Open AccessPhosphorylation of the major heat shock protein of Dictyostelium discoideum.
Author(s) -
William F. Loomis,
Susan F. Wheeler,
J Schmidt
Publication year - 1982
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.2.5.484
Subject(s) - dictyostelium discoideum , phosphorylation , biology , heat shock protein , threonine , mycetozoa , methionine , biochemistry , shock (circulatory) , phosphate , microbiology and biotechnology , serine , amino acid , medicine , gene
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.