Abstract
THE cold-shock response in both Escherichia coli and Bacillus subtilis is induced by an abrupt downshift in growth temperature. It leads to the increased production of the major cold-shock proteins, CS7.4 and CspB, respectively1–3. CS7.4 is a transcriptional activator of two genes4,5. CS7.4 and CspB share 43 per cent sequence identity with the nucleic acid-binding domain of the eukaryotic gene-regulatory Y-box factors6. This cold-shock domain is conserved from bacteria to man7 and contains the RNA-binding RNP1 sequence motif8. As a prototype of the cold-shock domain, the structure of CspB has been determined here from two crystal forms. In both, CspB is present as an antiparallel five-stranded β-barrel. Three consecutive β-strands, the central one containing the RNP1 motif, create a surface rich in aromatic and basic residues that are presumably involved in nucleic acid binding. Preferential binding of CspB to single-stranded DNA is observed in gel retardation experiments.
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Schindelin, H., Marahiel, M. & Heinemann, U. Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature 364, 164–168 (1993). https://doi.org/10.1038/364164a0
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DOI: https://doi.org/10.1038/364164a0
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