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dc.contributor.authorPinkett, H.en
dc.contributor.authorShearwin, K.en
dc.contributor.authorStayrook, S.en
dc.contributor.authorDodd, I.en
dc.contributor.authorBurr, T.en
dc.contributor.authorHochschild, A.en
dc.contributor.authorEgan, J.en
dc.contributor.authorLewis, M.en
dc.identifier.citationMolecular Cell, 2006; 21(5):605-615en
dc.description.abstractBacteriophage λ is a paradigm for understanding the role of cooperativity in gene regulation. Comparison of the regulatory regions of λ and the unrelated temperate bacteriophage 186 provides insight into alternate ways to assemble functional genetic switches. The structure of the C-terminal domain of the 186 repressor, determined at 2.7 Å resolution, reveals an unusual heptamer of dimers, consistent with presented genetic studies. In addition, the structure of a cooperativity mutant of the full-length 186 repressor, identified by genetic screens, was solved to 1.95 Å resolution. These structures provide a molecular basis for understanding lysogenic regulation in 186. Whereas the overall fold of the 186 and λ repressor monomers is remarkably similar, the way the two repressors cooperatively assemble is quite different and explains in part the differences in their regulatory activity.en
dc.description.statementofresponsibilityHeather W. Pinkett, Keith E. Shearwin, Steven Stayrook, Ian B. Dodd, Tom Burr, Ann Hochschild, J. Barry Egan and Mitchell Lewisen
dc.publisherCell Pressen
dc.rightsCopyright © 2007 Elsevieren
dc.subjectBacteriophage lambda; Coliphages; Repressor Proteins; Viral Proteins; DNA, Viral; Crystallography, X-Ray; Amino Acid Substitution; Virus Assembly; Gene Expression Regulation, Viral; Protein Structure, Tertiary; Structure-Activity Relationship; Dimerizationen
dc.titleThe structural basis of cooperative regulation at an alternate genetic switchen
dc.typeJournal articleen
pubs.library.collectionMolecular and Biomedical Science publicationsen
Appears in Collections:Molecular and Biomedical Science publications

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