Ke. Shearwin et Jb. Egan, PURIFICATION AND SELF-ASSOCIATION EQUILIBRIA OF THE LYSIS-LYSOGENY SWITCH PROTEINS OF COLIPHAGE-186, The Journal of biological chemistry, 271(19), 1996, pp. 11525-11531
The CI repressor protein, responsible for maintenance of the lysogenic
state, and the Apl protein, required for efficient prophage induction
, are the two control proteins of the lysis-lysogeny transcriptional s
witch of coliphage 186. These proteins have been overexpressed, purifi
ed, and their self-association behavior examined by sedimentation equi
librium. Phage 186 CI dimers self-associate in solution through tetram
ers to octamers in a concerted process. The Apl protein of 186 is an u
nusual example of a helix-turn-helix protein which is monomeric in sol
ution.