Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 Mar;74(3):1013–1015. doi: 10.1073/pnas.74.3.1013

Ionic regulation in genetic translation systems.

P Douzou, P Maurel
PMCID: PMC430567  PMID: 15251

Abstract

The polyelectrolyte theory can provide an interpretation of the interdependence of pH, ionic strength, and polyamines one observes in the activity of ribonuclease acting on RNA. According to this theory: (i) A nucleic acid-enzyme complex and the suspending medium may be considered as two phases in equilibrium, even though within limits, the complex is soluble in water. (ii) The enzymatic catalysis is under tight control of the electrostatic potential generated by the system. Consequently, modification in electrostatic potential will induce a concomitant change in activity. (iii) The electrostatic potential can be modified through action on the system of "modulators", either "external" (ionic strength, pH, temperature, etc.) or "internal" (specific ligands, substrates, protein factors, etc.). Similarities between the reaction of ribonuclease (ribonuclease 3'-pyrimidino-oligonucleotidohydrolase; EC 3.1.4.22) and RNA and those observed with highly organized systems catalyzing DNA, RNA, and protein synthesis suggest that the electrostatic potential also provides an important regulatory mechanism in genetic translation. In this view, an essential function of nucleic acids is to provide their enzyme partners with polyanionic microenvironments within which their catalytic activities are controlled by variation in physicochemical parameters, including the proton concentration induced through "modulation" of the local electrostatic potential.

Full text

PDF
1013

Selected References

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

  1. Arai N., Kaziro Y. Mechanism of the ribosome-dependent uncoupled GTPase reaction catalyzed by polypeptide chain elongation factor G. J Biochem. 1975 Feb;77(2):439–447. doi: 10.1093/oxfordjournals.jbchem.a130743. [DOI] [PubMed] [Google Scholar]
  2. Byrnes J. J., Downey K. M., So A. G. Bone marrow cytoplasmic deoxyribonucleic acid polymerase. Variation of pH and ionic environment as a possible control mechanism. Biochemistry. 1973 Oct 23;12(22):4378–4384. doi: 10.1021/bi00746a013. [DOI] [PubMed] [Google Scholar]
  3. GOLDSTEIN L., LEVIN Y., KATCHALSKI E. A WATER-INSOLUBLE POLYANIONIC DERIVATIVE OF TRYPSIN. II. EFFECT OF THE POLYELECTROLYTE CARRIER ON THE KINETIC BEHAVIOR OF THE BOUND TRYPSIN. Biochemistry. 1964 Dec;3:1913–1919. doi: 10.1021/bi00900a022. [DOI] [PubMed] [Google Scholar]
  4. IRIE M. EFFECTS OF SALTS ON THE REACTION OF BOVINE PANCREATIC RIBONUCLEASE. J Biochem. 1965 Mar;57:355–362. doi: 10.1093/oxfordjournals.jbchem.a128089. [DOI] [PubMed] [Google Scholar]
  5. Igarashi K., Kumagai H., Watanabe Y., Toyoda N., Hirose S. Change of substrate specificity by polyamines of ribonucleases which hydrolyze ribonucleic acid at linkages attached to pyrimidine nucleotides. Biochem Biophys Res Commun. 1975 Dec 1;67(3):1070–1077. doi: 10.1016/0006-291x(75)90783-4. [DOI] [PubMed] [Google Scholar]
  6. KALNITSKY G., HUMMEL J. P., DIERKS C. [Some factors which affect the enzymatic digestion of ribonucleic acid]. J Biol Chem. 1959 Jun;234(6):1512–1516. [PubMed] [Google Scholar]
  7. KOTIN L. ON THE EFFECT OF IONIC STRENGTH ON THE MELTING TEMPERATURE OF DNA. J Mol Biol. 1963 Sep;7:309–311. doi: 10.1016/s0022-2836(63)80009-1. [DOI] [PubMed] [Google Scholar]
  8. Maurel P., Douzou P. Catalytic implications of electrostatic potentials: the lytic activity of lysozymes as a model. J Mol Biol. 1976 Apr 5;102(2):253–264. doi: 10.1016/s0022-2836(76)80052-6. [DOI] [PubMed] [Google Scholar]
  9. Pon C. L., Gualerzi C. The role of 16S rRNA in ribosomal binding of IF-3. Biochemistry. 1976 Feb 24;15(4):804–811. doi: 10.1021/bi00649a012. [DOI] [PubMed] [Google Scholar]
  10. Raae A. J., Kleppe R. K., Kleppe K. Kinetics and effect of salts and polyamines on T4 polynucleotide ligase. Eur J Biochem. 1975 Dec 15;60(2):437–443. doi: 10.1111/j.1432-1033.1975.tb21021.x. [DOI] [PubMed] [Google Scholar]
  11. Voigt J., Sander G., Nagel K., Parmeggiani A. Effect of NH+4 and K+ on the activity of the ribosomal subunits in the EF-G- and EF-T-dependent GTR hydrolysis. Biochem Biophys Res Commun. 1974 Apr 23;57(4):1279–1286. doi: 10.1016/0006-291x(74)90834-1. [DOI] [PubMed] [Google Scholar]
  12. Walter G., Zillig W., Palm P., Fuchs E. Initiation of DNA-dependent RNA synthesis and the effect of heparin on RNA polymerase. Eur J Biochem. 1967 Dec;3(2):194–201. doi: 10.1111/j.1432-1033.1967.tb19515.x. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES