The DDT family consists of members containing the DDT domain, a likely DNA binding domain. It consists of conserved N terminal phenylalanines, as well as conserved C terminal leucines. The putative protein-protein interaction motif of this domain is not conserved . It was originally identified in bromodomain PHD finger transcription factors (BPTFs), chromatin remodeling factors of the BAZ-family and other putative nuclear proteins (Doerks et al., 2001).

The Arabidopsis genome contains at least 12 genes that encode DDT-domain proteins, which could be grouped into five subfamilies based on the sequence similarity (Dong et al., 2013). The SLIDE domain of AtISWI (Imitation Switch) is able to bind members from different AtDDT subfamilies. Moreover, a human ISWI protein SNF2H is capable of binding AtDDT-domain proteins through its SLIDE domain, suggesting that binding to DDT-domain proteins is a conserved biochemical function for the SLIDE domain of ISWIs in eukaryotes (Dong et al., 2013). The maize genome also harbors at least 12 DDT domain encoding genes.

Last updated June 2023 by John Gray

References:

Doerks T, Copley R, Bork P. DDT -- a novel domain in different transcription and chromosome remodeling factors. Trends Biochem Sci. 2001 Mar;26(3):145-6. doi: 10.1016/s0968-0004(00)01769-2. PMID: 11246006.

Dong J, Gao Z, Liu S, Li G, Yang Z, Huang H, Xu L. SLIDE, the protein interacting domain of Imitation Switch remodelers, binds DDT-domain proteins of different subfamilies in chromatin remodeling complexes. J Integr Plant Biol. 2013 Oct;55(10):928-37. doi: 10.1111/jipb.12069. Epub 2013 Sep 16. PMID: 23691993.