IHF and HU: flexible architects of bent DNA.
The energetic cost of bending short segments of DNA is very high. This bending is critical for the packaging of DNA and is exploited to regulate many cellular processes. In prokaryotes, IHF and HU are key architectural proteins present at high concentrations. New protein-DNA co-crystal structures, and the adaptation of advanced biophysical and biochemical techniques have led to an improved understanding of how these proteins interact with DNA. These techniques include time-resolved synchrotron X-ray footprinting, differential scanning calorimetry, isothermal titration calorimetry and single-molecule experiments.
Swinger
Kerren K
KK
Department of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL 60637, USA.
Rice
Phoebe A
PA
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D002152:Calorimetry, Differential Scanning; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004926:Escherichia coli / Q000235:genetics; D034982:Integration Host Factors / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D016415:Sequence Alignment; D017385:Sequence Homology; D013329:Structure-Activity Relationship; D013816:Thermodynamics
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D034982:Integration Host Factors; C040330:histone-like protein HU, bacteria; D004247:DNA