{'fraction_non_alphanumeric': 0.02254428341384863, 'fraction_numerical': 0.024154589371980676, 'mean_word_length': 5.038834951456311, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
Phosphorylation of the major heat shock protein of Dictyostelium discoideum

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.