Literature DB >> 8626713

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

K E Shearwin1, J B Egan.   

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.

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Year:  1996        PMID: 8626713     DOI: 10.1074/jbc.271.19.11525

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  4 in total

1.  The multifunctional bacteriophage P2 cox protein requires oligomerization for biological activity.

Authors:  J M Eriksson; E Haggârd-Ljungquist
Journal:  J Bacteriol       Date:  2000-12       Impact factor: 3.490

2.  RNA polymerase efficiently transcribes through DNA-scaffolded, cooperative bacteriophage repressor complexes.

Authors:  Yue Lu; Zsuzsanna Voros; Gustavo Borjas; Cristin Hendrickson; Keith Shearwin; David Dunlap; Laura Finzi
Journal:  FEBS Lett       Date:  2022-07-22       Impact factor: 3.864

3.  Action at a distance in CI repressor regulation of the bacteriophage 186 genetic switch.

Authors:  Ian B Dodd; J Barry Egan
Journal:  Mol Microbiol       Date:  2002-08       Impact factor: 3.501

4.  Single molecule analysis of DNA wrapping and looping by a circular 14mer wheel of the bacteriophage 186 CI repressor.

Authors:  Haowei Wang; Ian B Dodd; David D Dunlap; Keith E Shearwin; Laura Finzi
Journal:  Nucleic Acids Res       Date:  2013-04-24       Impact factor: 16.971

  4 in total

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