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|Title:||Purification and self-association equilbria of the lysis-lysogeny switch proteins of coliphage 186|
|Citation:||Journal of Biological Chemistry, 1996; 271(19):11525-11531|
|Publisher:||AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC|
|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 switch of coliphage 186. These proteins have been overexpressed, purified, and their self-association behavior examined by sedimentation equilibrium. Phage 186 CI dimers self-associate in solution through tetramers to octamers in a concerted process. The Apl protein of 186 is an unusual example of a helix- turn-helix protein which is monomeric in solution.|
|Appears in Collections:||Aurora harvest 2|
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