Arabidopsis dynamin-related proteins DRP3A and DRP3B are functionally redundant in mitochondrial fission, but have distinct roles in peroxisomal fission
Arabidopsis dynamin-related proteins DRP3A and DRP3B are functionally redundant in mitochondrial fission, but have distinct roles in peroxisomal fission
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DOI：
10.1111/j.1365-313x.2009.03786.x
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发表时间：
2009-05-01
期刊：
影响因子：
7.2
通讯作者：
Tsutsumi, Nobuhiro
中科院分区：
文献类型：
--
作者：
Fujimoto, Masaru;Arimura, Shin-ichi;Tsutsumi, Nobuhiro
两个类似的拟南芥动力蛋白相关蛋白，DRP 3A和DRP 3B，被认为是线粒体和过氧化物酶体分裂的关键因素。然而，DRP 3A和DRP 3B之间的功能和遗传关系尚未得到充分研究。在酵母双杂交试验中，DRP 3A和DRP 3B相互作用。DRP 3A和DRP 3B定位于线粒体和过氧化物酶体，并在叶表皮细胞中相互共定位。在两个T-DNA插入突变体drp 3a和drp 3b中，线粒体比野生型细胞中的线粒体稍长，数量较少。在双突变体drp 3a/drp 3b中，线粒体相互连接，导致大量延长。DRP 3A或DRP 3B在drp 3a/drp 3b中的过表达恢复了线粒体的颗粒形状，表明DRP 3A和DRP 3B在线粒体分裂中是功能冗余的。在过氧化物酶体分裂的情况下，MRP 3A和MRP 3B似乎具有不同的功能：drp 3a中的过氧化物酶体比野生型中的过氧化物酶体更大且数量更少，而drp 3b中的过氧化物酶体与野生型中的过氧化物酶体一样大且数量一样多，drp 3a/drp 3b中的过氧化物酶体与drp 3a中的一样大且数量一样多。虽然DRP 3A在drp 3a/drp 3b中的过表达恢复了过氧化物酶体的形状和数量，但DRP 3B的过表达并没有恢复表型，而是经常引起伸长。这些结果表明，DRP 3B和DRP 3A在线粒体分裂中具有冗余的分子功能，而DRP 3B在过氧化物酶体分裂中具有与DRP 3A不同的次要作用。
Two similar Arabidopsis dynamin-related proteins, DRP3A and DRP3B, are thought to be key factors in both mitochondrial and peroxisomal fission. However, the functional and genetic relationships between DRP3A and DRP3B have not been fully investigated. In a yeast two-hybrid assay, DRP3A and DRP3B interacted with themselves and with each other. DRP3A and DRP3B localized to mitochondria and peroxisomes, and co-localized with each other in leaf epidermal cells. In two T-DNA insertion mutants, drp3a and drp3b, the mitochondria are a little longer and fewer in number than those in the wild-type cells. In the double mutant, drp3a/drp3b, mitochondria are connected to each other, resulting in massive elongation. Overexpression of either DRP3A or DRP3B in drp3a/drp3b restored the particle shape of mitochondria, suggesting that DRP3A and DRP3B are functionally redundant in mitochondrial fission. In the case of peroxisomal fission, DRP3A and DRP3B appear to have different functions: peroxisomes in drp3a were larger and fewer in number than those in the wild type, whereas peroxisomes in drp3b were as large and as numerous as those in the wild type, and peroxisomes in drp3a/drp3b were as large and as numerous as those in drp3a. Although overexpression of DRP3A in drp3a/drp3b restored the shape and number of peroxisomes, overexpression of DRP3B did not restore the phenotypes, and often caused elongation instead. These results suggest that DRP3B and DRP3A have redundant molecular functions in mitochondrial fission, whereas DRP3B has a minor role in peroxisomal fission that is distinct from that of DRP3A.