Ribonucleoproteins Package 700 nucleotides of Pre-mRNA into a Repeating Array of Regular Particles

LITERATURE CITED

• Beyer, A. L. 1983. Ultrastructural analysis of the ribonucleoprotein structure of nascent hnRNA. Mol. Biol. Rep. 9:49–58.
   PubMedGoogle Scholar
• Beyer, A. L., A. H. Bouton, and O. L. Miller, Jr. 1981. Correlation of hnRNP structure and nascent transcript cleavage. Cell 26:155–165.
   PubMed Web of Science ®Google Scholar
• Beyer, A. L., M. E. Christensen, B. W. Walker, and W. M. LeStourgeon. 1977. Identification and characterization of the packaging proteins of core 40S hnRNP particles. Cell 11:127–138.
   PubMed Web of Science ®Google Scholar
• Beyer, A. L., O. L. Miller, Jr., and S. L. McKnight. 1980. Ribonucleoprotein structure in nascent hnRNA is nonrandom and sequence-dependent. Cell 20:75–84.
   PubMedGoogle Scholar
• Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254.
   PubMed Web of Science ®Google Scholar
• Choi, Y. D., and G. Dreyfuss. 1984. Isolation of the hnRNA- ribonucleoprotein complex (hnRNP): a unique supramolecular assembly. Proc. Natl. Acad. Sci. USA 81:7471–7475.
   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
• Chung, S. Y., and J. Wooley. 1986. A set of novel, conserved proteins fold pre-messenger RNA into ribonucleosomes. Proteins: Struct. Funct. Genet. 1:195–210.
   PubMedGoogle Scholar
• Daskal, Y., L. Komaromy, and H. Busch. 1980. Isolation and partial characterization of perichromatin granules. Exp. Cell Res. 126:39–46.
   PubMed Web of Science ®Google Scholar
• Dreyfuss, G. 1986. Structure and function of nuclear and cytoplasmic ribonucleoprotein particles. Annu. Rev. Cell Biol. 2:457–496.
   Google Scholar
• Dreyfuss, G., Y. D. Choi, and S. A. Adam. 1984. Characterization of heterogeneous nuclear RNA-protein complexes in vivo with monoclonal antibodies. Mol. Cell. Biol. 4:1104–1114.
   PubMedGoogle Scholar
• Economides, I. V., and T. Pederson. 1983. Structure of nuclear ribonucleoprotein: heterogeneous nuclear RNA is complexed with a major sextet of proteins in vivo. Proc. Natl. Acad. Sci. USA 80:1599–1602.
   PubMedGoogle Scholar
• Fakan, S., L. Leser, and T. E. Martin. 1984. Ultrastructural distribution of nuclear ribonucleoproteins as visualized by immunocytochemistry on thin sections. J. Cell Biol. 98:358–363.
   PubMedGoogle Scholar
• Glatzer, K. H., and P.-M. Kloetzel. 1986. Differential chromosomal distribution of ribonucleoprotein antigens in nuclei of Drosophila spermatocytes. J. Cell Biol. 103:2113–2119.
   PubMedGoogle Scholar
• Grabowski, P. J., R. A. Padgett, and P. A. Sharp. 1984. Messenger RNA splicing in vitro: an excised intervening sequence and a potential intermediate. Cell 37:415–427.
   PubMed Web of Science ®Google Scholar
• Grabowski, P. J., S. R. Seiler, and P. A. Sharp. 1985. A multicomponent complex is involved in the splicing of messenger RNA precursors. Cell 42:345–353.
   PubMed Web of Science ®Google Scholar
• Green, M. R. 1986. Pre-mRNA splicing. Annu. Rev. Genet. 20:671–708.
   PubMed Web of Science ®Google Scholar
• Itzhaki, R. F., and D. M. Gill. 1964. A micro-biuret method for estimating proteins. Anal. Biochem. 9:401–410.
