IPR008917
Transcription factor, Skn-1-like, DNA-binding domain superfamily
InterPro entry
Short name | TF_DNA-bd_sf |
Overlapping entries |
Description
The DNA-binding domain of certain eukaryotic transcription factors displays a distinctive helix-turn-helix (HTH) motif. The MafG basic region-leucine zipper (bZIP) protein and the Caenorhabditis elegans Skn-1 transcription factor share this HTH motif.
MafG is a member of the Maf family of proteins, which are a subgroup of bZIP proteins that function as transcriptional regulators of cellular differentiation. Mafs can form either homodimers, or heterodimers with other bZIP proteins through their leucine zipper domains. MafG proteins are small Mafs that lack a putative transactivation domain. The DNA-binding domain of MafG contains the conserved Maf extended homology region (EHR), which is not present in other bZIP proteins. The EHR together with the basic region are responsible for the DNA-binding specificity of Mafs.
Skn-1 is a transcription factor that specifies mesodermal development in C. elegans. Skn-1 and MafG share a conserved DNA-binding motif, however Skn-1 lacks the leucine zipper dimerisation domain that is found in all bZIP proteins. Skn-1 acts as a monomer.
References
1. Solution structure of the DNA-binding domain of MafG. Kusunoki H, Motohashi H, Katsuoka F, Morohashi A, Yamamoto M, Tanaka T. Nat. Struct. Biol. 9, 252-6, (2002). View articlePMID: 11875518
2. A new DNA-binding motif in the Skn-1 binding domain-DNA complex. Rupert PB, Daughdrill GW, Bowerman B, Matthews BW. Nat. Struct. Biol. 5, 484-91, (1998). View articlePMID: 9628487
GO terms
biological process
molecular function
cellular component
- None
Cross References
Contributing Member Database Entry
- SUPERFAMILY:SSF47454