Btcd, a mouse protein that binds to curved DNA, can substitute in Escherichia coli for H-NS, a bacterial nucleoid protein.

In an Escherichia coli mutant devoid of H-NS, a bacterial nucleoid protein, mouse protein Btcd was able to substitute for H-NS in two tested functions. It restored cell motility and repression of the expression of the bgl operon. Btcd1, a mutant Btcd protein deleted of its zinc finger and thus having reduced DNA binding, failed to substitute for H-NS. Mouse protein Btcd was shown to repress the bgl operon at the level of transcription initiation and to bind preferentially to a curved DNA fragment encompassing the bgl promoter. These effects of Btcd on bacterial gene transcription can be accounted for by the binding of Btcd or H-NS to a curved DNA sequence near a promoter. A few mammalian proteins have been shown to substitute for their Escherichia prototypes involved in DNA and RNA transactions. The efficiency of Btcd protein in substituting for H-NS in Escherichia suggests its possible involvement in regulating gene expression in mouse cells.