Autonomous DNA binding domains of lambda integrase recognize two different sequence families.
The 40 kd lambda Integrase protein is shown to contain two autonomous DNA binding domains with different sequence specificities. Competition experiments in which the binding activity of Int is assayed through nuclease protection demonstrate the functional independence of the two DNA recognition specificities. Proteolytic cleavage of Int and footprinting analysis of the resulting two major peptides allow the physical separation and identification of two DNA binding domains: an amino-terminal peptide that interacts with "arm-type" sites and a carboxy-terminal peptide that binds to "core-type" sequences. In addition, the data suggest that the two domains can bind DNA simultaneously, consistent with a model in which Integrase would link two disparate DNA sequences.
Moitoso de Vargas
L
L
Division of Biology and Medicine, Brown University, Providence, Rhode Island 02912.
Pargellis
C A
CA
Hasan
N M
NM
Bushman
E W
EW
Landy
A
A
D000595:Amino Acid Sequence; D010582:Bacteriophage lambda / Q000201:enzymology*; D001483:Base Sequence; D001665:Binding Sites; D001667:Binding, Competitive; D002918:Chymotrypsin; D004254:DNA Nucleotidyltransferases / Q000378:metabolism*; D004262:DNA Restriction Enzymes; D004274:DNA, Recombinant / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000378:metabolism*; D003851:Deoxyribonucleases; D019426:Integrases; D008957:Models, Genetic; D010957:Plasmids
D004274:DNA, Recombinant; D004268:DNA-Binding Proteins; D004254:DNA Nucleotidyltransferases; D019426:Integrases; D003851:Deoxyribonucleases; D004262:DNA Restriction Enzymes; D002918:Chymotrypsin