CLEAVAGE-SITE MOTIFS IN MITOCHONDRIAL TARGETING PEPTIDES

CLEAVAGE-SITE MOTIFS IN MITOCHONDRIAL TARGETING PEPTIDES
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DOI:
10.1093/protein/4.1.33
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发表时间:
1990-10-01
期刊:
PROTEIN ENGINEERING
影响因子:
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通讯作者:
VONHEIJNE, G
VONHEIJNE, G
中科院分区:
其他
文献类型:
--
作者:
GAVEL, Y;VONHEIJNE, G

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尽管线粒体靶向肽缺乏共同的共有序列,但最近发现氨基酸的位置分布存在一定的偏差。这些模式似乎与基质加工蛋白酶对前体蛋白的切割有关。我们扩展了之前的研究,发现了线粒体靶向肽亚组中保守的新序列基序。这些基序具有某些共同的主题,表明它们与一种蛋白酶的切割有关。两个保守模式具有很高的预测价值,但即使对于不具有这些模式的序列,也可以对切割位点进行相当准确的预测。我们还建议,可以使用保守的 RXY.dwnarw.(S/A) 模式将有效识别的切割位点设计成未切割的或人工线粒体靶向肽。
Although mithochondrial targeting peptides lack a common consensus sequence, a certain bias in the positional distribution of amino acids has recently been found. These patterns seem to be associated with cleavage of the precursor proteins by matrix processing protease. We have extended the previous studies and found new sequence motifs that are conserved within subgroups of mitochondrial targeting peptides. These motifs have certain common themes, indicating that they are associated with cleavage by one single protease. Two of the conserved patterns have a high predictive value, but even for sequences that do not possess these patterns, a fairly accurate prediction of the cleavage site is shown to be possible. We also suggest that a well-conserved RXY.dwnarw.(S/A) pattern may be used to engineer efficiently recognized cleavage sites into uncleaved or artificial mitochondrial targeting peptides.