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. 1971 Aug;68(8):1780–1785. doi: 10.1073/pnas.68.8.1780

Pressure-Induced Dissociation of Sedimenting Ribosomes: Effect on Sedimentation Patterns

Anthony A Infante 1, Ralph Baierlein 1
PMCID: PMC389292  PMID: 5288765

Abstract

Anomalous sedimentation patterns arise when free ribosomes from sea urchin eggs are centrifuged at high speeds. Pressure-induced dissociation of the ribosomes during sedimentation can explain the peculiar behavior; the assumption of such dissociation also yields estimates of the equilibrium constant (as a function of KCl concentration) and the change in molecular volume (500 ± 100 ml/mol) in the reaction: subunits ⇄ ribosome. Such dissociation during centrifugation may explain many experiments in which apparent reduced sedimentation coefficients for ribosomes, and increased coefficients for the subunits, have been ascribed to conformational changes.

Keywords: ultracentrifuge, sea urchin, Strongylocentrotus, ribosomal conformation

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Selected References

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

  1. BRAKKE M. K. NONIDEAL SEDIMENTATION AND THE CAPACITY OF SUCROSE GRADIENT COLUMNS FOR VIRUS IN DENSITY-GRADIENT CENTRIFUGATION. Arch Biochem Biophys. 1964 Sep;107:388–403. doi: 10.1016/0003-9861(64)90295-4. [DOI] [PubMed] [Google Scholar]
  2. Ceccarini C., Campo M. S., Andronico F. Biosynthesis and distribution of ribosomal particles in the cellular slime mould, Dictyostelium purpureum. J Mol Biol. 1970 Nov 28;54(1):33–44. doi: 10.1016/0022-2836(70)90444-4. [DOI] [PubMed] [Google Scholar]
  3. Falvey A. K., Staehelin T. Structure and function of mammalian ribosomes. II. Exchange of ribosomal subunits at various stages of in vitro polypeptide synthesis. J Mol Biol. 1970 Oct 14;53(1):21–34. doi: 10.1016/0022-2836(70)90043-4. [DOI] [PubMed] [Google Scholar]
  4. Infante A. A., Graves P. N. Stability of free ribosomes, derived ribosomes and polysomes of the sea urchin. Biochim Biophys Acta. 1971 Aug 12;246(1):100–110. doi: 10.1016/0005-2787(71)90075-x. [DOI] [PubMed] [Google Scholar]
  5. Infante A. A., Krauss M. Dissociation of ribosomes induced by centrifugation: evidence for doubting conformational changes in ribosomes. Biochim Biophys Acta. 1971 Aug 12;246(1):81–99. [PubMed] [Google Scholar]
  6. Infante A. A., Nemer M. Heterogeneous ribonucleoprotein particles in the cytoplasm of sea urchin embryos. J Mol Biol. 1968 Mar 28;32(3):543–565. doi: 10.1016/0022-2836(68)90342-2. [DOI] [PubMed] [Google Scholar]
  7. Josephs R., Harrington W. F. An unusual pressure dependence for a reversibly associating protein system; sedimentation studies on myosin. Proc Natl Acad Sci U S A. 1967 Oct;58(4):1587–1594. doi: 10.1073/pnas.58.4.1587. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Josephs R., Harrington W. F. On the stability of myosin filaments. Biochemistry. 1968 Aug;7(8):2834–2847. doi: 10.1021/bi00848a020. [DOI] [PubMed] [Google Scholar]
  9. Kaempfer R. Dissociation of ribosomes on polypeptide chain termination and origin of single ribosomes. Nature. 1970 Nov 7;228(5271):534–537. doi: 10.1038/228534a0. [DOI] [PubMed] [Google Scholar]
  10. Kegeles G., Rhodes L., Bethune J. L. Sedimentation behavior of chemically reacting systems. Proc Natl Acad Sci U S A. 1967 Jul;58(1):45–51. doi: 10.1073/pnas.58.1.45. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Martin T. E., Rolleston F. S., Low R. B., Wool I. G. Dissociation and reassociation of skeletal muscle ribosomes. J Mol Biol. 1969 Jul 14;43(1):135–149. doi: 10.1016/0022-2836(69)90084-9. [DOI] [PubMed] [Google Scholar]
  12. Morimoto T. Intermediate stage in the association and dissociation of Escherichia coli ribosomes and the combining properties of their subunits. Biochim Biophys Acta. 1969 May 20;182(1):135–146. doi: 10.1016/0005-2787(69)90528-0. [DOI] [PubMed] [Google Scholar]
  13. Reisner A. H., Rowe J., Macindoe H. M. Structural studies on the ribosomes of Paramecium: evidence for a "primitive" animal ribosome. J Mol Biol. 1968 Mar 28;32(3):587–610. doi: 10.1016/0022-2836(68)90345-8. [DOI] [PubMed] [Google Scholar]
  14. Ron E. Z., Kohler R. E., Davis B. D. Magnesium ion dependence of free and polysomal ribosomes from Escherichia coli. J Mol Biol. 1968 Aug 28;36(1):83–89. doi: 10.1016/0022-2836(68)90221-0. [DOI] [PubMed] [Google Scholar]
  15. Schreier M. H., Noll H. Chain initiation in primitive protein synthesis: a 60S intermediate in the formation of active 70S ribosomes. Nature. 1970 Jul 11;227(5254):128–133. doi: 10.1038/227128a0. [DOI] [PubMed] [Google Scholar]
  16. Schreier M. H., Noll H. Conformational changes in ribosomes during protein synthesis. Proc Natl Acad Sci U S A. 1971 Apr;68(4):805–809. doi: 10.1073/pnas.68.4.805. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Subramanian A. R., Ron E. Z., Davis B. D. A factor required for ribosome dissociation in Escherichia coli. Proc Natl Acad Sci U S A. 1968 Oct;61(2):761–767. doi: 10.1073/pnas.61.2.761. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Suzuka I. Effect of ethylendiaminetetraacetate on Escherichia coli B ribosomes--binding of phenylalanyl sRNA to 50S particles converted from 70S ribosomes. Biochem Biophys Res Commun. 1967 Dec 15;29(5):667–673. doi: 10.1016/0006-291x(67)90268-9. [DOI] [PubMed] [Google Scholar]
  19. TASHIRO Y., SIEKEVITZ P. ULTRACENTRIFUGAL STUDIES ON THE DISSOCIATION OF HEPATIC RIBOSOMES. J Mol Biol. 1965 Feb;11:149–165. doi: 10.1016/s0022-2836(65)80047-x. [DOI] [PubMed] [Google Scholar]
  20. Teneyck L. F., Kauzmann W. Pressure and hydration effects on chemically reacting systems in the ultracentrifuge. Proc Natl Acad Sci U S A. 1967 Sep;58(3):888–894. doi: 10.1073/pnas.58.3.888. [DOI] [PMC free article] [PubMed] [Google Scholar]

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