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SLIDE , The Protein Interacting Domain of Imitation Switch Remodelers, Binds DDT ‐ D omain Proteins of Different Subfamilies in Chromatin Remodeling Complexes
Author(s) -
Dong Jiaqiang,
Gao Zheng,
Liu Shujing,
Li Guang,
Yang Zhongnan,
Huang Hai,
Xu Lin
Publication year - 2013
Publication title -
journal of integrative plant biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.734
H-Index - 83
eISSN - 1744-7909
pISSN - 1672-9072
DOI - 10.1111/jipb.12069
Subject(s) - protein domain , chromatin , chromatin remodeling , egf like domain , b3 domain , biology , arabidopsis , microbiology and biotechnology , genetics , dna binding protein , gene , transcription factor , mutant
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.