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Prediction of structural domains of TAP reveals details of its interaction with p15 and nucleoporins

机译:TAP结构域的预测揭示了其与p15和核孔蛋白相互作用的细节

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摘要

Vertebrate TAP is a nuclear mRNA export factor homologous to yeast Mex67p. The middle domain of TAP binds directly to p15, a protein related to the nuclear transport factor 2 (NTF2), whereas its C-terminal domain interacts with various nucleoporins, the components of the nuclear pore complex (NPC). Here, we report that the middle domain of TAP is also similar to NTF2, as well as to regions in Ras-GAP SH3 domain binding protein (G3BP) and some plant protein kinases. Based on the known three-dimensional structure of NTF2 homodimer, a heterodimerization model of TAP and p15 could be inferred. This model was confirmed by site-directed mutagenesis of residues located at the dimer interface. Furthermore, the C-terminus of TAP was found to contain a ubiquitin-associated (UBA) domain. By site-directed mutagenesis we show that a conserved loop in this domain plays an essential role in mediating TAP–nucleoporin interaction.
机译:脊椎动物TAP是与酵母Mex67p同源的核mRNA输出因子。 TAP的中间结构域直接与p15结合,该蛋白与核转运因子2(NTF2)相关,而其C端结构域则与各种核孔蛋白(核孔复合物(NPC)的组成部分)相互作用。在这里,我们报道TAP的中间域也类似于NTF2,以及Ras-GAP SH3域结合蛋白(G3BP)和某些植物蛋白激酶中的区域。基于已知的NTF2同型二聚体的三维结构,可以推断出TAP和p15的异源二聚化模型。通过对位于二聚体界面的残基进行定点诱变证实了该模型。此外,发现TAP的C端含有泛素相关(UBA)结构域。通过定点诱变,我们表明该域中的保守环在介导TAP-核孔蛋白相互作用中起着至关重要的作用。

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