
   PubMedGoogle Scholar
• Black, D. L. 1992. Activation of c-src neuron-specific splicing by an unusual RNA element in vivo and in vitro. Cell 69:795–807.
   PubMedGoogle Scholar
• Caceres, J. F., S. Stamm, D. M. Helfman, and A. R. Krainer. 1994. Regulation of alternative splicing in vivo by overexpression of antagonistic splicing factors. Science 265:1706–1709.
   PubMed Web of Science ®Google Scholar
• Choi, Y. D., and G. Dreyfuss. 1984. Monoclonal antibody characterization of the C proteins of heterogeneous nuclear ribonucleoprotein complexes in vertebrate cells. J. Cell Biol. 99:1997–2004.
   PubMedGoogle Scholar
• Choi, Y. D., P. J. Grabowski, P. A. Sharp, and G. Dreyfuss. 1986. Heterogeneous nuclear ribonucleoproteins: role in RNA splicing. Science 231:1534–1539.
   PubMed Web of Science ®Google Scholar
• Colot, H., F. Stutz, and M. Rosbash. 1996. The yeast splicing factor Mudl3p is a commitment complex component and corresponds to CBP20, the small subunit of the nuclear cap-binding complex. Genes Dev. 10:1699–1708.
   PubMedGoogle Scholar
• Darzynkiewicz, E., I. Ekiel, S. M. Tahara, L. S. Seliger, and A. J. Shatkin. 1985. Chemical synthesis and characterization of 7-methylguanosine analogues. Biochemistry 24:1701–1707.
   Web of Science ®Google Scholar
• Dignam, J. D., R. M. Lebovitz, and R. G. Roeder. 1983. Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1475–1489.
   PubMed Web of Science ®Google Scholar
• Dreyfuss, G., M. J. Matunis, S. Pinol-Roma, and C. G. Burd. 1993. hnRNP proteins and the biogenesis of mRNA. Annu. Rev. Biochem. 62:289–321.
   PubMed Web of Science ®Google Scholar
• Dreyfuss, G., M. S. Swanson, and S. Pinol-Roma. 1988. Heterogeneous nuclear ribonucleoprotein particles and the pathway of mRNA formation. Trends Biochem. Sci. 13:86–91.
   PubMedGoogle Scholar
• Durfee, T., K. Becherer, P. L. Chen, S. H. Yeh, Y. Yang, A. E. Kilburn, W. H. Lee, and S. J. Elledge. 1993. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. 7:555–569.
   PubMed Web of Science ®Google Scholar
• Fields, S., and O. Song. 1989. A novel genetic system to detect protein-protein interactions. Nature 340:245–246.
   PubMed Web of Science ®Google Scholar
• Fu, X. D. 1995. The superfamily of arginine/serine-rich splicing factors. RNA 1:663–680.
   PubMed Web of Science ®Google Scholar
• Gamberi, C. Unpublished data.
   Google Scholar
• Gattoni, R., D. Mahe, P. Mahl, N. Fischer, M.-G. Mattei, J. Stevenin, and J.-P. Fuchs. 1996. The human hnRNP-M proteins: structure and relation with early heat shock-induced splicing arrest and chromosome mapping. Nucleic Acids Res. 24:2535–2542.
   PubMedGoogle Scholar
• Gorlich, D., R. Kraft, S. Kostka, F. Vogel, E. Hartmann, R. A. Laskey, I. W. Mattaj, and E. Izaurralde. 1996. Importin provides a link between nuclear protein import and U snRNA export. Cell, 87:21–32.
   PubMed Web of Science ®Google Scholar
• Gorlich, D., and I. W. Mattaj. 1996. Nucleocytoplasmic transport. Science 271:1513–1518.
   PubMed Web of Science ®Google Scholar
• Harlow, E., and D. Lane. 1988. Antibodies: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Honore, B., H. H. Rasmussen, H. Vorum, K. Dejgaard, X. Liu, P. Gromov, P. Madsen, B. Gesser, N. Tommerup, and J. E. Celis. 1995. Heterogeneous nuclear ribonucleoproteins H, H′, and F are members of a ubiquitously expressed subfamily of related but distinct proteins encoded by genes mapping to different chromosomes. J. Biol. Chem. 270:28780–28789.
   PubMedGoogle Scholar
• Ito, H., Y. Fukuda, K. Murata, and A. Kimura. 1983. Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153:163–168.
   PubMed Web of Science ®Google Scholar
• Izaurralde, E., A. Jarmolowski, C. Beisel, I. W. Mattaj, G. Dreyfuss, and U. Fischer. A role for the hnRNP A1 M9-transport signal in mRNA nuclear export. J. Cell Biol., in press.
   Google Scholar
• Izaurralde, E., J. Lewis, C. Gamberi, A. Jarmolowski, C. McGuigan, and I. W. Mattaj. 1995. A cap-binding protein complex mediating U snRNA export. Nature 376:709–712.
   PubMed Web of Science ®Google Scholar
• Izaurralde, E., J. Lewis, C. McGuigan, M. Jankowska, E. Darzynkiewicz, and I. W. Mattaj. 1994. A nuclear cap binding protein complex involved in pre-mRNA splicing. Cell 78:657–668.
