Protein phosphorylation in response to stress in Clostridium acetobutylicum
| Autor: | Eliezer Rapaport, I A Balodimos, Eva R. Kashket |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1990 |
| Předmět: |
Clostridium acetobutylicum
Hot Temperature Butanols macromolecular substances Applied Microbiology and Biotechnology Clostridium 1-Butanol Bacterial Proteins Heat shock protein Protein phosphorylation Nucleotide HSP70 Heat-Shock Proteins Phosphorylation Heat-Shock Proteins Gel electrophoresis chemistry.chemical_classification Ecology biology Chemistry Escherichia coli Proteins biology.organism_classification Phosphorus-32 Biochemistry bacteria Dinucleoside Phosphates Food Science Biotechnology Research Article |
| Popis: | The possible involvement of protein phosphorylation in the clostridial stress response was investigated by radioactively labeling growing cells of Clostridium acetobutylicum with {sup 32}P{sub i} or cell extracts with ({gamma}-{sup 32}P)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{prime},5{double prime}{prime}-P{sup 1},P{sup 4}-tetraphosphate had no influence on protein phosphorylation. |
| Databáze: | OpenAIRE |
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