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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1993-07

AUTHORS

H Schindelin, M A Marahiel, U Heinemann

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. More... »

PAGES

164-168

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/364164a0

DOI

http://dx.doi.org/10.1038/364164a0

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https://app.dimensions.ai/details/publication/pub.1046167867

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8321288


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