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Curr Opin Struct Biol. 2009 Feb;19(1):79-86. doi: 10.1016/j.sbi.2008.12.008. Epub 2009 Jan 30.

The bacteriophage lambda CI protein finds an asymmetric solution.

Author information

1
Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115, United States. ahochschild@hms.harvard.edu

Abstract

The CI protein of bacteriophage lambda (lambdaCI) 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, lambdaCI 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 lambda 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 lambdaCI dimer reveals that the two subunits of the dimer adopt different conformations. This unexpected asymmetry helps explain how these higher-order complexes are assembled.

PMID:
19181516
PMCID:
PMC2684985
DOI:
10.1016/j.sbi.2008.12.008
[Indexed for MEDLINE]
Free PMC Article

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