Skip to main content
NCBI home page
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1983 Oct 25;11(20):7057–7068. doi: 10.1093/nar/11.20.7057

Different RNA patterns of globin and non-globin 40S heterogeneous nuclear RNA-protein complexes in chicken reticulocyte nuclei.

H M Huang, C B Chae
PMCID: PMC326438  PMID: 6634409

Abstract

40s heterogeneous nuclear RNA-protein complex (HnRNP) was isolated from chicken reticulocyte nuclei after digestion of RNA by the endogenous nuclease. The size of the total RNA and beta globin RNA was compared by agarose and high resolution acrylamide gel electrophoresis. The results show that size of the total RNA ranges between 20 to 650 bases and the most prominent sizes are between 20 and 70-80 bases. The size of the RNA increases at roughly 10 base intervals between 40 and 70 bases on an acrylamide gel. The size of the beta globin RNA is smaller (25-50 bases) than the total RNA and also the RNA pattern is considerably different from that of total RNA. This suggests that, although the overall structure of 40s HnRNP might be the same, there is significant differences in the interaction of globin RNA with HnRNP protein and that of non-globin RNA with HnRNP protein in chicken reticulocyte nuclei.

Full text

PDF
7057

Images in this article

7062Image
on p.7062
7063Image
on p.7063
7064Image
on p.7064
7065Image
on p.7065

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bantle J. A., Hahn W. E. Complexity and characterization of polyadenylated RNA in the mouse brain. Cell. 1976 May;8(1):139–150. doi: 10.1016/0092-8674(76)90195-1. [DOI] [PubMed] [Google Scholar]
  2. Beyer A. L., Christensen M. E., Walker B. W., LeStourgeon W. M. Identification and characterization of the packaging proteins of core 40S hnRNP particles. Cell. 1977 May;11(1):127–138. doi: 10.1016/0092-8674(77)90323-3. [DOI] [PubMed] [Google Scholar]
  3. Beyer A. L., Miller O. L., Jr, McKnight S. L. Ribonucleoprotein structure in nascent hnRNA is nonrandom and sequence-dependent. Cell. 1980 May;20(1):75–84. doi: 10.1016/0092-8674(80)90236-6. [DOI] [PubMed] [Google Scholar]
  4. Ciejek E. M., Nordstrom J. L., Tsai M. J., O'Malley B. W. Ribonucleic acid precursors are associated with the chick oviduct nuclear matrix. Biochemistry. 1982 Sep 28;21(20):4945–4953. doi: 10.1021/bi00263a018. [DOI] [PubMed] [Google Scholar]
  5. Civelli O., Vincent A., Maundrell K., Buri J. F., Scherrer K. The translational repression of globin mRNA in free cytoplasmic ribonucleoprotein complexes. Eur J Biochem. 1980 Jun;107(2):577–585. doi: 10.1111/j.1432-1033.1980.tb06066.x. [DOI] [PubMed] [Google Scholar]
  6. Economidis I. V., Pederson T. Structure of nuclear ribonucleoprotein: heterogeneous nuclear RNA is complexed with a major sextet of proteins in vivo. Proc Natl Acad Sci U S A. 1983 Mar;80(6):1599–1602. doi: 10.1073/pnas.80.6.1599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hamkalo B. A., Miller O. L., Jr, Bakken A. H. Ultrastructure of active eukaryotic genomes. Cold Spring Harb Symp Quant Biol. 1974;38:915–919. doi: 10.1101/sqb.1974.038.01.093. [DOI] [PubMed] [Google Scholar]
  8. Imaizumi-Scherrer M. T., Maundrell K., Civelli O., Scherrer K. Transcriptional and post-transcriptional regulation in duck erythroblasts. Dev Biol. 1982 Sep;93(1):126–138. doi: 10.1016/0012-1606(82)90246-9. [DOI] [PubMed] [Google Scholar]
  9. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  10. Lehrach H., Diamond D., Wozney J. M., Boedtker H. RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination. Biochemistry. 1977 Oct 18;16(21):4743–4751. doi: 10.1021/bi00640a033. [DOI] [PubMed] [Google Scholar]
