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Nucleic Acids Research, 1992, Vol. 20, No. 7 1553-1558
© 1992

MOLECULAR BIOLOGY

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

Heisaburo Shindo, Arata Furubayashi, Mitsuhiro Shimizu, Masaki Miyake and Fumio Imamoto1

Tokyo College of Pharmacy Horinouchi, Hachioji, Tokyo 192-03 1Institute of Molecular and Cellular Biology for Pharmaceutical Sciences, Kyoto Pharmaceutical University Yamashida-ku, Kyoto 607, Japan

Received January 17, 1992. Revised March 10, 1992. Accepted March 10, 1992.

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 supercoiied piasmid in the presence of HU{alpha}. It was shown that HU{alpha} protein has preferential affinity to negatively supercoiied DNA relative to relaxed, nicked and linearized DNAs. There were two modes for binding of HU{alpha} to the supercoiied 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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