Structural motif of the DNA binding domain of gamma delta-resolvase characterized by affinity cleaving.
The DNA binding domain of gamma delta-resolvase, residues 141-183, is thought to bind DNA by a helix-turn-helix motif based on sequence similarities with other known DNA binding proteins. Incorporation of the DNA cleaving moiety, EDTA Fe, at the NH2 and COOH termini of gamma delta(141-183) allows the positions of these residues relative to the DNA bases at three resolvase binding sites, each consisting of inverted copies of an imperfectly conserved 9-base pair sequence, to be mapped by high resolution gel electrophoresis. The cleavage data for EDTA-gamma delta(141-183) reveals that the NH2 terminus of the DNA binding domain of gamma delta-resolvase is bound proximal to the minor groove of DNA near the center of the resolvase binding sites. Cleavage by EDTA Fe attached to a lysine side chain (Asn183----Lys183) at the COOH terminus of gamma delta(141-183) reveals that the putative recognition helix is in the adjacent major groove on the same face of the helix, oriented toward the center of the inverted repeats.
Graham
K S
KS
Arnold and Mabel Beckman Laboratory of Chemical Synthesis, California Institute of Technology 91125.
Dervan
P B
PB
D000595:Amino Acid Sequence; D001482:Base Composition; D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000235:genetics / Q000378:metabolism*; D004492:Edetic Acid; D008957:Models, Genetic; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D009713:Nucleotidyltransferases / Q000235:genetics / Q000378:metabolism*; D010455:Peptides / Q000138:chemical synthesis; D013379:Substrate Specificity; D019895:Transposases
D010455:Peptides; D004247:DNA; D004492:Edetic Acid; D009713:Nucleotidyltransferases; D019895:Transposases