AppppA binds to several proteins in Escherichia coli, including the heat shock and oxidative stress proteins DnaK, GroEL, E89, C45 and C40
| Autor: | D B Johnstone, S B Farr |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
Photochemistry
Mutant Catabolite repression medicine.disease_cause Second Messenger Systems General Biochemistry Genetics and Molecular Biology Bacterial Proteins Heat shock protein Escherichia coli medicine Electrophoresis Gel Two-Dimensional Phosphorylation Molecular Biology Chromatography High Pressure Liquid Heat-Shock Proteins Mutation General Immunology and Microbiology biology General Neuroscience Affinity Labels biology.organism_classification Enterobacteriaceae GroEL Biochemistry Autoradiography Electrophoresis Polyacrylamide Gel Chromatography Thin Layer Oxidation-Reduction Dinucleoside Phosphates Oxidative stress Research Article Plasmids |
| Zdroj: | The EMBO Journal. 10:3897-3904 |
| ISSN: | 0261-4189 |
| DOI: | 10.1002/j.1460-2075.1991.tb04959.x |
| Popis: | The dinucleotide AppppA (5',5'''-P1, P4-diadenosine tetraphosphate) is rapidly synthesized in cells exposed to heat stress or oxidative stress. Stress-induced AppppA accumulation has been observed in all cell types studied to date. In order to study the function(s) of AppppA, we created a mutation in the Escherichia coli gene that encodes the sole AppppN hydrolase (apaH). High levels of AppppA have subsequently been shown to affect many cellular processes, including expression of catabolite repressible genes and the ability to survive starvation, oxidative stress and near-UV irradiation. Nevertheless, the precise role of AppppA remains undefined. In order to better understand the mechanism by which AppppA exerts its effects, we attempted to determine which proteins bind to AppppA by synthesizing (alpha'-32P) 8-N3AppppA for use in photocrosslinking experiments with extract derived from cells with different genetic backgrounds and exposed to various stress conditions. We report here that several E. coli proteins bind AppppA, including the heat shock and oxidative stress proteins DnaK, GroEL, E89, C45 and C40. In addition, we show that apaH mutants, which have high basal levels of AppppA, are hypersensitive to killing by heat. |
| Databáze: | OpenAIRE |
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