Affinity of protein HU for different nucleic acids.
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.
Holck
A
A
Kleppe
K
K
D001426:Bacterial Proteins / Q000378:metabolism*; D010584:Bacteriophage phi X 174; D002846:Chromatography, Affinity; D003454:Cryptococcus; D004269:DNA, Bacterial / Q000378:metabolism; D004277:DNA, Single-Stranded / Q000378:metabolism; D004278:DNA, Superhelical / Q000378:metabolism; D004279:DNA, Viral / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000032:analysis*; D009696:Nucleic Acids / Q000378:metabolism*; D012329:RNA, Bacterial / Q000378:metabolism; D012331:RNA, Fungal / Q000378:metabolism
D001426:Bacterial Proteins; D004269:DNA, Bacterial; D004277:DNA, Single-Stranded; D004278:DNA, Superhelical; D004279:DNA, Viral; D004268:DNA-Binding Proteins; D009696:Nucleic Acids; D012329:RNA, Bacterial; D012331:RNA, Fungal; C040330:histone-like protein HU, bacteria