Cold shock induces a major ribosomal-associated protein that unwinds double-stranded RNA in Escherichia coli
| Autor: | Pamela G. Jones, Young Ho Kim, Weining Jiang, Masanori Mitta, Masayori Inouye |
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| Rok vydání: | 1996 |
| Předmět: |
Molecular Sequence Data
RNA-binding protein Biology medicine.disease_cause Ribosome DEAD-box RNA Helicases Bacterial Proteins Escherichia coli medicine Protein biosynthesis Electrophoresis Gel Two-Dimensional HSP70 Heat-Shock Proteins Amino Acid Sequence Derepression RNA Double-Stranded Messenger RNA Multidisciplinary Escherichia coli Proteins RNA-Binding Proteins RNA Chaperonin 60 Gene Expression Regulation Bacterial Ribosomal RNA Molecular biology Cold Temperature Mutagenesis Insertional RNA Bacterial Nucleic Acid Conformation Ribosomes RNA Helicases Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 93:76-80 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | A 70-kDa protein was specifically induced in Escherichia coli when the culture temperature was shifted from 37 to 15 degrees C. The protein was identified to be the product of the deaD gene (reassigned csdA) encoding a DEAD-box protein. Furthermore, after the shift from 37 to 15 degrees C, CsdA was exclusively localized in the ribosomal fraction and became a major ribosomal-associated protein in cells grown at 15 degrees C. The csdA deletion significantly impaired cell growth and the synthesis of a number of proteins, specifically the derepression of heat-shock proteins, at low temperature. Purified CsdA was found to unwind double-stranded RNA in the absence of ATP. Therefore, the requirement for CsdA in derepression of heat-shock protein synthesis is a cold shock-induced function possibly mediated by destabilization of secondary structures previously identified in the rpoH mRNA. |
| Databáze: | OpenAIRE |
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