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

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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.

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Abbreviations

rRNA:

ribosomal RNA

r-protein:

ribosomal protein

pre-mRNA:

precursor mRNA

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Authors and Affiliations

  1. Biochemisch Laboratorium, Vrije Universiteit, de Boelelaan 1083, NL-1081 HV, Amsterdam, The Netherlands

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

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  1. Tarek T. A. L. ElBaradi
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  2. Carine A. F. M. van der Sande
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  3. Willem H. Mager
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  4. Hendrik A. Raué
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  5. Rudi J. Planta
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ElBaradi, T.T.A.L., van der Sande, C.A.F.M., Mager, W.H. et al. The cellular level of yeast ribosomal protein L25 is controlled principally by rapid degradation of excess protein. Curr Genet 10, 733–739 (1986). https://doi.org/10.1007/BF00405095

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  • DOI: https://doi.org/10.1007/BF00405095

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