Purification and self-association equilbria of the lysis-lysogeny switch proteins of coliphage 186
| dc.contributor.author | Shearwin, K. | |
| dc.contributor.author | Egan, J. | |
| dc.date.issued | 1996 | |
| dc.description.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. | |
| dc.identifier.citation | Journal of Biological Chemistry, 1996; 271(19):11525-11531 | |
| dc.identifier.doi | 10.1074/jbc.271.19.11525 | |
| dc.identifier.issn | 0021-9258 | |
| dc.identifier.issn | 1083-351X | |
| dc.identifier.orcid | Shearwin, K. [0000-0002-7736-2742] | |
| dc.identifier.uri | http://hdl.handle.net/2440/11317 | |
| dc.language.iso | en | |
| dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | |
| dc.source.uri | https://doi.org/10.1074/jbc.271.19.11525 | |
| dc.title | Purification and self-association equilbria of the lysis-lysogeny switch proteins of coliphage 186 | |
| dc.type | Journal article | |
| pubs.publication-status | Published |