Department of Botany and Plant Biology, University of Geneva, Chemin des Embrouchis 10, 1254, Jussy, Geneva, Switzerland.
Curr Microbiol. 2011 Jul;63(1):100-5. doi: 10.1007/s00284-011-9954-9. Epub 2011 May 20.
α-Actinin, an actin-binding protein of the spectrin superfamily, is present in most eukaryotes except plants. It is composed of three domains: N-terminal CH-domains, C-terminal calcium-binding domain (with EF-hand motifs), and a central rod domain. We have cloned and expressed Neurospora crassa α-actinin as GST and GFP fusion proteins for biochemical characterization and in vivo localization, respectively. The intracellular localization pattern of α-actinin suggests that this protein is intimately associated with actin filaments and plays an important role in the processes of germination, hyphal elongation, septum formation, and conidiation. These functions were confirmed by the experiments on the effect of α-actinin gene deletion in N. crassa.
α-辅肌动蛋白是 spectrin 超家族的一种肌动蛋白结合蛋白，存在于大多数真核生物中，除了植物。它由三个结构域组成：N 端 CH 结构域、C 端钙结合结构域（具有 EF 手型基序）和中心杆状结构域。我们已经克隆并表达了粗糙脉孢菌 α-辅肌动蛋白作为 GST 和 GFP 融合蛋白，分别用于生化特性分析和体内定位。α-辅肌动蛋白的细胞内定位模式表明，该蛋白与肌动蛋白丝密切相关，在萌发、菌丝伸长、隔膜形成和分生孢子形成等过程中发挥重要作用。这些功能通过在粗糙脉孢菌中进行α-辅肌动蛋白基因缺失实验得到了证实。
