Ribosomes as Sensors of Heat and Cold Shock in Escherichia coli

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 87; no. 15; pp. 5589 - 5593
• Main Authors: VanBogelen, Ruth A., Neidhardt, Frederick C.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 01-08-1990; National Acad Sciences
• Subjects: Anti-Bacterial Agents - pharmacology; Antibiotics; Biological and medical sciences; Cell structures and functions; Cold shock response; Cold Temperature; Electrophoresis, Gel, Two-Dimensional; Escherichia coli - drug effects; Escherichia coli - growth & development; Escherichia coli - metabolism; Fundamental and applied biological sciences. Psychology; Gels; Heat; Heat shock response; Heat-Shock Proteins - biosynthesis; Heat-Shock Proteins - isolation & purification; Hot Temperature; Inductive reasoning; Models, Biological; Molecular and cellular biology; Mops; Ribosome; Ribosomes; Ribosomes - metabolism; Sensors; Shock heating; Tetracycline - pharmacology; Antibiotic; Temperature; Ribosome; Escherichia coli; Guanine derivatives; Heat shock protein; Bacteria; Two dimensional electrophoresis; Enterobacteriaceae
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.87.15.5589

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.