Protein-DNA interactions for metalloregulator mediated transcriptional regulation.
 

    Metalloregulators respond to metal ion concentrations via conformational changes that lead to their different interactions with their target DNA sequences and thus transcriptional regulation in gene expression. We are studying the conformational dynamics of metalloregulators and DNA, and their interaction dynamics involved in these regulation processes. We have developed a novel single-molecule method using engineered DNA Holliday junctions as single-molecule reporters to study metalloregulator-DNA interactions (see Figure below). By encoding targeting sequences in a DNA Holliday junction, protein actions on the DNA are converted to the changes on the structural dynamics of the engineered Holliday junction, which can be followed easily at the single-molecule level.

Figure. Engineered DNA Holliday junctions as generalizable single-molecule reporters for protein-DNA interactions.