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

Nature. 1993 Jul 8;364(6433):164-8. doi: 10.1038/364164a0.


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, respectively. CS7.4 is a transcriptional activator of two genes. CS7.4 and CspB share 43 per cent sequence identity with the nucleic acid-binding domain of the eukaryotic gene-regulatory Y-box factors. This cold-shock domain is conserved from bacteria to man and contains the RNA-binding RNP1 sequence motif. 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 beta-barrel. Three consecutive beta-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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / chemistry*
  • Bacterial Proteins / chemistry*
  • Base Sequence
  • Binding Sites
  • Crystallography
  • DNA-Binding Proteins / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • RNA-Binding Proteins / chemistry*


  • Bacterial Proteins
  • DNA-Binding Proteins
  • RNA-Binding Proteins
  • cold-shock protein CspB, Bacteria