Identification of Two RNA-Binding Proteins in Balbiani Ring Premessenger Ribonucleoprotein Granules and Presence of These Proteins in Specific Subsets of Heterogeneous Nuclear Ribonucleoprotein Particles

REFERENCES

• Baurén, G., and L. Wieslander. 1994. Splicing of Balbiani ring 1 gene pre-mRNA occurs simultaneously with transcription. Cell 76:183–192.
   PubMed Web of Science ®Google Scholar
• Bennett, M., S. Piñol-Roma, 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
• Burd, C. G., and G. Dreyfuss. 1994. RNA binding specificity of hnRNP: significance of hnRNP A1 high-affinity binding sites in pre-mRNA splicing. EMBO J. 13:1197–1204.
   PubMed Web of Science ®Google Scholar
• Burd, C. G., M. S. Swanson, M. Görlach, and G. Dreyfuss. 1989. Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1 and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts. Proc. Natl. Acad. Sci. USA 86:9788–9792.
   PubMed Web of Science ®Google Scholar
• Buvoli, M., F. Cobianchi, G. Biamonti, and S. Riva. 1990. Recombinant hnRNA protein A1 and its N-terminal domain show preferential affinity for oligodeoxynucleotides homologous to intron/exon acceptor sites. Nucleic Acids Res. 18:6595–6600.
   PubMed Web of Science ®Google Scholar
• Cáceres, 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., 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
• Chung, S. Y., and J. Wooley. 1986. Set of novel, conserved proteins fold premessenger RNA into ribonucleosomes. Proteins 1:195–210.
   PubMedGoogle Scholar
• Cobianchi, F., R. L. Karpel, K. R. Williams, V. Notario, and S. H. Wilson. 1988. Mammalian heterogeneous nuclear ribonucleoprotein complex protein A1. J. Biol. Chem. 263:1063–1071.
   PubMedGoogle Scholar
• Dreyfuss, G. 1986. Structure and function of nuclear and cytoplasmic ribonucleoprotein particles. Annu. Rev. Cell Biol. 2:459–498.
   PubMedGoogle 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
• Economides, I. V., and T. Pederson. 1983. In vitro assembly of a pre-messenger ribonucleoprotein. Proc. Natl. Acad. Sci. USA 80:4296–4300.
   PubMedGoogle Scholar
• Ghetti, A., S. Pinol-Roma, W. M. Michael, C. Morandi, and G. Dreyfuss. 1992. hnRNP I, the polypyrimidine tract-binding protein: distinct nuclear localization and association with hnRNAs. Nucleic Acids Res. 20:3671–3678.
   PubMed Web of Science ®Google Scholar
• Gil, A., P. A. Sharp, S. F. Jamison, and M. García-Blanco. 1991. Characterization of cDNAs encoding the polypyrimidine tract-binding protein. Genes Dev. 5:1224–1236.
   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
• Jacob, M., G. Devilliers, J. P. Fuchs, H. Gallinaro, R. Gattoni, C. Judes, and J. Stevenin. 1981. Isolation and structure of the ribonucleoprotein fibrils containing heterogeneous nuclear RNA, p. 193–246. In H. Busch (ed.), The cell nucleus, vol. 9. Academic Press, New York.
   Google Scholar
• Jones, K. E., C. S. Okamura, and T. E. Martin. 1980. Immunofluorescent localization of the proteins of nuclear ribonucleoprotein complexes. J. Cell Biol. 86:235–243.
   PubMed Web of Science ®Google Scholar
• Kiledjian, M., C. G. Burd, M. Görlach, D. S. Portman, and G. Dreyfuss. 1994. Structure and function of hnRNP proteins, p. 127–149. In K. Nagai and I. Mattaj (ed.), RNA-protein interactions: frontiers in molecular biology. Oxford University Press, Oxford.
   Google Scholar
• Kiseleva, E., T. Wurtz, N. Visa, and D. Daneholt. 1994. Assembly and disassembly of spliceosomes along a specific pre-messenger RNP fiber. EMBO J. 13:6052–6061.
   PubMedGoogle Scholar
• Lacroix, J. C., R. Azzouz, D. Boucher, C. Abbadie, C. K. Pyne, and J. Charlemagne. 1985. Monoclonal antibodies to lampbrush chromosome antigens of Pleurodeles waltlii. Chromosoma 92:69–80.
   PubMed Web of Science ®Google Scholar
• Lezzi, M., B. Meyer, and R. Mähr. 1981. Heat shock phenomena in Chi-ronomus tentans. I. In vivo effects of heat, overheat and quenching on salivary chromosome puffing. Chromosoma 83:327–339.
   PubMedGoogle Scholar
• Lönnroth, A., K. Alexciev, H. Mehlin, T. Wurtz, U. Skoglund, and B. Daneholt. 1992. Demonstration of a 7 nm RNP fiber as the basic structural element in a premessenger RNP particle. Exp. Cell Res. 199:292–296.
   PubMedGoogle 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, 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
• 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
• Mehlin, H., B. Daneholt, and U. Skoglund. 1992. Translocation of a specific premessenger RNP particle through the nuclear pore studied with electron microscope tomography. Cell 69:605–613.
   PubMed Web of Science ®Google Scholar
• Miller, O. L., and A. H. Bakken. 1972. Morphological studies of transcription. Karolinska Symp. Res. Methods Reprod. Endocrinol. 5:155–167.
