Abstract
Horizontal gene transfer (HGT) is a major driver of bacterial evolution, allowing for rapid development of deleterious functions - such as virulence or antibiotic resistance. However, expressing foreign DNA without selection is at best a waste of resources and at worst fatal to the bacterium. Bacteria have, therefore, developed mechanisms to selectively silence foreign genes. For instance, the histone-like nucleoid-structuring protein (H-NS) silences foreign genes that are recognized by their AT content. It has previously been shown that the binding of H-NS to AT-rich DNA dramatically changes the persistence length of the DNA. However, we discovered that the persistence length measured under no load, via tethered particle motion (TPM), and under increasing H-NS concentrations was much less sensitive to concentration than when stretched with optical tweezers. Our results indicate a previously unknown protein-DNA structure which breaks down under an applied force.
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