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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Cp1 -dependent Partitioning Of Pretransfer And Posttransfer Editing In Leucyl-trna Synthetase
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Cp1 -dependent Partitioning Of Pretransfer And Posttransfer Editing In Leucyl-trna Synthetase

机译：亮氨酸合成酶中Cp1依赖的转移前和转移后编辑的分区

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摘要

Mistranslation is toxic to bacterial and mammalian cells and can lead to neurodegeneration in the mouse. Mistranslation is caused by the attachment of the wrong amino acid to a specific tRNA. Many aminoacyl-tRNA synthetases have an editing activity that deacylates the mischarged amino acid before capture by the elongation factor and transport to the ribosome. For class I tRNA synthetases, the editing activity is encoded by the CP1 domain, which is distinct from the active site for aminoacylation. What is not clear is whether the enzymes also have an editing activity that is separable from CP1. A point mutation in CP1 of class I leucyl-tRNA synthetase inactivates deacylase activity and produces misacylated tRNA. In contrast, although deletion of the entire CP1 domain also disabled the deacylase activity, the deletion-bearing enzyme produced no mischarged tRNA. Further investigation showed that a second tRNA-dependent activity prevented misacylation and is intrinsic to the active site for aminoacylation.
机译：误翻译对细菌和哺乳动物细胞有毒，可导致小鼠神经退行性变。误翻译是由于错误的氨基酸附着到特定的tRNA引起的。许多氨酰基-tRNA合成酶具有编辑活性，可在被延伸因子捕获并转运到核糖体之前使带错电荷的氨基酸脱酰基。对于I类tRNA合成，编辑活性由CP1域编码，该域与氨基酰化的活性位点不同。还不清楚这些酶是否还具有可与CP1分离的编辑活性。 I类亮氨酰-tRNA合成酶CP1中的点突变使去酰基化酶活性失活并产生错误的tRNA。相反，尽管整个CP1结构域的缺失也使脱酰基酶活性丧失，但带有缺失的酶没有产生带错电荷的tRNA。进一步的研究表明，第二种依赖tRNA的活性可防止误酰化作用，并且是氨酰化活性位点所固有的。

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