title: SLIDE, the protein interacting domain of Imitation Switch remodelers, binds DDT-domain proteins of different subfamilies in chromatin remodeling complexes.
abstract: The Imitation Switch (ISWI) type adenosine triphosphate (ATP)-dependent chromatin remodeling factors are conserved proteins in eukaryotes, and some of them are known to form stable remodeling complexes with members from a family of proteins, termed DDT-domain proteins. Although it is well documented that ISWIs play important roles in different biological processes in many eukaryotic species, the molecular basis for protein interactions in ISWI complexes has not been fully addressed. Here, we report the identification of interaction domains for both ISWI and DDT-domain proteins. By analyzing CHROMATIN REMODELING11 (CHR11) and RINGLET1 (RLT1), an Arabidopsis thaliana ISWI (AtISWI) and AtDDT-domain protein, respectively, we show that the SLIDE domain of CHR11 and the DDT domain together with an adjacent sequence of RLT1 are responsible for their binding. 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. The SLIDE domain of AtISWI 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.
authors.affiliation: National Laboratory of Plant Molecular Genetics, Institute of Plant Physiology & Ecology, Shanghai Institutes for Biological Sciences, the Chinese Academy of Sciences, Shanghai, 200032, China.
authors.forename: Jiaqiang
authors.initials: J
authors.lastname: Dong
authors.forename: Zheng
authors.initials: Z
authors.lastname: Gao
authors.forename: Shujing
authors.initials: S
authors.lastname: Liu
authors.forename: Guang
authors.initials: G
authors.lastname: Li
authors.forename: Zhongnan
authors.initials: Z
authors.lastname: Yang
authors.forename: Hai
authors.initials: H
authors.lastname: Huang
authors.forename: Lin
authors.initials: L
authors.lastname: Xu
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism*; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000254:growth & development / Q000378:metabolism; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000378:metabolism*; D042002:Chromatin Assembly and Disassembly; D019295:Computational Biology; D017124:Conserved Sequence; D019143:Evolution, Molecular; D006801:Humans; D008969:Molecular Sequence Data; D010641:Phenotype; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D016415:Sequence Alignment; D017384:Sequence Deletion; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D029681:Arabidopsis Proteins; C086468:ISWI protein; D014157:Transcription Factors; D000251:Adenosine Triphosphatases
keywords: Arabidopsis; DDT-domain proteins; Imitation Switch; chromatin remodeling factors; protein interaction