Article ID Journal Published Year Pages File Type
10822647 Current Opinion in Structural Biology 2009 8 Pages PDF
Abstract
The CI protein of bacteriophage λ (λCI) is both a repressor and activator of transcription that has served as a model for understanding how gene regulatory proteins work. A dimeric DNA-binding protein, λCI also forms higher-order oligomers that allow it to bind cooperatively to both adjacent and nonadjacent operator sites within the phage genome. The ability of phage λ to transition efficiently from one program of gene expression to another depends upon the formation of these higher-order protein-DNA complexes. A recently determined crystal structure of a DNA-bound λCI dimer reveals that the two subunits of the dimer adopt different conformations. This unexpected asymmetry helps explain how these higher-order complexes are assembled.
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Life Sciences Biochemistry, Genetics and Molecular Biology Biochemistry
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