  11. Lutter L. C. Precise location of DNase I cutting sites in the nucleosome core determined by high resolution gel electrophoresis. Nucleic Acids Res. 1979 Jan;6(1):41–56. doi: 10.1093/nar/6.1.41. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Malcolm D. B., Sommerville J. The structure of chromosome-derived ribonucleoprotein in oocytes of Triturus cristatus carnifex (Laurenti). Chromosoma. 1974;48(2):137–158. doi: 10.1007/BF00283960. [DOI] [PubMed] [Google Scholar]
  13. Maniatis T., Jeffrey A., van deSande H. Chain length determination of small double- and single-stranded DNA molecules by polyacrylamide gel electrophoresis. Biochemistry. 1975 Aug 26;14(17):3787–3794. doi: 10.1021/bi00688a010. [DOI] [PubMed] [Google Scholar]
  14. Mariman E. C., van Eekelen C. A., Reinders R. J., Berns A. J., van Venrooij W. J. Adenoviral heterogeneous nuclear RNA is associated with the host nuclear matrix during splicing. J Mol Biol. 1982 Jan 5;154(1):103–119. doi: 10.1016/0022-2836(82)90420-x. [DOI] [PubMed] [Google Scholar]
  15. Maundrell K., Scherrer K. Characterization of pre-messenger-RNA-containing nuclear ribonucleoprotein particles from avian erythroblasts. Eur J Biochem. 1979 Sep;99(2):225–238. doi: 10.1111/j.1432-1033.1979.tb13249.x. [DOI] [PubMed] [Google Scholar]
  16. Maxam A. M., Gilbert W. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 1980;65(1):499–560. doi: 10.1016/s0076-6879(80)65059-9. [DOI] [PubMed] [Google Scholar]
  17. Pederson T. Proteins associated with heterogeneous nuclear RNA in eukaryotic cells. J Mol Biol. 1974 Feb 25;83(2):163–183. doi: 10.1016/0022-2836(74)90386-6. [DOI] [PubMed] [Google Scholar]
  18. Rigby P. W., Dieckmann M., Rhodes C., Berg P. Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I. J Mol Biol. 1977 Jun 15;113(1):237–251. doi: 10.1016/0022-2836(77)90052-3. [DOI] [PubMed] [Google Scholar]
  19. Ross D. A., Yen R. W., Chae C. B. Association of globin ribonucleic acid and its precursors with the chicken erythroblast nuclear matrix. Biochemistry. 1982 Feb 16;21(4):764–771. doi: 10.1021/bi00533a029. [DOI] [PubMed] [Google Scholar]
  20. Samarina O. P., Lukanidin E. M., Molnar J., Georgiev G. P. Structural organization of nuclear complexes containing DNA-like RNA. J Mol Biol. 1968 Apr 14;33(1):251–263. doi: 10.1016/0022-2836(68)90292-1. [DOI] [PubMed] [Google Scholar]
  21. Stévenin J., Gattoni R., Divilliers G., Jacob M. Rearrangements in the course of ribonuclease hydrolysis of pre-messenger ribonucleoproteins. A warning. Eur J Biochem. 1979 Apr;95(3):593–606. doi: 10.1111/j.1432-1033.1979.tb13000.x. [DOI] [PubMed] [Google Scholar]
  22. Stévenin J., Gattoni R., Keohavong P., Jacob M. Mild nuclease treatment as a probe for a non-random distribution of adenovirus-specific RNA sequences and of cellular RNA in nuclear ribonucleoprotein fibrils. J Mol Biol. 1982 Mar 5;155(3):185–205. doi: 10.1016/0022-2836(82)90001-8. [DOI] [PubMed] [Google Scholar]
  23. Wahl G. M., Stern M., Stark G. R. Efficient transfer of large DNA fragments from agarose gels to diazobenzyloxymethyl-paper and rapid hybridization by using dextran sulfate. Proc Natl Acad Sci U S A. 1979 Aug;76(8):3683–3687. doi: 10.1073/pnas.76.8.3683. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Wang D., Moore S. Preparation of protease-free and ribonuclease-free pancreatic deoxyribonuclease. J Biol Chem. 1978 Oct 25;253(20):7216–7219. [PubMed] [Google Scholar]
  25. Wold B. J., Klein W. H., Hough-Evans B. R., Britten R. J., Davidson E. H. Sea urchin embryo mRNA sequences expressed in the nuclear RNA of adult tissues. Cell. 1978 Aug;14(4):941–950. doi: 10.1016/0092-8674(78)90348-3. [DOI] [PubMed] [Google Scholar]
  26. van Eekelen C. A., van Venrooij W. J. hnRNA and its attachment to a nuclear protein matrix. J Cell Biol. 1981 Mar;88(3):554–563. doi: 10.1083/jcb.88.3.554. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Nucleic Acids Research are provided here courtesy of Oxford University Press

RESOURCES