Abstract
Seventeen ribosomal proteins of Saccharomyces cerevisiae were isolated from small ribosomal subunits and disodium ethylenediaminetetraacetate treated 80S ribosomes by chromatography on a column of carboxymethylcellulose and/or by filtration through Sephacryl S-200. The isolated proteins are YS4, YS7, YS8, YS9, YS10, YS12, YS14, YS18, YS23, YS29, YL11, YL13, YL16, YL17, YL22, YL38, and YL40 [nomenclature according to Otaka & Osawa (1981) [Otaka, E., & Osawa, S. (1981) Mol. Gen. Genet. 181, 176-182]]. The purification procedures and the amino acid compositions of these proteins are presented. Amino-terminal amino acid sequences of YS4, YS6, YS11, YS15, YS16, YS22, YL10, and YL31 have been determined and compared with those from rat liver [Wittmann-Liebold, B., Geissler, A. W., Lin, A., & Wool, I. G. (1979) J. Supramol. Struct. 12, 425-433] and Halobacterium cutirubrum [Matheson, A. T., Möller, W., Amons, R., & Yaguchi, M. (1980) in Ribosomes: Structure, Function and Genetics (Chambliss, G., et al., Eds.) pp 297-332, University Park Press, Baltimore, MD; M. Yaguchi, unpublished experiments].