Molecular and General Genetics MGG

, Volume 195, Issue 3, pp 544–546

Yeast ribosomal proteins

VIII. Isolation of two proteins and sequence characterization of twenty-four proteins from cytoplasmic ribosomes

Authors

  • Eiko Otaka
    • Department of Biochemistry and Biophysics, Research Institute for Nuclear Medicine and BiologyHiroshima University
  • Ken-ichi Higo
    • Department of Biochemistry and Biophysics, Research Institute for Nuclear Medicine and BiologyHiroshima University
  • Takuzi Itoh
    • Department of Biochemistry and Biophysics, Research Institute for Nuclear Medicine and BiologyHiroshima University
Short Communication

DOI: 10.1007/BF00341461

Cite this article as:
Otaka, E., Higo, K. & Itoh, T. Mol Gen Genet (1984) 195: 544. doi:10.1007/BF00341461

Summary

Two proteins, YL41 and YL43, were isolated from 80S ribosomes of Saccharomyces cerevisiae by filtration through a Sephacryl S-200 column and by chromatography on a column of carboxymethylcellulose. Their amino acid compositions are presented. Twenty-four proteins including these two proteins were subjected to sequence analyses by automated Edman degradation. Amino-terminal amino acid sequences were determined for 17 proteins, YS3, YS9, YS23, YS24, YS29, YL6, YL8, YL11, YL15, YL17, YL23, YL28, YL33, YL37, YL39, YL41, and YL43. YL41, which has a 72.7% lysine and arginine content, was found to be particular to eukaryotic ribosomes. The aminotermini of another seven proteins, YS2, YS5, YS8, YS12, YS13, YS20, and YS27, were suggested to be blocked.

Comparison of the amino-terminal sequences with all other ribosomal protein sequences so far available indicates that YS9 shows sequence homology to rat liver ribosomal protein S8 (Wittmann-Liebold et al. 1979).

Copyright information

© Springer-Verlag 1984