Current Genetics

, Volume 10, Issue 7, pp 537–544

Immunological homologies between ribosomal proteins amongst lower eukaryotes

  • Christian Kreutzfeldt
  • Thomas Neumann
  • Axel Dierig


Polyclonal antibodies were raised against the purified ribosomal proteins Ll and L2, the 5S rRNA binding protein L3, all from Saccharomyces cerevisiae, and against Ll and L2 from Schizosaccharomyces pombe (numbering according to Otaka and Osawa 1981; Otaka et al. 1983, respectively). For clarity prefixes Sc and Sp have been added to the numbering of proteins derived from S. cerevisiae and S. pombe, respectively. Ribosomal proteins from these yeasts and from Kluyveromyces marxianus, Rhodotorula glutinis, the slime mold Dictyostelium discoideum and the protozoan Tetrahymena thermophila were checked for antigenic cross-reactivity by the immunoblot technique. Anti-ScL1 bound to the largest ribosomal proteins of all organisms but not with equal strength. A fast migrating protein band from R. glutinis was also reactive. Anti-ScL2 reacted strongly with L2 or analogous proteins derived exclusively from the yeasts. Anti-ScL3 cross-reacted only with one protein band from K. marxianus, whereas anti-SpL1 cross-reacted with Ll or its analogues from the other organisms, but also with proteins of lower molecular weight. In S. cerevisiae, these proteins are located exclusively on the small ribosomal subunit. L2 or analogous ribosomal proteins of all organisms were recognized by anti-SpL2 but additionally the ribosomal protein YL28 of S. cerevisiue and fast migrating proteins of T. thermophila exhibited anti-SpL2 binding.

Key words

Ribosomal proteins Immunological homology Yeasts Immunoblot 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Adoutte-Panvier A, Davies JE, Gritz LR, Littlewood BS (1980) Mol Gen Genet 179:273–282Google Scholar
  2. Chooi WY, Otaka E (1984) Mol Cell Biol 4:2535–2539Google Scholar
  3. Coddington A (1977) Mol Gen Genet 158:93–100Google Scholar
  4. Erdmann VA (1981) Nucleic Acids Res 9:x25-x43Google Scholar
  5. Erdmann VA, Wolters J, Huysmans E, Vandenberghe A, deWachter R (1984) Nucleic Acids Res 12:x133-x166Google Scholar
  6. Fried HM, Warner JR (1981) Proc Natl Acad Sci USA 78:238–242Google Scholar
  7. Gerton GL, Wardrip NJ, Hedrick JL (1982) Anal Biochem 126:116–121Google Scholar
  8. Grant PG, Schinder D, Davies JE (1976) Genetics 63:667–673Google Scholar
  9. Hardy SJS, Kurland CG, Voynow P, Mora G (1969) Biochemistry 8:2897–2905Google Scholar
  10. Hawkes R, Niday E, Gordon J (1982) Anal Biochem 119:142–147Google Scholar
  11. Irrgang KD, Kreutzfeldt C, Lochmann ER (1985) Biol Chem Hoppe-Seyler 366:387–394Google Scholar
  12. Itch T, Higo K, Otaka E (1979) Biochemistry 18:5787–5793Google Scholar
  13. Komiya H, Miyazaki M, Takemura S (1981) J Biochem (Tokyo) 89:1663–1666Google Scholar
  14. Kristiansen K, Krüger A (1978) Biochim Biophys Acta 521:435–451Google Scholar
  15. Kristiansen K, Plessner P, Krüger A (1978) Eur J Biochem 83:395–403Google Scholar
  16. Laemmli UK (1970) Nature (London) 227:680–685Google Scholar
  17. Legocki RP, Verma DPS (1981) Anal Biochem 111:385–392Google Scholar
  18. LeGoff V, Perrot M, Begueret J (1984) Curr Genet 9:53–58Google Scholar
  19. Nazar RN, Yaguchi M, Willick GE, Rollin CF, Roy C (1979) Eur J Biochem 102:573–582Google Scholar
  20. Nazar RN, Yaguchi M, Willick GE (1982) Can J Biochem 60:490–496Google Scholar
  21. Otaka E, Osawa S (1981) Mol Gen Genet 181:176–182Google Scholar
  22. Otaka E, Higo K, Itch T (1983) Mol Gen Genet 191:519–524Google Scholar
  23. Ramagopal S, Ennis HL (1980) Eur J Biochem 105:245–258Google Scholar
  24. Schmid G, Böck A (1984) Syst Appl Microbiol 5:1–10Google Scholar
  25. Schmid G, Strobel 0, Stöffler-Meilicke M, Stöffler G, Böck A (1984) FEBS Left 177:189–194Google Scholar
  26. Schultz LD, Friesen JD (1983) J Bacteriol 155:8–14Google Scholar
  27. Towbin H, Staehelin T, Gordon J (1979) Proc Natl Acad Sci USA 76:4350–4354Google Scholar
  28. Van der Zeijst BAM, Bult H (1972) Eur J Biochem 28:463–474Google Scholar
  29. Wei C, Hansen BS, Vaughan MH, McLaughlin CS (1974) Proc Natl Acad Sci USA 71:713–717Google Scholar

Copyright information

© Springer-Verlag 1986

Authors and Affiliations

  • Christian Kreutzfeldt
    • 1
  • Thomas Neumann
    • 1
  • Axel Dierig
    • 1
  1. 1.Institut für Pharmakologie und ToxikologiePhilipps-Universität MarburgGermany

Personalised recommendations