Department of Biochemistry, University of Wisconsin - Madison, 433 Babcock Dr., Madison, WI 53706, USA.
Biochem Biophys Res Commun. 2010 Mar 19;393(4):734-9. doi: 10.1016/j.bbrc.2010.02.070. Epub 2010 Feb 18.
The Arabidopsis dynamin-related protein 1A (AtDRP1A) is involved in endocytosis and cell plate maturation in Arabidopsis. Unlike dynamin, AtDRP1A does not have any recognized membrane binding or protein-protein interaction domains. We report that GTPase active AtDRP1A purified from Escherichia coli as a fusion to maltose binding protein forms homopolymers visible by negative staining electron microscopy. These polymers interact with protein-free liposomes whose lipid composition mimics that of the inner leaflet of the Arabidopsis plasma membrane, suggesting that lipid-binding may play a role in AtDRP1A function. However, AtDRP1A polymers do not appear to assemble and disassemble in a dynamic fashion and do not have the ability to tubulate liposomes in vitro, suggesting that additional factors or modifications are necessary for AtDRP1A's in vivo function.
拟南芥动力蛋白相关蛋白 1A（AtDRP1A）参与拟南芥的内吞作用和细胞板成熟。与动力蛋白不同，AtDRP1A 没有任何公认的膜结合或蛋白质-蛋白质相互作用结构域。我们报告说，从大肠杆菌中作为麦芽糖结合蛋白融合体纯化的 GTP 酶活性 AtDRP1A 通过负染色电子显微镜可见形成同源聚合物。这些聚合物与没有蛋白质的脂质体相互作用，脂质组成模拟拟南芥质膜的内小叶，表明脂质结合可能在 AtDRP1A 功能中起作用。然而，AtDRP1A 聚合物似乎不会以动态方式组装和解体，并且在体外没有使脂质体成管的能力，这表明 AtDRP1A 的体内功能还需要其他因素或修饰。
