Yeast ribosomal proteins: VII. Cytoplasmic ribosomal proteins from Schizosaccharomyces pombe
β Scribed by Otaka, Eiko ;Higo, Ken-ichi ;Itoh, Takuzi
- Book ID
- 104770503
- Publisher
- Springer
- Year
- 1983
- Tongue
- English
- Weight
- 607 KB
- Volume
- 191
- Category
- Article
- ISSN
- 0026-8925
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β¦ Synopsis
The cytoplasmic ribosomal proteins from a fission yeast Schizosaccharomyces pombe were analysed by two-dimensional polyacrylamide gel electrophoresis. Seventy-three protein species were identified in the 80S ribosome, and named SP-S1 to SP-S33 and SP-L1 to SP-L40 in the small and large subunits, respectively. Many of these proteins could be correlated to those of Saccharomyces cerevisiae on the basis of their electrophoretic mobilities. Eleven proteins were isolated from the 80S ribosome, and their amino acid compositions were determined. Of these, SP-S6, SP-L1, SP-L12, SP-L15, SP-L17, SP-L27, SP-L36 and SP-L40c and d were sequenced from their amino-termini. SP-S28 and SP-L2 appear to have their amino-termini blocked. These results were compared with the data available for the S. cerevisiae and rat liver ribosomal proteins. The S. cerevisiae counterparts of the eight proteins mentioned above were found to be YS4, YL1, YL10, YL14, YL35, YL40 and YL44c and d, respectively. The rat liver counterparts of SP-S6, SP-L1, SP-L27 and SP-L40c and d were the rat S6, L4, L37 and P2, respectively. Comparison of the partial sequences of these ribosomal proteins suggests that these two yeasts are relatively far apart, phylogenetically.
π SIMILAR VOLUMES
The 80S ribosome of Schizosaccharomyces pombe contains 93 proteins as determined by twodimensional electrophoresis on polyacrylamide gels. Of these, 76 are basic and 17 are acidic at pH 8.7. 38 proteins could be assigned unambiguously to the large sub-unit and 19 to the small. 67 proteins were extra
Proteins of yeast cytoplasmic ribosomes were analyzed by two different methods of two dimensional gel electrophoresis: run at pH 8.6 in 1-D1 and at pH 4.6 in 2-D (Method A); run at pH 5.0 in 1-D and in the presence of sodium dodecyl sulfate in 2-D (Method B). The numbers of proteins estimated were 2