Periodicity in recA protein-DNA complexes.
The reaction of guanine residues with dimethylsulfate was studied for complexes of recA protein with fluorescent dye tagged double stranded oligonucleotides. The patterns of dimethylsulfate modification obtained demonstrate a similarity of DNA states in the complexes with recA protein formed as a result of recA promoted strand exchange and renaturation reactions. The guanine modification efficiency varies periodically as a function of the base position along the oligonucleotide axis, with a period of 3 nucleotides. This effect suggests that the arrangement of recA monomers along the oligonucleotide is strictly ordered, and the dimethylsulfate reactivity of a guanine residue depends on the site of its binding in a recA monomer.
Volodin
A A
AA
Institute of Molecular Genetics of the Russian Academy of Sciences, Moscow.
Smirnova
H A
HA
Bocharova
T N
TN
D001483:Base Sequence; D001665:Binding Sites; D004269:DNA, Bacterial / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D005456:Fluorescent Dyes; D006147:Guanine / Q000737:chemistry; D046911:Macromolecular Substances; D009838:Oligodeoxyribonucleotides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011938:Rec A Recombinases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013463:Sulfuric Acid Esters
D004269:DNA, Bacterial; D005456:Fluorescent Dyes; D046911:Macromolecular Substances; D009838:Oligodeoxyribonucleotides; D013463:Sulfuric Acid Esters; D006147:Guanine; D011938:Rec A Recombinases; C007482:dimethyl sulfate