H
IPR008917

Transcription factor, Skn-1-like, DNA-binding domain superfamily

InterPro entry
Short nameTF_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

molecular function

cellular component

  • None

Cross References

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