B3域
蛋白质结构域
生物
染色质
染色质重塑
表皮生长因子样结构域
拟南芥
环核苷酸结合域
遗传学
拟南芥
细胞生物学
计算生物学
基因
DNA结合蛋白
肽序列
转录因子
突变体
作者
Jiaqiang Dong,Zheng Gao,S. Liu,Guang Li,Zhong‐Nan Yang,Hai Huang,Lin Xu
摘要
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.
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