The Mechanism of Subunit Interaction as a Key to the Understanding of Ribosome Function

  • Hans Noll
  • Markus Noll
  • Bern Hapke
  • Gerbrand van Dieijen
Part of the Colloquium der Gesellschaft für Biologische Chemie 26.–28. April 1973 in Mosbach/Baden book series (MOSBACH, volume 24)


The most intriguing feature of the ribosome is its highly asymmetrical construction of two unequal subunits that, in the case of prokaryotic organisms, are described by their 30 S and 50 S sedimentation values. Although the pioneering work of Tissières and Watson [1] established that Mg2+ ions were essential to maintain the associated state and hinted at the existence of a dynamic equilibrium, a rather static view of ribosome structure dominated the thinking for nearly a decade. Perhaps consonant with the prevailing mores of the time, it was taken for granted that the union between the two subunits was a marriage for life. This vision seemed to satisfy an inner need, for how else could it be explained that the scientists would suppress their natural curiosity and refrain from a closer scrutiny of the relationship between the subunits ? However, the less reverent and more open climate of the sexual revolution and women’s lib was not going to bypass the ribosome, and soon representatives of the younger generation [2] boldly proclaimed that ribosomes not engaged in protein synthesis normally existed as free subunits that would enter a temporary union only for the purpose of creating a new polypeptide chain. Although this radical view subsequently turned out to be untenable, by removing an old taboo it led to fresh experiments and marked the beginning of a more dynamic view of the ribosome.


Initiation Factor Sucrose Gradient Sedimentation Pattern Tight Couple Initiation Complex 
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Copyright information

© Springer-Verlag Berlin · Heidelberg 1973

Authors and Affiliations

  • Hans Noll
    • 1
  • Markus Noll
    • 1
  • Bern Hapke
    • 1
  • Gerbrand van Dieijen
    • 1
  1. 1.Department of Biological SciencesNorthwestern UniversityEvanstonUSA

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