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首页> 外文期刊>FEBS Open Bio >Interaction of the dual targeting peptide of Thr-tRNA synthetase with the chloroplastic receptor Toc34 in Arabidopsis thaliana
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Interaction of the dual targeting peptide of Thr-tRNA synthetase with the chloroplastic receptor Toc34 in Arabidopsis thaliana

机译：Thr-tRNA合成酶的双重靶向肽与拟南芥中叶绿体受体Toc34的相互作用

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Organellar proteins synthesized in the cytosol are usually selective for only one destination in a cell but some proteins are localized in more than one compartment, for example in both mitochondria and chloroplasts. The mechanism of dual targeting of proteins to mitochondria and chloroplasts is yet poorly understood. Previously, we observed that the dual targeting peptide of threonyl-tRNA synthetase in Arabidopsis thaliana (AtThrRS-dTP) interacts with the mitochondrial receptor AtTom20 mainly through its N-terminal part. Here we report on the interaction of AtThrRS-dTP with the chloroplastic receptor AtToc34, presenting for the first time the mode of interactions of a dual targeting peptide with both Tom20 and Toc34. By NMR spectroscopy we investigated changes in ^1^5N HSQC spectra of AtThrRS-dTP as a function of AtToc34 concentration. Line broadening shows that the interaction with AtToc34 involves residues along the entire sequence, which is not the case for AtTom20. The N-terminal @f@g@g@f@f motif, which plays an important role in AtTom20 recognition, shows no specificity for AtToc34. These results are supported by import competition studies into both mitochondria and chloroplasts, in which the effect of peptides corresponding to different segments of AtThrRS-dTP on in vitro import of organelle specific proteins was examined. This demonstrates that the N-terminal A2-Y29 segment of AtThrRS-dTP is essential for import into both organelles, while the C-terminal L30-P60 part is important for chloroplastic import efficiency. In conclusion, we have demonstrated that the recognition of the dual targeting peptide of AtThr-tRNA synthetase is different for the mitochondrial and chloroplastic receptors.
机译：在细胞质中合成的细胞器蛋白通常仅对细胞中的一个目的地具有选择性，但是某些蛋白位于一个以上的区域，例如线粒体和叶绿体中。蛋白质对线粒体和叶绿体双重靶向的机制仍知之甚少。以前，我们观察到拟南芥中苏氨酸-tRNA合成酶的双重靶向肽（AtThrRS-dTP）主要通过其N末端部分与线粒体受体AtTom20相互作用。在这里，我们报告了AtThrRS-dTP与叶绿体受体AtToc34的相互作用，这首次提出了双重靶向肽与Tom20和Toc34相互作用的模式。通过NMR光谱，我们研究了AtThrRS-dTP的^ 1 ^ 5N HSQC光谱随AtToc34浓度的变化。线变宽表明与AtToc34的相互作用涉及整个序列中的残基，而AtTom20并非如此。在AtTom20识别中起重要作用的N末端@ f @ g @ g @ f @ f基序对AtToc34没有特异性。这些结果得到线粒体和叶绿体进口竞争研究的支持，其中研究了与AtThrRS-dTP的不同片段相对应的肽对细胞器特异性蛋白的体外进口的影响。这表明AtThrRS-dTP的N末端A2-Y29片段对于导入两个细胞器都是必不可少的，而C末端的L30-P60部分对于提高叶绿体的导入效率很重要。总之，我们已经证明，对于线粒体和叶绿体受体，AtThr-tRNA合成酶的双重靶向肽的识别是不同的。

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