The structural basis of cooperative regulation at an alternate genetic switch

Molecular Cell
Heather W PinkettM Lewis

Abstract

Bacteriophage lambda is a paradigm for understanding the role of cooperativity in gene regulation. Comparison of the regulatory regions of lambda 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 A 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 A resolution. These structures provide a molecular basis for understanding lysogenic regulation in 186. Whereas the overall fold of the 186 and lambda 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.

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Citations

Apr 7, 2007·Nucleic Acids Research·Petri Henriksson-PeltolaElisabeth Haggård-Ljungquist
Jul 20, 2010·Nucleic Acids Research·Tariq MassadPål Stenmark
Feb 2, 2010·Journal of Bacteriology·Margit PedersenKarin Hammer
May 5, 2016·Bacteriophage·Gail E Christie, Richard Calendar
May 15, 2007·Journal of Molecular Biology·Ian B DoddKim Sneppen
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Oct 22, 2008·Journal of Molecular Biology·Margit Pedersen, Karin Hammer
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Dec 6, 2018·International Journal of Biological Macromolecules·Anindya BiswasSubrata Sau
Jan 30, 2021·Nucleic Acids Research·Nan HaoIan B Dodd

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