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https://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 |
DOI: | 10.1016/j.molcel.2006.01.019 |
Description (link): | http://www.molecule.org/ |
Published version: | http://dx.doi.org/10.1016/j.molcel.2006.01.019 |
Appears in Collections: | Aurora harvest 6 Molecular and Biomedical Science publications |
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