A chimeric Rec-A protein that implicates non-Watson-Crick interactions in homologous pairing.
The helical filament formed by RecA protein on single-stranded DNA plays an important role in homologous recombination and pairs with a complementary single strand or homologous duplex DNA. The RecA nucleoprotein filament also recognizes an identical single strand. The chimeric protein, RecAc38, forms a nucleoprotein filament that recognizes a complementary strand but is defective in recognition of duplex DNA, and is associated with phenotypic defects in repair and recombination. As described here, RecAc38 nucleoprotein filament is also defective in recognition of an identical strand, either when the filament has within it a single strand or duplex DNA. A model that postulates three DNA binding sites rationalizes these observations and suggests that the third binding site mediates non-Watson-Crick interactions that are instrumental in recognition of homology in duplex DNA.
Kurumizaka
H
H
Laboratory of Cellular and Molecular Biology, Institute of Physical and Chemical Research (RIKEN), Saitama, Japan.
Rao
B J
BJ
Ogawa
T
T
Radding
C M
CM
Shibata
T
T
D001483:Base Sequence; D001665:Binding Sites; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004277:DNA, Single-Stranded / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D011938:Rec A Recombinases / Q000737:chemistry / Q000378:metabolism*; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000378:metabolism*; D017385:Sequence Homology; D013329:Structure-Activity Relationship
D004277:DNA, Single-Stranded; D011993:Recombinant Fusion Proteins; D004247:DNA; D011938:Rec A Recombinases