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SLIDE, the Protein Interacting Domain of imitation switch Remodelers, Binds DDT-Domain Proteins of Different Subfamilies in Chromatin Remodeling Complexes

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Journal of Integrative Plant Biology 2013年第10期55卷 928-937页

作者： Jiaqiang Dong Zheng Gao Shujing Liu Guang Li Zhongnan Yang Hai Huang Lin Xu National Laboratory of Plant Molecular Genetics Institute of Plant Physiology & Ecology Shanghai Institutes for Biological Sciences the Chinese Academy of Sciences College of Life and Environment Sciences Shanghai Normal University

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 （CH R11） and RINGLET1 （RLT1）, an Arabidopsis thaliana ISWI （AtlSWI） 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 AtlSWI 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.

关键词： Arabidopsis chromatin remodeling factors DDT-domain proteins imitation switch protein interaction.

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