   PubMed Web of Science ®Google Scholar
• Konarska, M. M., P. J. Grabowski, R. A. Padgett, and P. A. Sharp. 1985. Characterization of the branch site in lariat RNA produced by splicing of mRNA precursors. Nature (London) 313:552–557.
   PubMed Web of Science ®Google Scholar
• Konarska, M. M., R. A. Padgett, and P. A. Sharp. 1984. Recognition of cap structure in splicing in vitro of mRNA precursors. Cell 38:731–736.
   PubMed Web of Science ®Google Scholar
• Kumar, A., K. R. Williams, and W. Szer. 1986. Purification and domain structure of core hnRNP proteins Al and A2, and their relation to ssDNA binding proteins. J. Biol. Chem. 261:11266–11274.
   PubMedGoogle Scholar
• Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685.
   PubMed Web of Science ®Google Scholar
• LeStourgeon, W. M., A. L. Beyer, M. E. Christensen, B. W. Walker, S. Poupore, and L. P. Daniels. 1978. The packaging proteins of core hnRNP particles and the maintenance of proliferative cell states. Cold Spring Harbor Symp. Quant. Biol. 42:885–898.
   PubMedGoogle Scholar
• LeStourgeon, W. M., L. Lothstein, B. W. Walker, and A. L. Beyer. 1981. The composition and general topology of RNA and protein in monomer 40S ribonucleoprotein particles, p. 49–87. In H. Busch (ed.), The cell nucleus, vol. 9. Nuclear particles. Academic Press, Inc., New York.
   Google Scholar
• Lothstein, L., H. P. Arenstorf, S. Chung, B. W. Walker, J. C. Wooley, and W. M. LeStourgeon. 1985. General organization of protein in HeLa 40S nuclear ribonucleoprotein particles. J. Cell Biol. 100:1570–1581.
   PubMedGoogle Scholar
• Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265–273.
   PubMed Web of Science ®Google Scholar
• Malcolm, D., and J. Sommerville. 1974. The structure of chromosome-derived ribonucleoprotein in oocytes of Triturus cristatus carnifex (Laurenti). Chromosoma 48:137–158.
   PubMedGoogle Scholar
• Malcolm, D. B., and J. Sommerville. 1977. The structure of nuclear ribonucleoprotein of amphibian oocytes. J. Cell Sci. 24:143–165.
   PubMedGoogle Scholar
• Maniatis, T., E. F. Fritsch, and J. Sambrook. 1982. Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Maniatis, T., and R. Reed. 1987. The role of small nuclear ribonucleoprotein particles in pre-mRNA splicing. Nature (London) 325:673–678.
   PubMed Web of Science ®Google Scholar
• Martin, T., P. Billings, A. Levy, S. Ozarslan, T. Quinlan, H. Swift, and L. Urbas. 1974. Some properties of RNA:protein complexes from the nucleus of eukaryotic cells. Cold Spring Harbor Symp. Quant. Biol. 38:921–932.
   PubMedGoogle Scholar
• Martin, T. E., P. B. Billings, J. M. Pullman, B. J. Stevens, and A. J. Kinniburgh. 1978. Substructures of nuclear ribonucleoprotein complexes. Cold Spring Harbor Symp. Quant. Biol. 42:899–909.
   PubMedGoogle Scholar
• Mayrand, S., and T. Pederson. 1981. Nuclear ribonucleoprotein particles probed in living cells. Proc. Natl. Acad. Sci. USA 78:2208–2212.
   PubMed Web of Science ®Google Scholar
• Melton, D. A., P. A. Krieg, M. R. Rebagliati, T. Maniatis, K. Zinn, and M. R. Green. 1984. Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res. 12:7035–7056.
   PubMed Web of Science ®Google Scholar
• Osheim, Y. N., and O. L. Miller, Jr. 1983. Novel amplification and transcriptional activity of chorion genes in Drosophila melanogaster follicle cells. Cell 33:543–553.
