A new DNA-binding motif in the Skn-1 binding domain–DNA complex
- 1 June 1998
- journal article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 5 (6) , 484-491
- https://doi.org/10.1038/nsb0698-484
Abstract
The DNA-binding domain of Skn-1, a developmental transcription factor that specifies mesoderm in C. elegans. is shown by X-ray crystallography to have a novel fold in which a compact, monomeric, four-helix unit organizes two DNA-contact elements. At the C-terminus, a helix extends from the domain to occupy the major groove of DNA in a manner similar to bZip proteins. Skn-1, however, lacks the leucine zipper found in all bZips. Additional contacts with the DNA are made by a short basic segment at the N-terminus of the domain, reminiscent of the ‘homeodomain arm’.Keywords
This publication has 45 references indexed in Scilit:
- SKN-1 domain folding and basic region monomer stabilization upon DNA bindingGenes & Development, 1997
- Skn-1: Evidence for a bipartite recognition helix in DNA bindingProceedings of the National Academy of Sciences, 1997
- Formation of a Monomeric DNA Binding Domain by Skn-1 bZIP and Homeodomain ElementsScience, 1994
- Bacterial expression and characterization of the CREB bZip module: Circular dichroism and 2D 1H‐NMR studiesProtein Science, 1993
- Protein traffic on the heat shock promoter: Parking, stalling, and trucking alongCell, 1993
- skn-1, a maternally expressed gene required to specify the fate of ventral blastomeres in the early C. elegans embryoCell, 1992
- DNA-induced increase in the .alpha.-helical content of C/EBP and GCN4Biochemistry, 1991
- Altered protein conformation on DNA binding by Fos and JunNature, 1990
- Folding transition in the DMA-binding domain of GCN4 on specific binding to DNANature, 1990
- Nucleotide sequence and structural analysis of the zeste locus of Drosophila melanogasterMolecular Genetics and Genomics, 1988