FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
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DOI：
10.1126/science.1132516
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发表时间：
2006-11-03
期刊：
影响因子：
56.9
通讯作者：
Goerlich, Dirk
中科院分区：
文献类型：
--
作者：
Frey, Steffen;Richter, Ralf P.;Goerlich, Dirk
核孔复合体允许与核运输受体结合的货物快速通过，但在其他方面抑制了惰性大分子的核质通量。为了解释这种选择性，提出了一种渗透性屏障的筛子结构，这种结构是通过Phe和富含Gly(FG)的核孔蛋白重复序列之间的可逆交联来创建的。根据这个模型，核转运受体克服了筛子的大小限制，通过竞争性地破坏相邻重复间的接触来催化自己的核孔通道，从而瞬时打开相邻的网状结构。在这里，我们发现苯丙氨酸介导的重复间相互作用确实将FG-重复结构域交联成弹性和可逆水凝胶。此外，我们获得的证据表明，这种水凝胶的形成是酵母生存所必需的。
Nuclear pore complexes permit rapid passage of cargoes bound to nuclear transport receptors, but otherwise suppress nucleocytoplasmic fluxes of inert macromolecules >= 30 kilodaltons. To explain this selectivity, a sieve structure of the permeability barrier has been proposed that is created through reversible cross-linking between Phe and Gly (FG) - rich nucleoporin repeats. According to this model, nuclear transport receptors overcome the size limit of the sieve and catalyze their own nuclear pore-passage by a competitive disruption of adjacent inter-repeat contacts, which transiently opens adjoining meshes. Here, we found that phenylalanine-mediated inter-repeat interactions indeed cross-link FG-repeat domains into elastic and reversible hydrogels. Furthermore, we obtained evidence that such hydrogel formation is required for viability in yeast.