Structural Basis of Interaction of Bipartite Nuclear Localization Signal from Agrobacterium VirD2 with Rice Importin-o  

出　　处：《Molecular Plant》2014年第6期1061-1064,共4页分子植物（英文版）

摘　　要：Dear Editor, In the eukaryotic cell, the nuclear envelope separates genomic DNA from the rest of the cell, but ensures a molecu- lar communication between the nucleus and the cytoplasm through the nuclear pore complexes （NPCs）. Nuclear trans- port of macromolecules is an energy-dependent process, exemplified by the classical nuclear import pathway. In the cytoplasm, proteins containing classical nuclear localization signals （cNLSs） are recognized by a hetero-dimeric transport receptor （importin-α （Impα）：importin-β （Impl3） complex）. Impa is employed as an adaptor protein that specifically rec-ognizes the classical nuclear localization signal （cNLS） from the cargo protein （Marfori et al., 2011）. Translocation of the trimeric cargo：transport receptor import complex through the NPCs is mediated by transient interactions between Impβ and nucleoporins in the NPC. The directionality of the trans- port is imparted by the asymmetric distribution, between the cytoplasm and the nucleus, of the distinct nucleotide-bound （GTP/GDP） states of the small GTPase Ran （Tran et al., 2007）.Dear Editor, In the eukaryotic cell, the nuclear envelope separates genomic DNA from the rest of the cell, but ensures a molecu- lar communication between the nucleus and the cytoplasm through the nuclear pore complexes （NPCs）. Nuclear trans- port of macromolecules is an energy-dependent process, exemplified by the classical nuclear import pathway. In the cytoplasm, proteins containing classical nuclear localization signals （cNLSs） are recognized by a hetero-dimeric transport receptor （importin-α （Impα）：importin-β （Impl3） complex）. Impa is employed as an adaptor protein that specifically rec-ognizes the classical nuclear localization signal （cNLS） from the cargo protein （Marfori et al., 2011）. Translocation of the trimeric cargo：transport receptor import complex through the NPCs is mediated by transient interactions between Impβ and nucleoporins in the NPC. The directionality of the trans- port is imparted by the asymmetric distribution, between the cytoplasm and the nucleus, of the distinct nucleotide-bound （GTP/GDP） states of the small GTPase Ran （Tran et al., 2007）.

分 类 号：Q26[生物学—细胞生物学] Q510.3