Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/23998
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Type: Journal article
Title: The structural basis of cooperative regulation at an alternate genetic switch
Author: Pinkett, H.
Shearwin, K.
Stayrook, S.
Dodd, I.
Burr, T.
Hochschild, A.
Egan, J.
Lewis, M.
Citation: Molecular Cell, 2006; 21(5):605-615
Publisher: Cell Press
Issue Date: 2006
ISSN: 1097-4164
1097-2765
Statement of
Responsibility: 
Heather W. Pinkett, Keith E. Shearwin, Steven Stayrook, Ian B. Dodd, Tom Burr, Ann Hochschild, J. Barry Egan and Mitchell Lewis
Abstract: Bacteriophage 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.
Keywords: Bacteriophage 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; Dimerization
Rights: Copyright © 2007 Elsevier
RMID: 0020060343
DOI: 10.1016/j.molcel.2006.01.019
Description (link): http://www.molecule.org/
Appears in Collections:Molecular and Biomedical Science publications

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