Journal
GENES & DEVELOPMENT
Volume 15, Issue 17, Pages 2273-2281Publisher
COLD SPRING HARBOR LAB PRESS
DOI: 10.1101/gad.920301
Keywords
transcription repression; DNA looping; protein-protein interaction; HU mutants
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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 GaIR-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.
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