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Purification and self-association equilibria of the lysis-lysogeny switch proteins of coliphage 186.

作者信息

Shearwin K E, Egan J B

机构信息

Department of Biochemistry, University of Adelaide, Australia.

出版信息

J Biol Chem. 1996 May 10;271(19):11525-31. doi: 10.1074/jbc.271.19.11525.

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.

摘要

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