Interactions between integrase and excisionase in the phage lambda excisive nucleoprotein complex.
Bacteriophage lambda site-specific recombination comprises two overall reactions, integration into and excision from the host chromosome. Lambda integrase (Int) carries out both reactions. During excision, excisionase (Xis) helps Int to bind DNA and introduces a bend in the DNA that facilitates formation of the proper excisive nucleoprotein complex. The carboxyl-terminal alpha-helix of Xis is thought to interact with Int through direct protein-protein interactions. In this study, we used gel mobility shift assays to show that the amino-terminal domain of Int maintained cooperative interactions with Xis. This finding indicates that the amino-terminal arm-type DNA binding domain of Int interacts with Xis.
Department of Science Education, Chosun University, Kwangju, Korea.
Eun Hee
EH
Cho
Richard I
RI
Gumport
Jeffrey F
JF
Gardner
D010582:Bacteriophage lambda / Q000235:genetics / Q000378:metabolism*; D004254:DNA Nucleotidyltransferases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004279:DNA, Viral / Q000378:metabolism; D015967:Gene Expression Regulation, Viral; D019426:Integrases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D009698:Nucleoproteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D011995:Recombination, Genetic; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D004279:DNA, Viral; D009698:Nucleoproteins; D014764:Viral Proteins; D004254:DNA Nucleotidyltransferases; D019426:Integrases; C063911:excisionase