您好，欢迎访问浙江省农业科学院 机构知识库！
浙江省农业科学院机构知识库

全部

  • 全部
  • 标题
  • 学者
  • 机构
  • 关键词

BENT UPPERMOST INTERNODE1 Encodes the Class II Formin FH5 Crucial for Actin Organization and Rice Development

文献类型： 外文期刊

作者： Yang, Weibing 1 ; Ren, Sulin 2 ; Zhang, Xiaoming 3 ; Gao, Mingjun 1 ; Ye, Shenghai; Qi, Yongbin; Zheng, Yiyan 2 ; W 1 ;

作者机构： 1.Chinese Acad Sci, Inst Plant Physiol & Ecol, Natl Key Lab Plant Mol Genet, Shanghai 200032, Peoples R China

2.Chinese Acad Sci, Inst Bot, Key Lab Photosynth & Environm Mol Physiol, Beijing 100093, Peoples R China

3.Zhejiang Acad Agr Sci, State Key Lab Breeding Base Zhejiang Sus

关键词： actin cytoskeleton;phosphatase: 9013-05-2;tensin: 265992-04-9;formin: 174882-62-3;class II formin;FH5;morphogenesis;spatial organization;cell expansion;pleiotropic phenotype;plant dwarfism

期刊名称：PLANT CELL （ 影响因子：11.277； 五年影响因子：12.061 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： The actin cytoskeleton is an important regulator of cell expansion and morphogenesis in plants. However, the molecular mechanisms linking the actin cytoskeleton to these processes remain largely unknown. Here, we report the functional analysis of rice (Oryza sativa) FH5/BENT UPPERMOST INTERNODE1 (BUI1), which encodes a formin-type actin nucleation factor and affects cell expansion and plant morphogenesis in rice. The bui1 mutant displayed pleiotropic phenotypes, including bent uppermost internode, dwarfism, wavy panicle rachis, and enhanced gravitropic response. Cytological observation indicated that the growth defects of bui1 were caused mainly by inhibition of cell expansion. Map-based cloning revealed that BUI1 encodes the class II formin FH5. FH5 contains a phosphatase tensin-like domain at its amino terminus and two highly conserved formin-homology domains, FH1 and FH2. In vitro biochemical analyses indicated that FH5 is capable of nucleating actin assembly from free or profilin-bound monomeric actin. FH5 also interacts with the barbed end of actin filaments and prevents the addition and loss of actin subunits from the same end. Interestingly, the FH2 domain of FH5 could bundle actin filaments directly and stabilize actin filaments in vitro. Consistent with these in vitro biochemical activities of FH5/BUI1, the amount of filamentous actin decreased, and the longitudinal actin cables almost disappeared in bui1 cells. The FH2 or FH1FH2 domains of FH5 could also bind to and bundle microtubules in vitro. Thus, our study identified a rice formin protein that regulates de novo actin nucleation and spatial organization of the actin filaments, which are important for proper cell expansion and rice morphogenesis.

  • 相关文献

[1]OsGLU3, a Putative Membrane-Bound Endo-1,4-Beta-Glucanase, Is Required for Root Cell Elongation and Division in Rice (Oryza sativa L.). Zhang, Jin-Wei,Xu, Lei,Wu, Yun-Rong,Chen, Xin-Ai,Liu, Yu,Wu, Ping,Yi, Ke-Ke,Zhu, Shi-Hua,Ding, Wo-Na,Yi, Ke-Ke.

[2]WIDE AND THICK GRAIN 1, which encodes an otubain-like protease with deubiquitination activity, influences grain size and shape in rice. Huang, Ke,Duan, Penggen,Zhang, Baolan,Xu, Ran,Li, Na,Li, Yunhai,Huang, Ke,Wang, Dekai.

作者其他论文 更多>>
置顶
购物车
反馈

© 京ICP备09089781号-29 主办单位：浙江省农业科学院

学术资源： 中国农业科学院 农业专业知识服务系统 农科联盟资源共建共享平台 中国农业科技文献与信息服务平台 中国农业期刊集成服务平台