Physical Review Letters · 2010 · 40 citations · 15 references
Life SciencesBiophysicsMolecular BiologyGene StructureMolecular BiophysicsMolecular PhysicsConformational DynamicsDna LoopingDna StructureLoop ModelingMacromolecular AssemblyDna Looping DynamicsDna-binding Protein-mediated LoopingDna-protein Interactions Under ForceLoop Formation KineticsMechanics Of Dna Loop FormationPolymer Models Of Dna LoopingProtein-dna Complex StructureThermal Fluctuations
We show that minuscule entropic forces, on the order of 100 fN, can prevent the formation of DNA loops-a ubiquitous means of regulating the expression of genes. We observe a tenfold decrease in the rate of LacI-mediated DNA loop formation when a tension of 200 fN is applied to the substrate DNA, biasing the thermal fluctuations that drive loop formation and breakdown events. Conversely, once looped, the DNA-protein complex is insensitive to applied force. Our measurements are in excellent agreement with a simple polymer model of loop formation in DNA, and show that an antiparallel topology is the preferred LacI-DNA loop conformation for a generic loop-forming construct.
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Crystal Structure of the Lactose Operon Repressor and Its Complexes with DNA and Inducer
Mitchell Lewis, Geoffrey Chang, Nancy C. Horton et al. · Science · 1996 · 801 citations
The three operators of the lac operon cooperate in repression.
Stefan Oehler, Elisabeth R. Eismann, Helmut Krämer et al. · The EMBO Journal · 1990 · 492 citations · Full text