Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 19, Issue 1, Pages 79-86Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2008.12.008
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Funding
- NIH [GM44025, GM44617]
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The Cl protein of bacteriophage X (lambda Cl) 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, lambda Cl 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 X to transition efficiently from one program gene expression to another depends upon the formation of these higher-order protein-DNA complexes. A recently determined crystal structure of a DNA-bound lambda Cl 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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