Ribosomes as sensors of heat and cold shock in Escherichia coli
Autor: | Ruth A. Vanbogelen, Frederick C. Neidhardt |
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Rok vydání: | 1990 |
Předmět: |
Hot Temperature
Cell medicine.disease_cause Models Biological Ribosome Heat shock protein Escherichia coli medicine Electrophoresis Gel Two-Dimensional Heat-Shock Proteins Multidisciplinary biology Tetracycline Cold-shock domain biology.organism_classification Anti-Bacterial Agents Cold shock response Cell biology Cold Temperature medicine.anatomical_structure Biochemistry Shock (circulatory) medicine.symptom Ribosomes Bacteria Research Article |
Zdroj: | Proceedings of the National Academy of Sciences. 87:5589-5593 |
ISSN: | 1091-6490 0027-8424 |
DOI: | 10.1073/pnas.87.15.5589 |
Popis: | Nearly all cells respond to an increase in temperature by inducing a set of proteins, called heat shock proteins (HSPs). Because a large number of other stress conditions induce the HSPs (or at least the most abundant ones), this response is often termed the universal stress response. However, a careful study of conditions that truly mimic a temperature shift suggested that these proteins are induced in response to a change in the translational capacity of the cell. To test this directly, Escherichia coli cells were treated with antibiotics that target the prokaryotic ribosome. Two-dimensional gels were used to evaluate the ability of these drugs to alter the rate of synthesis of the HSPs. One group of antibiotics induced the HSPs, whereas a second group repressed the HSPs and induced another set of proteins normally induced in response to a cold shock. Depending on the concentration used, the induction of the heat or cold shock proteins mimicked a mild or severe temperature shift. In addition, antibiotics of the cold shock-inducing group were found to block high temperature induction of the HSPs. The results implicate the ribosome as a prokaryotic sensor for the heat and cold shock response networks, a role it may serve in eukaryotes as well. |
Databáze: | OpenAIRE |
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