Abstract
Many ultrastructural and biochemical findings suggest that pre-mRNA is packaged during transcription into a repeating array of regular ribonucleoprotein particles by the six “core” proteins of 40S nuclear ribonucleoprotein particles (40S hnRNP particles). If true, then pre-mRNA is packaged in a fashion not totally dissimilar to the nucleosomal packaging of DNA. While the packaging of nascent transcripts into a repeating “ribonucleosome” structure [1,2] seems to complicate our present view of RNA splicing (i.e., splice site recognition, spliceosome assembly, lariat formation, excision, and ligation), there is considerable evidence that all these events do occur while RNA exists in a highly packaged state. On this point it is worth noting that biological systems have worked through the structural and sequence recognition problems created by the packaging of DNA into nucleosomes. More important, it now seems likely that the events of RNA processing can be understood in mechanistic detail because much progress has recently been made in the ability to isolate and study the fundamental repeating element of nascent transcripts and to monitor the biochemical events of RNA packaging in vitro. A better knowledge of monoparticle structure is a prerequisite to a detailed understanding of the events of RNA processing and will help to clarify present attempts to “characterize” the spliceosome complex, a structure quite different from the 40S hnRNP particles that function to package the bulk of nascent pre-mRNA transcripts and prevent the formation of heteroduplex RNA.
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References
Oda, T., Nakamura, T., and Watanabe, S. (1977) J. Electron. Microsc. (Tokyo) 26, 203–207.
Chung, S.Y., and Wooley, J. (1986) Proteins Struct. Func. Genet. 1, 195–210.
Derenzini, M., Pession-Brizzi, A., and Novello, F. (1981) J. Ultrastruct. Res. 77, 66–82.
Mott, M.R., and Callan, H.G. (1975) J. Cell. Sci. 17, 241–261.
Skoglund, U., et al. (1983) Cell 34, 847–855.
Lamb, M., and Daneholt, B. (1979) Cell 17, 835–848.
Olins, A., et al. (1984) Eur. J. Cell Biol. 35, 129–142.
Olins, D., et al., (1983) Science 220, 498–500.
Skoglund, U., Anderson, K., Strandberg, B., and Daneholt, B. (1986) Nature 319, 560–564.
Osheim, Y.N., Miller, O.L. Jr., and Beyer, A.L. (1985) Cell 43, 143–151.
Kierszenbaum, A.L., and Tres, L.L. (1974) J. Cell Biol. 63, 923–935.
Beyer, A., Miller, O., and McKnight, S. (1980) Cell 20, 75–84.
Beyer, A.L. (1983) Mol. Biol. Rep. 9, 49–58.
Beyer, A.L., Bouton, A.H., and Miller, O.L. Jr. (1981) Cell 26, 155–163.
Malcolm, D.B., and Sommerville, J. (1974) Chromosoma 48, 137–158.
Sommerville, J.J. (1973) J. Mol. Biol. 78, 487–503.
Sommerville, J. (1981) In The Cell Nucleus Vol. 8, 1–57, Busch, H. (ed.). Academic Press, New York.
Tsanev, R.G., and Djondurov, L.P. (1982) J. Cell Biol. 94, 662–666.
Fakan, S., Leser, G., and Martin, T.E. (1986) J. Cell Biol. 103, 1153–1157.
N’Da, E., Bonnanfant-Jais, M.L., Penrad-Mobayed, M., and Angelier N. (1986) J. Cell Sci. 81, 17–27.
Malcolm, D., and Sommerville, J (1977) J. Cell. Sci. 24, 143–165.
Samarina, O., and Krichevskaya, A. (1981) In The Cell Nucleus Vol. 9, 1–48, Busch, H. (ed.). Academic Press, New York.
Samarina, O.P., Lukanidin, E.M., Molnar, J., and Georgiev, G.P. (1968) J. Mol. Biol. 33, 251–263.
Samarina, O.P., Lukanidin, E.M., and Georgiev, G.P. (1967) Biochim. Biophys. Acta 142, 561–564.
Beyer, A.L., Christensen, M.E., Walker, B.W., and LeStourgeon, W.M. (1977) Cell 11, 127–138.
Conway, G., Wooley, J., Bibring, T., and LeStourgeon, W.M. (1988) Mol. Cell. Biol. 8, 2884–2895.
Lothstein, L., et al. (1985) J. Cell Biol. 100, 1570–1581.
Walker, B.W., Lothstein, L., Baker, C.L., and LeStourgeon, W.M. (1980) Nucleic Acids Res. 8, 3639–3657.
Martin, T.E., et al. (1978) Cold Spring Harbor Symp. Quant. Biol. 42, 899–909.
Kinneburgh, A.J., Billings, P.B., Quinlan, T.J., and Martin, T.E. (1976) Prog. Nucleic Acid Res. Mol. Biol. 19, 335–351.
Kish, V.M., and Pederson, T. (1978) Methods Cell Biol. 17, 377–399.
Munroe, S.H., and Pederson, T.J. (1981) Mol. Biol. 147, 437–449.
LeStourgeon, W.M., et al. (1977) Cold Spring Harbor Symp. Quant. Biol. 42, 885–898.
Economidis, I.V., and Pederson, T. (1983) Proc. Natl. Acad. Sci. USA 80, 1599–1602.
