
Allostery Across DNA Proteins, such as transcription factors and RNA polymerase, bind close to each other on DNA and their function is coordinated. Kim et al. (p. 816 ; see the Perspective by Crothers ) report single-molecule experiments that show that the DNA binding affinity of a protein is significantly altered by a second protein bound nearby. The effect oscillates between stabilizing and destabilizing the binding with a periodicity equal to the helical pitch of DNA. Allosteric coupling between a transcriptional repressor and RNA polymerase modulated gene expression in living bacteria.
570, Binding Sites, Base Sequence, Gene Expression, DNA-Directed RNA Polymerases, Gene Expression Regulation, Bacterial, Molecular Dynamics Simulation, 530, Nucleosomes, Protein Structure, Tertiary, DNA-Binding Proteins, Viral Proteins, Receptors, Glucocorticoid, Allosteric Regulation, Escherichia coli, Lac Repressors, DNA, B-Form, Protein Binding, Transcription Factors
570, Binding Sites, Base Sequence, Gene Expression, DNA-Directed RNA Polymerases, Gene Expression Regulation, Bacterial, Molecular Dynamics Simulation, 530, Nucleosomes, Protein Structure, Tertiary, DNA-Binding Proteins, Viral Proteins, Receptors, Glucocorticoid, Allosteric Regulation, Escherichia coli, Lac Repressors, DNA, B-Form, Protein Binding, Transcription Factors
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