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The two domains of cotton WLIMla protein are functionally divergent
by
Libo Han Yuanbao Li Yongduo Sun Haiyun Wang Zhaosheng Kong GuixianXia
in
a蛋白
/ DNA结合活性
/ LIM结构域
/ 棉纤维发育
/ 棉花
/ 红色荧光蛋白
/ 纤维伸长
/ 肌动蛋白结合蛋白
2016
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The two domains of cotton WLIMla protein are functionally divergent
by
Libo Han Yuanbao Li Yongduo Sun Haiyun Wang Zhaosheng Kong GuixianXia
in
a蛋白
/ DNA结合活性
/ LIM结构域
/ 棉纤维发育
/ 棉花
/ 红色荧光蛋白
/ 纤维伸长
/ 肌动蛋白结合蛋白
2016
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The two domains of cotton WLIMla protein are functionally divergent
Journal Article
The two domains of cotton WLIMla protein are functionally divergent
2016
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Overview
Our previous study demonstrated that WLIMla has dual roles in fiber elongation and secondary cell wall synthesis in upland cotton, and the protein acts either as an actin-binding protein or as a transcription factor. Because WLIMla consists of two different LIM domains, it is possible that these elements contribute differentially to the dual functions of the protein. In this study, we dissected the two LIM domains and characterized their biochemical functions. By using red fluorescent protein (RFP) fusion, co-sedimentation, and DNA binding methods, we found that the two domains of WLIM 1 a, domain 1 (D 1) and domain2 (D2), possessed different biochemical properties. While D1 contributed primarily to the actin filament-bundling activity of WLIMla, D2 contributed to the DNA-binding activity of the protein; both D1 and D2 relied on a linker sequence for their ac- tivities. In addition, we found that WLIMla and its two LIM domains form dimers in vitro. These results may lead to a better understanding of the molecular mechanisms of dual functions of WLIMla during cotton fiber development.
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