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

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Item Type:	Article
Title:	Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein
Creators Name:	Schindelin, H., Marahiel, M.A. and Heinemann, U.
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, 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.
Keywords:	Amino Acid Sequence, Bacillus subtilis, Bacterial Proteins, Base Sequence, Binding Sites, Crystallography, DNA-Binding Proteins, Molecular Models, Molecular Sequence Data, Secondary Protein Structure, Tertiary Protein Structure, RNA-Binding Proteins
Source:	Nature
ISSN:	0028-0836
Publisher:	Nature Publishing Group
Volume:	364
Number:	6433
Page Range:	164-168
Date:	8 July 1993
Official Publication:	https://doi.org/10.1038/364164a0
PubMed:	View item in PubMed

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