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Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein

Nature volume 364, pages 164–168 (1993)Cite this article

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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Author notes

  1. Mohamed A. Marahiel: Biochemie/FB Chemie, Philipps-Universität Marburg, Hans-Meerwein Strasse, D-35043 Marburg, Germany

Affiliations

  1. Institut für Kristallographie, Freie Universität Berlin, Takustrasse 6, D-14195, Berlin, Germany

    Hermann Schindelin, Mohamed A. Marahiel & Udo Heinemann

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  1. Hermann Schindelin
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  2. Mohamed A. Marahiel
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  3. Udo Heinemann
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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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