Recruitment of HU by piggyback: a special role of GalR in repressosome assembly

Abstract

In Gal repressosome assembly, a DNA loop is formed by the interaction of two GalR, bound to two distal operators, and the binding of the histone-like protein, HU, to an architecturally critical position on DNA to facilitate the GalR–GalR interaction. We show that GalR piggybacks HU to the critical position on the DNA through a specific GalR–HU interaction. This is the first example of HU making a specific contact with another protein. The GalR–HU contact that results in cooperative binding of the two proteins to DNA may be transient and absent in the final repressosome structure. A sequence-independent DNA-binding protein being recruited to an architectural site on DNA through a specific association with a regulatory protein may be a common mode for assembly of complex nucleoprotein structures.