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Type: Journal article
Title: Purification and self-association equilbria of the lysis-lysogeny switch proteins of coliphage 186
Author: Shearwin, K.
Egan, J.
Citation: Journal of Biological Chemistry, 1996; 271(19):11525-11531
Issue Date: 1996
ISSN: 0021-9258
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.
DOI: 10.1074/jbc.271.19.11525
Appears in Collections:Aurora harvest 2
Biochemistry publications

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