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The structural basis of cooperative regulation at an alternate genetic switch

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dc.contributor.authorPinkett, H.
dc.contributor.authorShearwin, K.
dc.contributor.authorStayrook, S.
dc.contributor.authorDodd, I.
dc.contributor.authorBurr, T.
dc.contributor.authorHochschild, A.
dc.contributor.authorEgan, J.
dc.contributor.authorLewis, M.
dc.date.issued2006
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.
dc.description.statementofresponsibilityHeather W. Pinkett, Keith E. Shearwin, Steven Stayrook, Ian B. Dodd, Tom Burr, Ann Hochschild, J. Barry Egan and Mitchell Lewis
dc.description.urihttp://www.molecule.org/
dc.identifier.citationMolecular Cell, 2006; 21(5):605-615
dc.identifier.doi10.1016/j.molcel.2006.01.019
dc.identifier.issn1097-4164
dc.identifier.issn1097-2765
dc.identifier.orcidShearwin, K. [0000-0002-7736-2742]
dc.identifier.orcidDodd, I. [0000-0003-2969-6841]
dc.identifier.urihttp://hdl.handle.net/2440/23998
dc.language.isoen
dc.publisherCell Press
dc.rightsCopyright © 2007 Elsevier
dc.source.urihttps://doi.org/10.1016/j.molcel.2006.01.019
dc.subjectBacteriophage lambda
dc.subjectColiphages
dc.subjectRepressor Proteins
dc.subjectViral Proteins
dc.subjectDNA, Viral
dc.subjectCrystallography, X-Ray
dc.subjectAmino Acid Substitution
dc.subjectVirus Assembly
dc.subjectGene Expression Regulation, Viral
dc.subjectProtein Structure, Tertiary
dc.subjectStructure-Activity Relationship
dc.subjectDimerization
dc.titleThe structural basis of cooperative regulation at an alternate genetic switch
dc.typeJournal article
pubs.publication-statusPublished

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