Wilk, H.E., Angeli, G., and Schafer, K.P. (1983) Biochemistry 22, 4592–4600.
Wilk, H.E., et al. (1985) Eur. J. Biochem. 146, 71–81.
Barnett, S.F., Friedman, D.L., and LeStourgeon, W.M. (1989) Mol. Cell Biol. 9, 492–498.
LeStourgeon, W.M., Lothstein, L., Walker, B., and Beyer, A. (1981) In The Cell Nucleus, 49–87, Busch, H. (ed.). Vol. 9, Academic Press, New York.
Karn, J., Vidali, G., Boffa, L., and Allfrey, V. (1977) J. Biol. Chern. 252, 969–976.
Pullman, J.M., and Martin, T.E. (1983) J. Cell Biol. 97, 99–111.
Choi, Y.D., and Dreyfuss, G. (1984) Proc. Natl. Acad. Sci USA 81, 7471–7475.
Dreyfuss, G., Choi, Y.D., and Adam, S.A. (1984) Mol. Cell. Biol. 4, 1104–1114.
Kinneburgh, A., and Martin, T. (1976) Proc. Natl. Acad. Sci. USA 73, 2725–2729.
Pederson, T., and Davis, N.G. (1980) J. Cell Biol. 87, 47–54.
Fakan, S., Leser, G., and Martin, T. (1983) J. Cell Biol. 98, 358–363.
Spirin, A.S., Belitsina, N.V., and Lerman, M.I. (1965) J. Mol. Biol. 14, 611–615.
Jones, R.E., Okamura, C.S., and Martin, T.E. (1980) J. Cell Biol. 86, 235–243.
Christensen, M.E., et al. (1981) J. Cell Biol. 90, 18–24.
Choi, Y.D., and Dreyfuss, G. (1984) J. Cell Biol. 99, 1997–2004.
Pinol-Roma, S., Choi, Y.D., Matunis, M.J., and Dreyfuss, G. (1988) Genes Dev. 2, 215–227.
Roth, M., and Gall, J. (1987) J. Cell Biol. 105, 1047–1054.
Holcomb, E.R., and Friedman, D.L. (1984) J. Biol. Chem. 259, 31–40.
Blanchard, J.M., Brunei, C., and Jeanteur, P. (1977) Biochem. Soc. Trans. 5, 670–671.
Periasamy, M., Brunei, C., and Jeanteur, P. (1979) Biochimie 61, 823–826.
Periasamy, M., Brunei, C., Blanchard, J.M., and Jeanteur, P. (1977) Biochem. Biophys. Res. Commun. 79, 1077–1083.
Niessing, J., and Sekeris, C.E. (1970) Biochim. Biophys. Acta 209, 484–492.
Molnar-Kimber, K., Summers, J., Taylor, J., and Mason, W.J. (1983) J. Virology 45, 165–172.
Dreyfuss, G. (1986) Annu. Rev. Cell. Biol. 2, 457–495.
LeStourgeon, W.M., Lothstein, L., Walker, B., and Beyer, A. (1981) In The Cell Nucleus Vol. 9, 49–87, Busch, H. (ed.). Academic Press, New York.
Kinneburgh, A.J., and Martin, T.E. (1976) Biochem. Biophys. Res. Commun. 73, 718–726.
Augenlicht, L.H., and Lipkin, M. (1976) J. Biol. Chem. 251, 2592–2599.
Volkova, I.V., and Gauze, L.N. (1982) Mol. Biol. (Mosk.) 16, 123–128.
Barnett, S.F., and LeStourgeon, W.M. (1989) Mol. Cell Biol. 9, 492–498.
Celis, J.E., Bravo, R., Arenstorf, H.P., and LeStourgeon W.M. (1986) FEBS Lett. 194, 101–109.
Loeb, J., Ritz, E., Creuzet, C., and Jami, J. (1976) Exp. Cell. Res. 103, 4540–4553.
Wang, K., and Richard, F. (1974) J. Biol. Chem. 249, 375–389.
Barnett, S.F., LeStourgeon, W.M., and Friedman, D.L. (1988) J. Biochem. Biophys. Methods 16, 87–98.
Swanson, M.S., Nakagawa, T.Y., LeVan, K., and Dreyfuss, G. (1987) Mol. Cell. Biol. 7, 1731–1739.
Thiery, T., Barnett, S.F., Bibring, T., and LeStourgeon, W.M. (1989) (in press).
Thomas, J.O., Glowacka, S.K., and Szer, W. (1983) J. Mol. Biol. 171, 439–455.
Cobianchi, F., et al. (1988) J. Biol. Chem. 263, 1063–1071.
Wooley, J., Chung, S.Y., Wall, J., and LeStourgeon W.M. (1986) Biophys. J. 49, 17–19.
Daskal, Y., Komaromy, I., and Busch, H. (1980) Exp. Cell. Res. 126, 39–46.
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Barnett, S.F., Northington, S.J., LeStourgeon, W.M. (1989). Ribonucleoproteins and the Structure of Nascent Transcripts. In: Adolph, K.W. (eds) Molecular Biology of Chromosome Function. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3652-8_12
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DOI: https://doi.org/10.1007/978-1-4612-3652-8_12
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