InterPro domain: IPR002197

The Factor for Inversion Stimulation (FIS) protein is a regulator of bacterial functions, and binds specifically to weakly related DNA sequences [ 1 , 2 ]. It activates ribosomal RNA transcription, and is involved in upstream activation of rRNA promoters. The protein has been shown to play a role in the regulation of virulence factors in both Salmonella typhimurium and Escherichia coli [ 3 ]. Some of its functions include inhibition of the initiation of DNA replication from the OriC site, and promotion of Hin-mediated DNA inversion.

In its C-terminal extremity, FIS encodes a helix-turn-helix (HTH) DNA- binding motif, which shares a high degree of similarity with other HTH motifs of more primitive bacterial transcriptional regulators, such as the nitrogen assimilation regulatory proteins (NtrC) from species like Azobacter, Rhodobacter and Rhizobium. This has led to speculation that both evolved from a single common ancestor [ 4 ].

The 3-dimensional structure of the E. coli FIS DNA-binding protein has been determined by means of X-ray diffraction to 2.0A resolution [ 5 , 6 ]. FIS is composed of four alpha-helices tightly intertwined to form a globular dimer with two protruding HTH motifs. The 24 N-terminal amino acids are poorly defined, indicating that they might act as `feelers' suitable for DNA or protein (invertase) recognition [ 7 ]. Other proteins belonging to this subfamily include:

• E. coli: atoC, hydG, ntrC, fhlA, tyrR,
• Rhizobium spp.: ntrC, nifA, dctD

1. Sequence, regulation, and functions of fis in Salmonella typhimurium. J. Bacteriol. 177, 2021-32
2. Fis, a DNA nucleoid-associated protein, is involved in Salmonella typhimurium SPI-1 invasion gene expression. Mol. Microbiol. 39, 79-88
3. Role of the nucleoid-associated protein Fis in the regulation of virulence properties of enteropathogenic Escherichia coli. Mol. Microbiol. 41, 549-59
4. Evolution of new protein function: recombinational enhancer Fis originated by horizontal gene transfer from the transcriptional regulator NtrC. FEBS Lett. 433, 108-12
5. Crystal structure of the factor for inversion stimulation FIS at 2.0 A resolution. J. Mol. Biol. 226, 209-26
6. Structural analysis of the transcriptional activation on Fis: crystal structures of six Fis mutants with different activation properties. J. Mol. Biol. 302, 1139-51