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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >WD40 protein Mda1 is purified with Dnm1 and forms a dividing ring for mitochondria before Dnm1 in Cyanidioschyzon merolae
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WD40 protein Mda1 is purified with Dnm1 and forms a dividing ring for mitochondria before Dnm1 in Cyanidioschyzon merolae

机译：WD40蛋白Mda1用Dnm1纯化，并在Cyanidioschyzon merolae中的Dnm1之前形成线粒体的分隔环

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Mitochondria are not produced de novo but are maintained by division. Mitochondrial division is a coordinated process of positioning and constriction of the division site and fission of double membranes, in which dynamin-related protein is believed to mediate outer membrane fission. Part of the mitochondrial division machinery was purified from M phase-arrested Cyanidioschyzon merolae cells through biochemical fractionation. The dynamin-related protein Dnm1 was one of the two major proteins in the purified fraction and was accompanied by a newly identified protein CMR185C, named Mda1. Mda1 contained a predictable coiled-coil region and WD40 repeats, similarly to Mdv1 and Caf4 in yeasts. Immunofluorescence and immunoelectron microscopy showed that Mda1 localizes as a medial belt or ring on the mitochondrial outer surface throughout the division. The ring formation of Mda1 followed the plane of the ring of FtsZ, a protein that resides in the matrix. Dnm1 consistently colocalized with Mda1 only in the late stages of division. Mda1 protein was expressed through S to M phases and was phosphorylated specifically in M phase when Mda1 transformed from belt into foci and became colocalizing with Dnm1. Dephosphorylation of Mda1 in vitro increased its sedimentation coefficient, suggesting conformational changes of the macromolecule. Disassembly of the purified mitochondrial division machinery was performed by adding GTP to independently release Dnm1, suggesting that Mda1 forms a stable homo-oligomer by itself as a core structure of the mitochondrial division machinery.
机译：线粒体不是从头产生的，而是由分裂维持的。线粒体分裂是分裂位点的定位和收缩以及双膜裂变的协调过程，其中动力蛋白相关蛋白被认为介导外膜裂变。通过生化分级分离，从M期停滞的Cyanidioschyzon merolae细胞中纯化了部分线粒体分裂机制。与动力蛋白有关的蛋白质Dnm1是纯化级分中的两个主要蛋白质之一，并伴有一个新发现的蛋白质CMR185C，名为Mda1。 Mda1包含一个可预测的卷曲螺旋区域和WD40重复序列，类似于酵母中的Mdv1和Caf4。免疫荧光和免疫电子显微镜检查显示，Mda1在整个分裂过程中定位为线带或外环的中间带或环。 Mda1的环形成遵循FtsZ环的平面，FtsZ是一种驻留在基质中的蛋白质。仅在分裂后期，Dnm1与Mda1始终共定位。 Mda1蛋白通过S到M期表达，当Mda1从皮带转变为病灶并与Dnm1共定位时，Mda1蛋白在M期特异性磷酸化。 Mda1的体外去磷酸化增加了其沉降系数，表明大分子的构象变化。通过添加GTP来独立释放Dnm1，进行了纯化的线粒体分裂机制的拆卸，这表明Mda1本身作为线粒体分裂机制的核心结构形成了稳定的均聚物。

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