ISSN:
1432-0983
Keywords:
Yeast
;
Ribosome synthesis
;
Regulation
;
Ribosomal protein turnover
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00405095
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