   PubMed Web of Science ®Google Scholar
• Osheim, Y. N., O. L. Miller, Jr., and A. L. Beyer. 1985. RNP particles and splice junction sequences in Drosophila chorion transcripts. Cell 43:143–151.
   PubMed Web of Science ®Google Scholar
• Pederson, T. 1974. Proteins associated with heterogeneous nuclear RNA in eucaryotic cells. J. Mol. Biol. 83:163–183.
   PubMedGoogle Scholar
• Pederson, T. 1983. Nuclear RNA-protein interactions and messenger RNA processing. J. Cell Biol. 97:1321–1326.
   PubMedGoogle Scholar
• Pullman, J. M., and T. E. Martin. 1983. Reconstitution of nucleoprotein complexes with mammalian heterogeneous nuclear ribonucleoprotein (hnRNP) core proteins. J. Cell Biol. 97:99–111.
   PubMedGoogle Scholar
• Riva, S., C. Morandi, P. Tsoulfus, M. Pandolfo, G. Biamonti, B. Merrill, K. R. Williams, G. Multhany, K. Bayrerther, H. Werr, B. Henrich, and K. P. Schafer. 1986. Mammalian singlestranded DNA binding protein UP1 is derived from the hnRNP core protein Al. EMBO J. 5:2267–2274.
   PubMed Web of Science ®Google Scholar
• Samarina, O. P., E. M. Lukanidin, J. Molnar, and G. P. Georgiev. 1968. Structural organization of nuclear complexes containing DNA-like RNA. J. Mol. Biol. 33:251–263.
   PubMed Web of Science ®Google Scholar
• Sharp, P. 1987. Splicing of messenger RNA precursors. Science 235:766–771.
   PubMed Web of Science ®Google Scholar
• Sierakowska, H., W. Szer, P. J. Furdon, and R. Kole. 1986. Antibodies to hnRNP proteins inhibit in vitro splicing of human beta-globin pre-mRNA. Nucleic Acids Res. 14:5241–5254.
   PubMedGoogle Scholar
• Thomas, J. O., S. K. Glowacka, and W. Szer. 1983. Structure of complexes between a major protein of heterogeneous nuclear ribonucleoprotein particles and polyribonucleotides. J. Mol. Biol. 171:439–455.
   PubMedGoogle Scholar
• Tsanev, R. G., and L. P. Djondjurov. 1982. Ultrastructure of free ribonucleoprotein complexes in spread mammalian nuclei. J. Cell Biol. 94:662–666.
   PubMedGoogle Scholar
• Van Eekelen, C. A., T. Riemer, and W. J. Van Venrooj. 1981. Specificity in the interaction of hnRNA and mRNA with proteins as revealed by in vivo crosslinking. FEBS Lett. 130:223–226.
   PubMedGoogle Scholar
• Walker, B. W., L. Lothstein, C. L. Baker, and W. M. LeStourgeon. 1980. The release of 40S hnRNP particles by brief digestion of HeLa nuclei with micrococcal nuclease. Nucleic Acids Res. 8:3639–3658.
   PubMed Web of Science ®Google Scholar
• Wieringa, B., E. Hofer, and C. Weissmann. 1984. A minimal intron length but no specific internal sequence is required for splicing the large rabbit beta-globin intron. Cell 37:915–925.
   PubMed Web of Science ®Google Scholar
• Wilk, H., G. Angeli, and K. Shafer. 1983. in vitro reconstitution of 35S ribonucleoprotein complexes. Biochemistry 22:4592–4600.
   PubMedGoogle Scholar
• Williams, R. 1977. Use of polylysine for absorption of nucleic acids and enzymes to electron microscope specimen films. Proc. Natl. Acad. Sci. USA 74:2311–2315.
   PubMed Web of Science ®Google Scholar
• Wooley, J., S. Y. Chung, J. Wall, and W. M. LeStourgeon. 1986. Architecture of pre-messenger, nuclear ribonucleoprotein monoparticles. Biophys. J. 49:17–19.
   PubMedGoogle Scholar