PMID:8995247
| Citation |
Jiang, W, Hou, Y and Inouye, M (1997) CspA, the major cold-shock protein of Escherichia coli, is an RNA chaperone. J. Biol. Chem. 272:196-202 |
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| Abstract |
CspA, the major cold-shock protein of Escherichia coli, is dramatically induced during the cold-shock response. The amino acid sequence of CspA shows 43% identity to the "cold-shock domain" of the eukaryotic Y-box protein family, which interacts with RNA and DNA to regulate their functions. Here, we demonstrate that CspA binds to RNA as a chaperone. First, CspA cooperatively binds to heat-denatured single-stranded RNA if it is larger than 74 bases, causing a supershift in gel electrophoresis. A minimal concentration of CspA at 2.7 x 10(-5) M is absolutely required for this cooperative binding, which is sufficiently lower than the estimated cellular concentration of CspA (10(-4) M) in cold-shocked cells. No specific RNA sequences for CspA binding were identified, indicating that it has a broad sequence specificity for its binding. When the 142-base 5'-untranslated region of the cspA mRNA was used as a substrate for ribonucleases A and T1, the addition of CspA significantly stimulated RNA hydrolysis by preventing the formation of RNase-resistant bands due to stable secondary structures in the 5'-untranslated region. These results indicate that binding of CspA to RNA destabilizes RNA secondary structures to make them susceptible to ribonucleases. We propose that CspA functions as an RNA chaperone to prevent the formation of secondary structures in RNA molecules at low temperature. Such a function may be crucial for efficient translation of mRNAs at low temperatures and may also have an effect on transcription. |
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| Keywords |
Bacterial Proteins/physiology; Base Sequence; Cold Temperature; DNA, Single-Stranded/metabolism; Escherichia coli/chemistry; Hot Temperature; Molecular Chaperones; Molecular Sequence Data; Nucleic Acid Conformation; Nucleic Acid Denaturation; RNA, Double-Stranded/metabolism; RNA-Binding Proteins/physiology |
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Significance
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The results in Fig. 7 demonstrate that CspA binding to the 5'UTR of cspA mRNA increases sensitivity to single-strand specific RNases A and T1. CspA is proposed to be an RNA chaperone that prevents the formation of RNA secondary structures at low temperature.
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