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Evolutionary Conservation of Reactions in Translation

C. H. Best Institute, Banting and Best Department of Medical Research, University of Toronto, Toronto, Ontario, Canada M5G 1L6

Current X-ray diffraction and cryoelectron microscopic data of ribosomes of eubacteria have shed considerable light on the molecular mechanisms of translation. Structural studies of the protein factors that activate ribosomes also point to many common features in the primary sequence and tertiary structure of these proteins. The reconstitution of the complex apparatus of translation has also revealed new information important to the mechanisms. Surprisingly, the latter approach has uncovered a number of proteins whose sequence and/or structure and function are conserved in all cells, indicating that the mechanisms are indeed conserved. The possible mechanisms of a new initiation factor and two elongation factors are discussed in this context.

This work is dedicated to the memory of Clelia H. Finney.

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