Protein phosphorylation in response to stress in Clostridium acetobutylicum.
The possible involvement of protein phosphorylation in the clostridial stress response was investigated by radioactively labeling growing cells of Clostridium acetobutylicum with 32Pi or cell extracts with [gamma-32P]ATP. Several phosphoproteins were identified; these were not affected by the growth stage of the culture. Although the extent of protein phosphorylation was increased by heat stress, the phosphoproteins did not correspond to known stress proteins seen in one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Purified clostridial DnaK, a stress protein, acted as a kinase catalyzing the phosphorylation of a 50-kilodalton protein. The phosphorylation of this protein was enhanced in extracts prepared from heat-stressed cells. Diadenosine-5',5"'-P1,P4-tetraphosphate had no influence on protein phosphorylation.
Balodimos
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Department of Microbiology, Boston University School of Medicine, Massachusetts 02118.
Rapaport
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Kashket
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D020001:1-Butanol; D001426:Bacterial Proteins / Q000378:metabolism*; D000440:Butanols / Q000494:pharmacology; D003013:Clostridium / Q000187:drug effects / Q000378:metabolism*; D015226:Dinucleoside Phosphates / Q000494:pharmacology; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006358:Hot Temperature; D010766:Phosphorylation
D001426:Bacterial Proteins; D000440:Butanols; D015226:Dinucleoside Phosphates; D029968:Escherichia coli Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; C020733:diadenosine tetraphosphate; D020001:1-Butanol; C063842:dnaK protein, E coli