An Escherichia coli protein that preferentially binds to sharply curved DNA.
We attempted to find Escherichia coli proteins which preferentially bind to a curved DNA sequence even in the presence of an excess amount of a non-curved DNA sequence as a competitor, mainly by means of a DNA-binding gel retardation assay. Since the two sequences used had nearly the same nucleotide compositions, including consecutive dA5 stretches, we reasoned that this strategy would allow us to identify proteins which preferentially recognize an overall DNA curvature. We purified such a protein from E. coli. Its preferential binding to the curved DNA was found to be inhibited by distamycin, which removes the curvature from appropriate DNA sequences. The purified protein was identified as the E. coli nucleoid protein, H-NS.
Yamada
H
H
Laboratory of Microbiology, School of Agriculture, Nagoya University, Aichi.
Muramatsu
S
S
Mizuno
T
T
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000378:metabolism*; D001483:Base Sequence; D001667:Binding, Competitive; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004214:Distamycins / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics*; D008969:Molecular Sequence Data; D008970:Molecular Weight
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D004214:Distamycins; C031908:H-NS protein, bacteria; D004247:DNA