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https://hdl.handle.net/2440/11317
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DC Field | Value | Language |
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dc.contributor.author | Shearwin, K. | - |
dc.contributor.author | Egan, J. | - |
dc.date.issued | 1996 | - |
dc.identifier.citation | Journal of Biological Chemistry, 1996; 271(19):11525-11531 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.issn | 1083-351X | - |
dc.identifier.uri | http://hdl.handle.net/2440/11317 | - |
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.language.iso | en | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.source.uri | http://dx.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 | - |
dc.identifier.doi | 10.1074/jbc.271.19.11525 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Shearwin, K. [0000-0002-7736-2742] | - |
Appears in Collections: | Aurora harvest 2 Biochemistry publications |
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