Current Genetics

, Volume 10, Issue 10, pp 733–739

The cellular level of yeast ribosomal protein L25 is controlled principally by rapid degradation of excess protein

  • Tarek T. A. L. ElBaradi
  • Carine A. F. M. van der Sande
  • Willem H. Mager
  • Hendrik A. Raué
  • Rudi J. Planta
Original Articles

DOI: 10.1007/BF00405095

Cite this article as:
ElBaradi, T.T.A.L., van der Sande, C.A.F.M., Mager, W.H. et al. Curr Genet (1986) 10: 733. doi:10.1007/BF00405095

Summary

When the gene dosage for the primary rRNA-binding ribosomal protein L25 in yeast cells was raised about 50-fold, the level of mature L25 transcripts was found to increase almost proportionally. The plasmid-derived L25 transcripts were structurally indistinguishable from their genomic counterparts, freely entered polysomes in vivo and were fully translatable in a heterologous in vitro system. Nevertheless, pulse-labelling for periods varying from 3–20 min did not reveal a significant elevation of the intracellular level of L25 protein. When pulse-times were decreased to 10–45 s, however, we did detect a substantial over production of L25. We conclude that, despite the strong RNA-binding capacity of the protein, accumulation of L25 is not controlled by an autogenous (pre-)mRNA-targeted mechanism similar to that operating in bacteria, but rather by extremely rapid degradation of excess protein produced.

Key words

YeastRibosome synthesisRegulationRibosomal protein turnover

Abbreviations

rRNA

ribosomal RNA

r-protein

ribosomal protein

pre-mRNA

precursor mRNA

Copyright information

© Springer-Verlag 1986

Authors and Affiliations

  • Tarek T. A. L. ElBaradi
    • 1
  • Carine A. F. M. van der Sande
    • 1
  • Willem H. Mager
    • 1
  • Hendrik A. Raué
    • 1
  • Rudi J. Planta
    • 1
  1. 1.Biochemisch LaboratoriumVrije UniversiteitAmsterdamThe Netherlands