   PubMed Web of Science ®Google Scholar
• Izaurralde, E., and I. W. Mattaj. 1995. RNA export. Cell 81:153–159.
   PubMedGoogle Scholar
• Izaurralde, E., J. Stepinski, E. Darzynkiewicz, and I. W. Mattaj. 1992. A cap binding protein that may mediate nuclear export of RNA polymerase II-transcribed RNAs. J. Cell Biol. 118:1287–1295.
   PubMed Web of Science ®Google Scholar
• Karsch, M. I., and S. R. Haynes. 1993. The Rb97D gene encodes a potential RNA-binding protein required for spermatogenesis in Drosophila. Nucleic Acids Res. 21:2229–2235.
   PubMedGoogle Scholar
• Kataoka, N., M. Ohno, K. Kangawa, Y. Tokoro, and Y. Shimura. 1994. Cloning of a complementary DNA encoding an 80 kilodalton nuclear cap binding protein. Nucleic Acids Res. 22:3861–3865.
   PubMedGoogle Scholar
• Kataoka, N., M. Ohno, I. Moda, and Y. Shimura. 1995. Identification of the factors that interact with NCBP, an 80 kDa nuclear cap binding protein. Nucleic Acids Res. 23:3638–3641.
   PubMedGoogle Scholar
• Kelley, R. L. 1993. Initial organization of the Drosophila dorsoventral axis depends on an RNA-binding protein encoded by the squid gene. Genes Dev. 7:948–960.
   PubMed Web of Science ®Google Scholar
• Konarska, M. M., and P. A. Sharp. 1987. Interactions between small nuclear ribonucleoprotein particles in formation of spliceosomes. Cell 49:763–774.
   PubMed Web of Science ®Google Scholar
• Lamm, G. M., and A. I. Lamond. 1993. Non-snRNP protein splicing factors. Biochim. Biophys. Acta 1173:247–265.
   PubMedGoogle Scholar
• Lee, M. S., M. Henry, and P. A. Silver. 1996. A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export. Genes Dev. 10:1233–1246.
   PubMed Web of Science ®Google Scholar
• Legrain, P., B. Séraphin, and M. Rosbash. 1988. Early commitment of yeast pre-mRNA to the spliceosome pathway. Mol. Cell. Biol. 8:3755–3760.
   PubMedGoogle Scholar
• Lewis, J. D., D. Gorlich, and I. W. Mattaj. 1996. A yeast cap-binding protein complex (yCBC) acts at an early step in pre-mRNA splicing. Nucleic Acids Res. 24:3332–3336.
   PubMed Web of Science ®Google Scholar
• Lewis, J. D., E. Izaurralde, A. Jarmolowski, C. McGuigan, and I. W. Mattaj. 1996. A nuclear cap-binding complex facilitates association of U1 snRNP with the cap-proximal 5′ splice site. Genes Dev. 10:1683–1698.
   PubMed Web of Science ®Google Scholar
• Liu, X., and J. E. Mertz. 1995. hnRNP L binds a cis-acting RNA sequence element that enables intron-dependent gene expression. Genes Dev. 9:1766–1780.
   PubMed Web of Science ®Google Scholar
• Manley, J. L., and R. Tacke. 1996. SR proteins and splicing control. Genes Dev. 10:1569–1579.
   PubMed Web of Science ®Google Scholar
• Matunis, E. L., R. Kelley, and G. Dreyfuss. 1994. Essential role for a heterogeneous nuclear ribonucleoprotein (hnRNP) in oogenesis: hrp40 is absent from the germ line in the dorsoventral mutant squid. Proc. Natl. Acad. Sci. USA 91:2781–2784.
   PubMedGoogle Scholar
• Matunis, E. L., M. J. Matunis, and G. Dreyfuss. 1992. Characterization of the major hnRNP proteins from Drosophila melanogaster. J. Cell Biol. 116:257–269.
   PubMedGoogle Scholar
• Matunis, E. L., M. J. Matunis, and G. Dreyfuss. 1993. Association of individual hnRNP proteins and snRNPs with nascent transcripts. J. Cell Biol. 121:219–228.
   PubMed Web of Science ®Google Scholar
• Matunis, M. J., E. L. Matunis, and G. Dreyfuss. 1992. Isolation of hnRNP complexes from Drosophila melanogaster. J. Cell Biol. 116:245–255.
   PubMedGoogle Scholar
• Matunis, M. J., J. Xing, and G. Dreyfuss. 1994. The hnRNP F protein: unique primary structure, nucleic acid-binding properties, and subcellular localization. Nucleic Acids Res. 22:1059–1067.
   PubMedGoogle Scholar
• Mayeda, A., and A. R. Krainer. 1992. Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2. Cell 68:365–375.
   PubMed Web of Science ®Google Scholar
• Michael, W. M., M. Choi, and G. Dreyfuss. 1995. A nuclear export signal in hnRNP Al: a signal-mediated, temperature-dependent nuclear protein export pathway. Cell 83:415–422.
