[Analysis of the interaction of cyanobacterial HU-type protein and supercoiled circular DNA].
The use of small topoisomerised DNA rings to study in vitro DNA-protein interactions with a cyanobacterial HU-type protein allowed to obtain stable complexes which in turn distinguish the properties of that protein as compared with those of histones. Like histones, the HU-type protein is able to compact topoisomers under two forms, but unlike histones, these two compacted forms cannot be separated by sedimentation. Similar cross-links, when observed with histones, are obtained by formaldehyde-mediated DNA-HU type protein cross-links.
Crevel
G
G
C.N.R.S., Laboratoire de Bioénergétique cellulaire et Cytophysiologie, Gif-sur-Yvette.
D001426:Bacterial Proteins / Q000378:metabolism*; D004278:DNA, Superhelical / Q000378:metabolism*; D004347:Drug Interactions; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000494:pharmacology; D007536:Isomerism; D009690:Nucleic Acid Conformation
D001426:Bacterial Proteins; D004278:DNA, Superhelical; D006657:Histones
Analyse de l'interaction entre une protéine cyanobactérienne de type HU et un ADN circulaire surenroulé.