The Bifunctional Nature of Ribosomal Proteins and Speculations on Their Origins
We undertook some years ago to isolate, to characterize, and to determine the structure of eukaryotic (rat) ribosomal proteins and nucleic acids (Wool, 1979). We chose rat ribosomes for reasons that are buried in the history of our research. What was it that led us to this undertaking which was not infrequently derided as an arduous, tedious, time consuming chore lacking excitement or intellectual challenge, indeed, as lacking importance? We made a commitment to the protein and nucleic acid chemistry because of an abiding belief that it was essential for a solution of the structure of the organelle; the structure in turn was needed for a coherent molecular account of the function of ribosomes in protein synthesis. Almost everyone agreed that this last was an enterprise that was to be taken seriously - that it was a formidable intellectual challenge, that it was of great importance, and that it did not lack for excitement. Moreover, no matter how pretentious it sounds, we felt we would be making a contribution to a compilation of data (the primary structure of the seventy to eighty proteins) that could be viewed as a general resource. It is perhaps even more pretentious to say that this prediction has been amply substantiated, that the sequences have been useful to many, including scientists whose research did not touch directly on ribosomes or protein synthesis. From the beginning we suspected that the sequences of amino acids in the proteins might also help in understanding the origins and the evolution of the ribosomal proteins, in unraveling the functions of the proteins, in defining the rules that govern the interaction of the proteins with the rRNAs, and in uncovering the amino acid sequences that direct the proteins to the nucleolus for assembly on nascent rRNA.
KeywordsZinc Tyrosine Glutathione Aldehyde Carboxyl
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