Role of the Xis protein of bacteriophage lambda in a specific reactive complex at the attR prophage attachment site

Phage lambda controls its integration and excision by differential catalysis of the forward and reverse reactions. The lambda Int protein is required for both directions, but Xis for excision only. Previous electron microscopic observations have shown that Int protein forms a stable, condensed protein-DNA complex with the phage (attP) and prophage left (attL) substrate sites, but not with the host (attB) or prophage right (attR) sites. We have found that Int and Xis together produce a stable, condensed complex with attR. The attR complex involves the P region DNA to the left of the crossover point (O site). In contrast, the attP complex includes DNA on both sides of the crossover point (P and P'), and the attL structure involves the P' DNA to the right of O. In the presence of Int and Xis, the attL and attR sites form a paired structure. We conclude that the role of Xis is to provide a distinct reactive structure at attR, allowing attL and attR to pair efficiently.