   Google Scholar
• Moore, C. L., J. Chen, and J. Whoriskey. 1988. Two proteins crosslinked to RNA containing the adenovirus L3 poly(A) site require the AAUAAA sequence for binding. EMBO J. 7:3159–3169.
   PubMed Web of Science ®Google Scholar
• Nacheva, G., D. Guschin, O. Preobrazhenskaya, V. Karpov, K. Ebralidse, and A. Mirzabekov. 1989. Changes in the pattern of histone binding to DNA upon transcriptional activation. Cell 58:27–36.
   PubMed Web of Science ®Google Scholar
• Nadler, S. G., B. M. Merrill, W. J. Roberts, K. M. Keating, M. J. Lisbin, S. F. Barnett, S. H. Wilson, and K. R. Williams. 1991. Interactions of the A1 heterogeneous nuclear ribonucleoprotein and its proteolytic derivative, UP1, with RNA and DNA: evidence for multiple RNA binding domains and salt-dependent binding mode transitions. Biochemistry 30:2968–2975.
   PubMedGoogle Scholar
• Patton, J. G., S. A. Mayer, P. Tempst, and B. Nadal-Ginard. 1991. Characterization and molecular cloning of a polypyrimidine tract-binding protein: a component of a complex necessary for pre-mRNA splicing. Genes Dev. 5:1237–1251.
   PubMed Web of Science ®Google Scholar
• Peters, K. E., and D. E. Comings. 1980. Two-dimensional gel electrophoresis of rat liver nuclear washes, nuclear matrix, and hnRNA proteins. J. Cell Biol. 86:135–155.
   PubMedGoogle Scholar
• Pinol-Roma, S., Y. D. Choi, M. J. Matunis, and G. Dreyfuss. 1988. Immu-nopurification of heterogeneous nuclear ribonucleoprotein particles reveals an assortment of RNA-binding proteins. Genes Dev. 2:215–227.
   PubMed Web of Science ®Google Scholar
• Pinol-Roma, S., and G. Dreyfuss. 1992. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature (London) 355:730–732.
   PubMed Web of Science ®Google Scholar
• Pinol-Roma, S., M. S. Swanson, J. G. Gall, and G. Dreyfuss. 1989. A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts. J. Cell Biol. 109:2575–2587.
   PubMedGoogle Scholar
• Roth, M. B., and J. G. Gall. 1987. Monoclonal antibodies that recognize transcription unit proteins on newt lampbrush chromosomes. J. Cell Biol. 105:1047–1054.
   PubMed Web of Science ®Google Scholar
• Sierakowska, H., W. Szer, P. J. Furdon, and R. Kole. 1986. Antibodies to hnRNA core proteins inhibit in vitro splicing of human β globin pre-mRNA. Nucleic Acids Res. 14:5241–5254.
   PubMedGoogle Scholar
• Skoglund, U., K. Andersson, B. Bjorkroth, M. M. Lamb, and B. Daneholt. 1983. Visualization of the formation and transport of a specific hnRNP particle. Cell 34:847–855.
   PubMedGoogle Scholar
• Skoglund, U., K. Andersson, B. Strandberg, and B. Daneholt. 1986. Three-dimensional structure of a specific pre-messenger RNP particle established by electron microscope tomography. Nature (London) 319:560–564.
   PubMedGoogle Scholar
• Spirin, A. S. 1969. Informosomes. Eur. J. Biochem. 10:20–35.
   PubMedGoogle Scholar
• Swanson, M. S., and G. Dreyfuss. 1988. Classification and purification of proteins of heterogeneous nuclear ribonucleoprotein particles by RNA-binding specificities. Mol. Cell. Biol. 8:2237–2241.
   PubMed Web of Science ®Google Scholar
• Swanson, M. S., and G. Dreyfuss. 1988. RNA binding specificity of hnRNP proteins: a subset bind to the 3′ end of introns. EMBO J. 7:3519–3529.
   PubMed Web of Science ®Google Scholar
• Tunon, P., and K.-E. Johansson. 1984. Yet another improved silver staining method for the detection of proteins in polyacrylamide gels. J. Biochem. Biophys. Methods 9:171–179.
   PubMedGoogle Scholar
• Visa, N., and B. Daneholt. Unpublished results.
   Google Scholar
• Wieslander, L. 1994. The Balbiani ring multigene family: coding repetitive sequences and evolution of a tissue specific cell function. Prog. Nucleic Acid Res. Mol. Biol. 48:275–313.
   PubMed Web of Science ®Google Scholar
• Wilusz, J., and T. Shenk. 1990. A uridylate tract mediates efficient heterogeneous nuclear ribonucleoprotein C protein-RNA cross-linking and functionally substitutes for the downstream element of the polyadenylation signal. Mol. Cell. Biol. 10:6397–6407.
   PubMed Web of Science ®Google Scholar
• Wurtz, T., A. Lonnroth, L. Ovchinnikov, U. Skoglund, and B. Daneholt. 1990. Isolation and initial characterization of a specific premessenger ribonucleoprotein particle. Proc. Natl. Acad. Sci. USA 87:831–835.
   PubMedGoogle Scholar
• Wyss, C. 1982. Chironomus tentans epithelial cell lines sensitive to ecdysteroids, juvenile hormone, insulin and heat shock. Exp. Cell Res. 139:309–319.
   PubMed Web of Science ®Google Scholar