Holck A, Kleppe K
FEBS Lett. 1985 Jun 3;185(1):121-4. doi: 10.1016/0014-5793(85)80753-5.
The binding of protein HU from Escherichia coli to nucleic acids was investigated by affinity chromatography under various conditions, by a nitrocellulose retention assay and by isopycnic centrifugations in metrizamide gradients. The results indicate that HU has a preference for binding to RNA and single-stranded DNA over double-stranded DNA. The affinity of HU for supercoiled DNA was also less than that of the corresponding relaxed DNA.