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PMID: 797388 Published · ppublish English Journal Article

A study of the influence of magnesium ions on the conformation of ribosomal ribonucleic acid and on the stability of the larger subribosomal particle of rabbit reticulocytes.

The Biochemical journal ·Vol. 160 ·No. 3 ·1976-12-15 ·Pages 505-19

Cox RA, Hirst W

Abstract

Mg2+ was shown to affect the conformation of rRNA over the range of 0.03-1.2M-KCl. The species studies were Escherichia coli S-rRNA and L-rRNA (the RNA moieties of the smaller and larger subribosomal particles respectively) and rabbits S-rRNA and L-rRNA. 2. The addition of Mg2+ to rRNA in reconstitution buffer (0.35M-KCl0.01M-Tris/HCl, pH7.2) at 20 degrees C let to an increase in bihelical secondary structure through the formation of additional (mainly A-U) base-pairs (e.g. an additional approx. 58 A-U base-pairs per molecule of E. coli S-rRNA as judged by u.v. difference spectrophotometry...

MeSH Terms
Ammonium Chloride/pharmacology Animals Base Sequence Escherichia coli/ultrastructure Magnesium/pharmacology Nucleic Acid Conformation/drug effects Potassium Chloride/pharmacology RNA, Ribosomal Rabbits Reticulocytes/ultrastructure Ribosomes/drug effects Spectrophotometry, Ultraviolet
Chemicals
RNA, Ribosomal Ammonium Chloride Potassium Chloride Magnesium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Cox R A
Hirst W
References (25)
25 references, click to expand
  1. Ribonucleic acid from Escherichia coli. III. The influence of ionic strength and temperature on hydrodynamic and optical properties.
    Biochim Biophys Acta. 1962 Aug 20;61:197-208 PMID: 13881911
  2. Reassembly of the peptidyltransferase centre of larger subparticles of rabbit reticulocyte ribosomes from a core-particle and split-protein fraction.
    Biochem J. 1976 Dec 15;160(3):533-46 PMID: 1016238
  3. Re-activation of the peptidyltransferase centre of rabbit reticulocyte ribosomes after inactivation by exposure to low concentrations of magnesium ion.
    Biochem J. 1976 Dec 15;160(3):521-31 PMID: 1016237
  4. Proton magnetic relaxation studies of marganous complexes of transfer RNA and related compounds.
    J Mol Biol. 1969 Jan 14;39(1):199-217 PMID: 4329286
  5. A study of the thermal stability of ribosomes and biologically active subribosomal particles.
    Biochem J. 1973 Jul;134(3):775-93 PMID: 4584137
  6. Cations and ribosome structure. 3. Effects on the 30S and 50S subunits of replacing bound Mg 2+ by inorganic cations.
    Biochemistry. 1973 Jan 30;12(3):450-6 PMID: 4566933
  7. Cations and ribosome structure. I. Effects on the 30S subunit of substituting polyamines for magnesium ion.
    Biochemistry. 1973 Jan 30;12(3):435-41 PMID: 4566931
  8. Conditions of structural and functional destabilization of mammalian ribosomes by magnesium ions.
    Biochim Biophys Acta. 1973 Aug 10;319(1):81-90 PMID: 4733695
  9. Magnesium-induced conformational change in transfer ribonucleic acid as measured by circular dichroism.
    Biochemistry. 1971 Jun 8;10(12):2216-22 PMID: 4940049
  10. Ionic effects on the ribosomal quaternary structure.
    Eur J Biochem. 1970 Mar 1;13(1):132-6 PMID: 4909094
  11. Structure and function of Escherichia coli ribosomes. VI. Mechanism of assembly of 30 s ribosomes studied in vitro.
    J Mol Biol. 1969 Mar 28;40(3):391-413 PMID: 4903714
  12. Structure of Escherichia coli ribosomes: effect of ribonuclease on the 30-S and 50-S subunits.
    Biochim Biophys Acta. 1970 Apr 15;204(2):489-501 PMID: 4909654
  13. Assembly mapping of 30S ribosomal proteins from E. coli.
    Nature. 1970 Jun 27;226(5252):1214 PMID: 4912319
  14. A spectrophotometric study of the secondary structure of ribonucleic acid isolated from the smaller and larger ribosomal subparticles of rabbit reticulocytes.
    Biochem J. 1970 Mar;117(1):101-18 PMID: 4911953
  15. The circular dichroism of ribosomal ribonucleic acids.
    Biochem J. 1976 May 1;155(2):279-91 PMID: 820335
  16. Primary sequence of the 16S ribosomal RNA of Escherichia coli.
    Nucleic Acids Res. 1975 Feb;2(2):265-78 PMID: 1091918
  17. Detection of cation-specific conformational changes in ribosomal RNA by gel electrophoresis.
    Nucleic Acids Res. 1975 Apr;2(4):447-58 PMID: 1094419
  18. tRNA conformation and magnesium binding. A study of a yeast phenylalanine-specific tRNA by a fluorescent indicator and differential melting curves.
    Eur J Biochem. 1975 Jun 16;55(1):271-84 PMID: 1100382
  19. Evidence for tertiary structural RNA-RNA interactions within the protein S4 binding site at the 5'-end of 16S ribosomal RNA of Escherichia coli.+.
    Nucleic Acids Res. 1975 Oct;2(10):1867-88 PMID: 1103089
  20. Dissociation of ribosomes from oocytes of Xenopus laevis into active subparticles.
    Biochem J. 1971 Oct;124(5):897-903 PMID: 5167141
  21. Conformation of nucleic acids and the analysis of the hypochromic effect.
    Biochem J. 1970 Dec;120(3):539-47 PMID: 5499966
  22. Molecular weights of ribosomal RNA in relation to evolution.
    J Mol Biol. 1968 Dec;38(3):355-65 PMID: 5718556
  23. The effect of temperature on the magnesium binding and ultracentrifugal properties of rat liver ribosomes.
    Biochemistry. 1967 Sep;6(9):2950-8 PMID: 6055205
  24. The dissociation of reticulocyte polysomes into subunits and the location of messenger RNA.
    J Mol Biol. 1966 Feb;15(2):600-18 PMID: 5915184
  25. The function of high-molecular-weight ribonucleic acid from rabbit reticulocytes in haemoglobin biosynthesis.
    Biochem J. 1964 Sep;92(3):648-61 PMID: 5891199
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1976-12-15
Pages
505-19
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1164267
Subset
IM
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