Skip to main content
Nucleic Acids Research logoLink to Nucleic Acids Research
. 1980 Jun 11;8(11):2489–2498. doi: 10.1093/nar/8.11.2489

Characterization of Mg2+-induced conformational change in the 50S ribosomal subunit by differential hydrogen exchange.

D Bonnet, E Begard, M Grunberg-Manago, G Hui Bon Hoa
PMCID: PMC324096  PMID: 7003535

Abstract

The technique of differential hydrogen exchange allows detection of a conformational change in the 50S subunit of Escherichia coli ribosome when the magnesium concentration is lowered in a range where ribosomal activity is fully preserved. This change is characterized by a seventy-fold acceleration of about thirty labile hydrogens in the case of a Mg2+ jump from 10 mM to 2 mM. The small number of hydrogens involved can explain the difficulty in detecting this change by other methods.

Full text

PDF
2489

Selected References

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

  1. Allen S. H., Wong K. P. Conformation of ribosomal proteins free in solution and bound to ribosomal RNA. Biochemistry. 1978 Sep 19;17(19):3971–3978. doi: 10.1021/bi00612a015. [DOI] [PubMed] [Google Scholar]
  2. Beaudry P., Begard E., Douzou P., Grunberg-Manago M. Protons and Mg2+ cations as probes in investigating the role of GTP in initiation complex formation. Eur J Biochem. 1978 Dec;92(2):613–619. doi: 10.1111/j.1432-1033.1978.tb12784.x. [DOI] [PubMed] [Google Scholar]
  3. Contreras A., Vázquez D. Cooperative and antagonistic interactions of peptidyl-tRNA and antibiotics with bacterial ribosomes. Eur J Biochem. 1977 Apr 15;74(3):539–547. doi: 10.1111/j.1432-1033.1977.tb11422.x. [DOI] [PubMed] [Google Scholar]
  4. Englander S. W., Downer N. W., Teitelbaum H. Hydrogen exchange. Annu Rev Biochem. 1972;41:903–924. doi: 10.1146/annurev.bi.41.070172.004351. [DOI] [PubMed] [Google Scholar]
  5. Englander S. W., Englander J. J. Hydrogen-tritium exchange. Methods Enzymol. 1972;26:406–413. doi: 10.1016/s0076-6879(72)26021-9. [DOI] [PubMed] [Google Scholar]
  6. Englander S. W. Measurement of structural and free energy changes in hemoglobin by hydrogen exchange methods. Ann N Y Acad Sci. 1975 Apr 15;244:10–27. doi: 10.1111/j.1749-6632.1975.tb41518.x. [DOI] [PubMed] [Google Scholar]
  7. Ginzburg I., Zamir A. Characterization of different conformational forms of 30 S ribosomal subunits in isolated and associated states: possible correlations between structure and function. J Mol Biol. 1975 Apr 25;93(4):465–476. doi: 10.1016/0022-2836(75)90240-5. [DOI] [PubMed] [Google Scholar]
  8. Hui Bon Hoa G., Graffe M., Grunberg-Manago M. Thermodynamic studies of the reversible association of Escherichia coli ribosomal subunits. Biochemistry. 1977 Jun 14;16(12):2800–2805. doi: 10.1021/bi00631a034. [DOI] [PubMed] [Google Scholar]
  9. Kang C., Wells B., Cantor C. R. A fluorescent derivative of ribosomal protein S18 which permits direct observation of messenger RNA binding. J Biol Chem. 1979 Jul 25;254(14):6667–6672. [PubMed] [Google Scholar]
  10. Kurland C. G. Structure and function of the bacterial ribosome. Annu Rev Biochem. 1972;41(10):377–408. doi: 10.1146/annurev.bi.41.070172.002113. [DOI] [PubMed] [Google Scholar]
  11. Mandal C., Kallenbach N. R., Englander S. W. Base-pair opening and closing reactions in the double helix. A stopped-flow hydrogen exchange study in poly(rA).poly(rU). J Mol Biol. 1979 Dec 5;135(2):391–411. doi: 10.1016/0022-2836(79)90443-1. [DOI] [PubMed] [Google Scholar]
  12. Nabedryk-Viala E., Thiéry C., Calvet P., Fermandjian S. Hydrogen-deuterium exchange of angiotensin II in trifluoroethanol. FEBS Lett. 1975 Oct 15;58(1):273–276. doi: 10.1016/0014-5793(75)80277-8. [DOI] [PubMed] [Google Scholar]
  13. Nabedryk-Viala E., Thiéry C., Calvet P., Thiéry J. M. Hydrogen-isotope exchange of oxidized and reduced cytochrome c. A comparison of mass spectrometry and infrared methods. Eur J Biochem. 1976 Jan 2;61(1):253–258. doi: 10.1111/j.1432-1033.1976.tb10018.x. [DOI] [PubMed] [Google Scholar]
  14. Rosa J. J., Richards F. M. An experimental procedure for increasing the structural resolution of chemical hydrogen-exchange measurements on proteins: application to ribonuclease S peptide. J Mol Biol. 1979 Sep 25;133(3):399–416. doi: 10.1016/0022-2836(79)90400-5. [DOI] [PubMed] [Google Scholar]
  15. Springer M., Dondon J., Graffe M., Grunberg-Manago M., Lelong J. C., Gros F. Role of translation factors in the interaction between aminoacyl tRNAs and their ribosomal decoding sites. Biochimie. 1971;53(10):1047–1057. doi: 10.1016/s0300-9084(71)80192-x. [DOI] [PubMed] [Google Scholar]
  16. Teitelbaum H., Englander S. W. Open states in native polynucleotides. I. Hydrogen-exchange study of adenine-containing double helices. J Mol Biol. 1975 Feb 15;92(1):55–78. doi: 10.1016/0022-2836(75)90091-1. [DOI] [PubMed] [Google Scholar]
  17. Teitelbaum H., Englander S. W. Open states in native polynucleotides. II. Hydrogen-exchange study of cytosine-containing double helices. J Mol Biol. 1975 Feb 15;92(1):79–92. doi: 10.1016/0022-2836(75)90092-3. [DOI] [PubMed] [Google Scholar]
  18. Wishnia A., Boussert A., Graffe M., Dessen P. H., Grunberg-Manago M. Kinetics of the reversible association of ribosomal subunits: stopped-flow studies of the rate law and of the effect of Mg2+. J Mol Biol. 1975 Apr 25;93(4):499–415. doi: 10.1016/0022-2836(75)90242-9. [DOI] [PubMed] [Google Scholar]
  19. Zamir A., Miskin R., Elson D. Inactivation and reactivation of ribosomal subunits: amino acyl-transfer RNA binding activity of the 30 s subunit of Escherichia coli. J Mol Biol. 1971 Sep 14;60(2):347–364. doi: 10.1016/0022-2836(71)90299-3. [DOI] [PubMed] [Google Scholar]

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

RESOURCES