PURIFICATION AND SELF-ASSOCIATION EQUILIBRIA OF THE LYSIS-LYSOGENY SWITCH PROTEINS OF COLIPHAGE-186

Citation
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
Citations number
28
Categorie Soggetti
Biology
ISSN journal
00219258
Volume
271
Issue
19
Year of publication
1996
Pages
11525 - 11531
Database
ISI
SICI code
0021-9258(1996)271:19<11525:PASEOT>2.0.ZU;2-0
Abstract
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.