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首页> 外文期刊>Molecular and Cellular Biology >Identification of a Novel, Intraperoxisomal Pex14-Binding Site in Pex13: Association of Pex13 with the Docking Complex Is Essential for Peroxisomal Matrix Protein Import
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Identification of a Novel, Intraperoxisomal Pex14-Binding Site in Pex13: Association of Pex13 with the Docking Complex Is Essential for Peroxisomal Matrix Protein Import

机译：Pex13中的新型，Intrateroxisomal Pex14结合位点的鉴定：Pex13与对接复合体的关联对于过氧化物酶体基质蛋白的导入是必不可少的。

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The peroxisomal docking complex is a key component of the import machinery for matrix proteins. The core protein of this complex, Pex14, is thought to represent the initial docking site for the import receptors Pex5 and Pex7. Associated with this complex is a fraction of Pex13, another essential component of the import machinery. Here we demonstrate that Pex13 directly binds Pex14 not only via its SH3 domain but also via a novel intraperoxisomal site. Furthermore, we demonstrate that Pex5 also contributes to the association of Pex13 with Pex14. Peroxisome function was affected only mildly by mutations within the novel Pex14 interaction site of Pex13 or by the non-Pex13-interacting mutant Pex5W204A. However, when these constructs were tested in combination, PTS1-dependent import and growth on oleic acid were severely compromised. When the SH3 domain-mediated interaction of Pex13 with Pex14 was blocked on top of that, PTS2-dependent matrix protein import was completely compromised and Pex13 was no longer copurified with the docking complex. We conclude that the association of Pex13 with Pex14 is an essential step in peroxisomal protein import that is enabled by two direct interactions and by one that is mediated by Pex5, a result which indicates a novel, receptor-independent function of Pex5.
机译：过氧化物酶体对接复合物是基质蛋白进口机制的关键组成部分。该复合物的核心蛋白Pex14被认为代表了导入受体Pex5和Pex7的初始对接位点。与这种复合物相关的是Pex13的一部分，Pex13是进口机械的另一个重要组成部分。在这里，我们证明Pex13不仅通过其SH3结构域而且还通过一个新的过氧化物酶体内位点直接结合Pex14。此外，我们证明Pex5也有助于Pex13与Pex14的关联。过氧化物酶体的功能仅受到Pex13新型Pex14相互作用位点内突变或与非Pex13相互作用的突变体Pex5 W204A 的轻微影响。但是，当将这些构建体进行组合测试时，PTS1依赖的进口和在油酸上的生长受到严重损害。最重要的是，当SH3结构域介导的Pex13与Pex14的相互作用被阻断时，PTS2依赖的基质蛋白的导入被完全破坏，Pex13不再与对接复合物共纯化。我们得出的结论是，Pex13与Pex14的结合是过氧化物酶体蛋白输入中必不可少的步骤，该过程由两种直接相互作用以及由Pex5介导的一种相互作用实现，这一结果表明Pex5具有新颖的，受体独立的功能。

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