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Structure in solution of the major cold-shock protein from Bacillus subtilis.

Schnuchel A, Wiltscheck R, Czisch M, Herrler M, Willimsky G, Graumann P, Marahiel MA, Holak TA
Nature 364 169-71 (1993)
Cited: 131 times
EuropePMC logo PMID: 8321289

Abstract

The cold-shock domain (CSD) is found in many eukaryotic transcriptional factors and is responsible for the specific binding to DNA of a cis-element called the Y-box. The same domain exists in the sequence of the Xenopus RNA-binding proteins FRG Y1 and FRG Y2 (refs 1, 3). The major cold-shock proteins of Escherichia coli (CS7.4) and B. subtilis (CspB) have sequences that are more than 40 per cent identical to the cold-shock domain. We present here the three-dimensional structure of CspB determined by nuclear magnetic resonance spectroscopy. The 67-residue protein consists of an antiparallel five-stranded beta-barrel with strands connected by turns and loops. The structure resembles that of staphylococcal nuclease and the gene-5 single-stranded-DNA-binding protein. A three-stranded beta-sheet, which contains the conserved RNA-binding motif RNP1 as well as a motif similar to RNP2 in two neighbouring antiparallel beta-strands, has basic and aromatic residues at its surface which could serve as a binding site for single-stranded DNA. CspB binds to single-stranded DNA in gel retardation experiments.

Articles - 1nmf mentioned but not cited (2)

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Related citations provided by authors (1)

  1. Characterization of Cspb, a Bacillus Subtilis Inducible Cold Shock Gene Affecting Cell Viability at Low Temperatures. Willimsky G, Bang H, Fischer G, Marahiel MA J. Bacteriol. 174 6326- (1992)

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