   PubMed Web of Science ®Google Scholar
• Michael, W. M., H. Siomi, M. Choi, S. Piñol-Roma, S. Nakielny, Q. Liu, and G. Dreyfuss. 1995. Signal sequences that target nuclear import and nuclear export of pre-mRNA binding proteins. Cold Spring Harbor Symp. Quant. Biol. 60:663–668.
   PubMedGoogle Scholar
• Michaud, S., and R. Reed. 1991. An ATP-independent complex commits pre-mRNA to the mammalian spliceosome assembly pathway. Genes Dev. 5:2534–2546.
   PubMedGoogle Scholar
• Min, H., R. C. Chan, and D. L. Black. 1995. The generally expressed hnRNP F is involved in a neural-specific pre-mRNA splicing event. Genes Dev. 9:2659–2671.
   PubMedGoogle Scholar
• Moore, M., C. Query, and P. Sharp. 1993. Splicing of precursors to messenger RNAs by the spliceosome, p. 303–357. In R. Gesteland and J. Atkins (ed.), The RNA world. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Ohno, M., N. Kataoka, and Y. Shimura. 1990. A nuclear cap binding protein from HeLa cells. Nucleic Acids Res. 18:6989–6995.
   PubMedGoogle Scholar
• Ohno, M., H. Sakamoto, K. Yasuda, T. S. Okada, and Y. Shimura. 1985. Nucleotide sequence of a chicken delta-crystallin gene. Nucleic Acids Res. 13:1593–1606.
   PubMed Web of Science ®Google Scholar
• Piñol-Roma, S., and G. Dreyfuss. 1991. Transcription-dependent and transcription-independent nuclear transport of hnRNP proteins. Science 253:312–314.
   PubMed Web of Science ®Google Scholar
• Piñol-Roma, S., and G. Dreyfuss. 1992. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature 355:730–732.
   PubMed Web of Science ®Google Scholar
• Robzyk, K., and Y. Kassir. 1992. A simple and highly efficient procedure for rescuing autonomous plasmids from yeast. Nucleic Acids Res. 20:3790.
   PubMed Web of Science ®Google Scholar
• Rymond, B. C., and M. Rosbash. 1992. Yeast pre-mRNA splicing, p. 143–192. In J. R. Pringle and J. R. Broach (ed.), The molecular and cellular biology of the yeast Saccharomyces. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Sakamoto, H., M. Ohno, K. Yasuda, K. Mizumoto, and Y. Shimura. 1987. In vitro splicing of a chicken delta-crystallin pre-mRNA in a mammalian nuclear extract. J. Biochem. (Tokyo) 102:1289–1301.
   PubMedGoogle Scholar
• Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular cloning: a laboratory manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
   Google Scholar
• Sanger, F., S. Nicklen, and A. R. Coulson. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   PubMed Web of Science ®Google Scholar
• Scherly, D., W. Boelens, W. van Venrooij, N. A. Dathan, J. Hamm, and I. W. Mattaj. 1989. Identification of the RNA binding segment of human U1 A protein and definition of its binding site on U1 snRNA. EMBO J. 8:4163–4170.
   PubMedGoogle Scholar
• Séraphin, B., L. Kretzner, and M. Rosbash. 1988. A U1 snRNApre-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.
   PubMed Web of Science ®Google Scholar
• Séraphin, B., and M. Rosbash. 1989. Identification of functional U1 snRNA-pre-mRNA complexes committed to spliceosome assembly and splicing. Cell 59:349–358.
   PubMed Web of Science ®Google Scholar
• Siebel, C. W., R. Kanaar, and D. C. Rio. 1994. Regulation of tissue-specific P element pre-mRNA splicing requires the RNA-binding protein PSI. Genes Dev. 8:1713–1725.
   PubMedGoogle Scholar
• Siomi, H., and G. Dreyfuss. 1995. A nuclear localization domain in the hnRNP Al protein. J. Cell Biol. 129:551–560.
   PubMed Web of Science ®Google Scholar
• Smith, D. B., and K. S. Johnson. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31–40.
   PubMed Web of Science ®Google Scholar
• Vernet, T., D. Dignard, and D. Y. Thomas. 1987. A family of yeast expression vectors containing the phage f1 intergenic region. Gene 52:225–233.
   PubMed Web of Science ®Google Scholar
• Villarejo, M. R., and I. Zabin. 1974. Beta-galactosidase from termination and deletion mutant strains. J. Bacteriol. 120:466–474.
   PubMedGoogle Scholar
• Visa, N., E. Izaurralde, J. Ferreira, B. Daneholt, and I. W. Mattaj. 1996. A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscription-ally and accompanies the ribonucleoprotein particle during nuclear export. J. Cell Biol. 133:5–14.
   PubMed Web of Science ®Google Scholar
• Weighardt, F., G. Biamonti, and S. Riva. 1995. Nucleocytoplasmic distribution of human hnRNP proteins: a search for the targeting domains in hnRNP Al. J. Cell Sci. 108:545–555.
   PubMed Web of Science ®Google Scholar