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. 1992 Apr 11;20(7):1553–1558. doi: 10.1093/nar/20.7.1553

Preferential binding of E.coli histone-like protein HU alpha to negatively supercoiled DNA.

H Shindo 1, A Furubayashi 1, M Shimizu 1, M Miyake 1, F Imamoto 1
PMCID: PMC312237  PMID: 1579448

Abstract

Binding specificity of histone-like HU alpha protein to supercoiled DNA was examined by gel retardation assay and chemical probing with OsO4. The latter method was proved to be a unique means for detecting torsional tension restrained in supercoiled plasmid in the presence of HU alpha. It was shown that HU alpha protein has preferential affinity to negatively supercoiled DNA relative to relaxed, nicked and linearized DNAs. There were two modes for binding of HU alpha to the supercoiled DNA: one was the binding associated with topological changes in DNA and the other was relatively strong binding, probably specific to certain particular structures of DNA. It was suggested that HU in vivo interacts preferentially with the regions deformed under torsional stress or with the metabolically active regions along DNA.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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