Purification and characterization of two ribosomal proteins of Saccharomyces cerevisiae

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Abstract
Two non‐acidic proteins, extracted from the ribosomes of Saccharomyces cerevisiae using 1 M ammonium chloride in the presence of 50% ethanol, have been purified and characterized. Similar proteins are present in other eukaryotic ribosomes tested, as determined by two‐dimensional gel electrophoresis and cross‐reaction with antisera. One of the two yeast proteins, protein YL23, seems to be very well preserved during evolution, since antisera specific for YL23 cross‐react with protein EC L11 from Escherichia coli. The structural similarity between these two proteins parallels a functional equivalence shown by the ability of the bacterial protein to reconstitute the activity of protein‐deficient core particles from yeast. However, in contrast to protein EC L11, protein YL23 interacts with the yeast acidic proteins, forming a complex probably similar to the one made by bacterial protein EC L10 with proteins EC L7 and EC L12 in the E. coli ribosome. Protein YL23 might play similar roles to those of proteins EC L10 and EC L11 in bacteria.