|Title||Purification and properties of a cruciform DNA binding protein from Ustilago maydis.|
|Publication Type||Journal Article|
|Year of Publication||1993|
|Authors||Kotani H, Kmiec EB, Holloman WK|
|Date Published||1993 May|
|Keywords||Base Sequence, Chromatography, Gel, DNA, Fungal, DNA-Binding Proteins, Kinetics, Molecular Sequence Data, Nucleic Acid Conformation, Protein Binding, Solubility, Ustilago|
A DNA binding protein with an M(r) of 11,000 was purified from Ustilago maydis. Its solubility in acid, amino acid composition, and mobility during gel electrophoresis are reminiscent of properties observed for the high mobility group nonhistone chromosomal proteins. The protein recognizes cruciform DNA made from oligonucleotides and also binds preferentially to a plasmid containing an extruded cruciform.