前体蛋白被Toc复合体识别。
Preprotein recognition by the Toc complex.
作者信息
Becker Thomas, Jelic Marko, Vojta Aleksandar, Radunz Alfons, Soll Jürgen, Schleiff Enrico
机构信息
Botanik, LMU München, Germany.
出版信息
EMBO J. 2004 Feb 11;23(3):520-30. doi: 10.1038/sj.emboj.7600089. Epub 2004 Feb 5.
Abstract
The Toc core complex consists of the pore-forming Toc75 and the GTPases Toc159 and Toc34. We confirm that the receptor form of Toc159 is integrated into the membrane. The association of Toc34 to Toc75/Toc159 is GTP dependent and enhanced by preprotein interaction. The N-terminal half of the pSSU transit peptide interacts with high affinity with Toc159, whereas the C-terminal part stimulates its GTP hydrolysis. The phosphorylated C-terminal peptide of pSSU interacts strongly with Toc34 and therefore inhibits binding and translocation of pSSU into Toc proteoliposomes. In contrast, Toc159 recognises only the dephosphorylated forms. The N-terminal part of the pSSU presequence does not influence binding to the Toc complex, but is able to block import into proteoliposomes through its interaction with Toc159. We developed a model of differential presequence recognition by Toc34 and Toc159.
摘要
Toc核心复合体由形成孔道的Toc75以及GTP酶Toc159和Toc34组成。我们证实Toc159的受体形式整合到了膜中。Toc34与Toc75/Toc159的结合依赖于GTP，并且前体蛋白的相互作用会增强这种结合。pSSU转运肽的N端一半与Toc159具有高亲和力相互作用，而C端部分则刺激其GTP水解。pSSU的磷酸化C端肽与Toc34强烈相互作用，因此抑制pSSU与Toc蛋白脂质体的结合和转运。相反，Toc159只识别去磷酸化形式。pSSU前导序列的N端部分不影响与Toc复合体的结合，但能够通过与Toc159的相互作用阻断向蛋白脂质体的导入。我们建立了一个Toc34和Toc159对前导序列进行差异识别的模型。
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