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. 1982 Mar;79(6):1781–1785. doi: 10.1073/pnas.79.6.1781

Heat shock induces rapid dephosphorylation of a ribosomal protein in Drosophila.

C V Glover
PMCID: PMC346064  PMID: 6804946

Abstract

Ribosomes isolated from Drosophila melanogaster tissue culture cells labeled in vivo with 32Pi contain a single, heavily phosphorylated, ribosomal protein. As much as 40% of this protein is phosphorylated in cells cultured at 25 degrees C. The molecular weight and other characteristics of this protein suggest possible homology with ribosomal protein S6. Following a shift-up to 37 degrees C, the protein is specifically and quantitatively dephosphorylated. The kinetics of this dephosphorylation are rapid with a half-time on the order of a few minutes. These kinetics closely parallel the heat shock-induced breakdown of the preexisting polysome population.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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