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Purification and characterization of a protein from escherichia coli which complexes with super helical and single stranded dna species

Purification and characterization of a protein from escherichia coli which complexes with super helical and single stranded dna species

Journal of Biochemistry 92(4): 1059-1068

From the cells of an E. coli K-12 strain, a 22,000-dalton protein which has an affinity for the superhelical DNA molecule was purified to apparent homogeneity by monitoring the DNA-binding activity using the filter binding assay. In the sedimentation analysis of the DNA-protein complex, the protein has an affinity for the superhelical or single-stranded DNA molecule but not for open circular DNA or for linear DNA molecules. The amino acid composition of the protein resembled those of the other prokaryotic histone-like proteins and also to eukaryotic histones H2A and H2B. The protein precipitated upon heating, which is in contrast to the heat-stable feature of the other histone-like proteins. DNA and RNA syntheses in vitro were not affected by the presence of the protein. This protein may play a role in maintaining the bacterial nucleoid structure.

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Purification and characterization of a protein from Escherichia coli which forms complexes with superhelical and single-stranded DNAs. Journal of Biochemistry 92(4): 1059-1068, 1982

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