Isolation of a DNA-binding protein from Deinococcus radiodurans having an affinity for a Z-form polynucleotide.
A protein which preferentially binds Z-form duplex DNA has been purified from the cells of Deinococcus radiodurans. The molecular weight of the protein was estimated to be approximately 68,000 by gel filtration and SDS-polyacrylamide gel electrophoresis. Amino acid analysis of the protein indicates that it is not so basic since it contains a lower mole percent of lysine and higher mole percent of aspartic acid than those in histone-like DNA binding protein II (HU) of Escherichia coli. The first fifteen amino acid residues from the N-terminus have been also determined.
Kitayama
S
S
Radiobiology Laboratory, Institute of Physical and Chemical Research, Saitama.
Matsumura
O
O
Masuda
S
S
D000596:Amino Acids / Q000032:analysis; D004269:DNA, Bacterial / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000302:isolation & purification* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D007700:Kinetics; D009690:Nucleic Acid Conformation
D000596:Amino Acids; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins