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. 1982 May;2(5):484–489. doi: 10.1128/mcb.2.5.484

Phosphorylation of the major heat shock protein of Dictyostelium discoideum.

W F Loomis, S Wheeler, J A Schmidt
PMCID: PMC369817  PMID: 6810097

Abstract

The major heat shock protein, hsp 70, of Dictyostelium discoideum was found to be rapidly phosphorylated. Analysis of [35S]methionine- and 32Pi-labeled hsp 70 revealed that two similar but distinct proteins of about 70,000 daltons each are synthesized at a high rate after a heat shock, and that each has a phosphorylated member. The phosphorylation chiefly modifies threonine residues. Rapid turnover of the phosphate group occurs, resulting in a steady-state condition in which only about half of the hsp 70 is phosphorylated at a given time.

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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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