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最小核孔复合体定义了转运所必需的FG重复结构域。

Minimal nuclear pore complexes define FG repeat domains essential for transport.

作者信息

Strawn Lisa A, Shen Tianxiang, Shulga Nataliya, Goldfarb David S, Wente Susan R

机构信息

Department of Cell and Developmental Biology, Vanderbilt University Medical Center, 3120A MRBIII, 465 21st Avenue South, Nashville, TN 37232-8240, USA.

出版信息

Nat Cell Biol. 2004 Mar;6(3):197-206. doi: 10.1038/ncb1097. Epub 2004 Feb 22.

DOI:10.1038/ncb1097
PMID:15039779
Abstract

Translocation through nuclear pore complexes (NPCs) requires interactions between receptor-cargo complexes and phenylalanine-glycine (FG) repeats in multiple FG domain-containing NPC proteins (FG-Nups). We have systematically deleted the FG domains of 11 Saccharomyces cerevisiae FG-Nups in various combinations. All five asymmetrically localized FG domains deleted together were non-essential. However, specific combinations of symmetrically localized FG domains were essential. Over half the total mass of FG domains could be deleted without loss of viability or the NPC's normal permeability barrier. Significantly, symmetric deletions caused mild reductions in Kap95-Kap60-mediated import rates, but virtually abolished Kap104 import. These results suggest the existence of multiple translocation pathways.

摘要

通过核孔复合体(NPC)的转运需要受体-货物复合体与多种含FG结构域的NPC蛋白(FG-Nups)中的苯丙氨酸-甘氨酸(FG)重复序列之间的相互作用。我们已经系统地以各种组合方式删除了11种酿酒酵母FG-Nups的FG结构域。一起删除的所有五个不对称定位的FG结构域并非必需。然而,对称定位的FG结构域的特定组合是必需的。在不丧失活力或NPC正常通透屏障的情况下,可以删除超过一半的FG结构域总质量。值得注意的是,对称缺失导致Kap95-Kap60介导的导入速率略有降低,但实际上消除了Kap104的导入。这些结果表明存在多种转运途径。

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Minimal nuclear pore complexes define FG repeat domains essential for transport.最小核孔复合体定义了转运所必需的FG重复结构域。
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