The role of the N-terminal domain of chloroplast targeting peptides in organellar protein import and miss-sorting
The role of the N-terminal domain of chloroplast targeting peptides in organellar protein import and miss-sorting
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DOI：
10.1016/j.febslet.2006.06.018
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发表时间：
2006-07-10
期刊：
影响因子：
3.5
通讯作者：
Glaser, Elzbieta
中科院分区：
文献类型：
--
作者：
Bhushan, Shashi;Kuhn, Claus;Glaser, Elzbieta
我们分析了拟南芥细胞器蛋白质组中发现的385条线粒体和567条叶绿体信号序列。尽管总体上有相似之处，但转运肽的前16个残基明显不同。为了验证N端截短的转运肽将叶绿体前体蛋白重定向到线粒体的假设，我们研究了Elip、PETC和Lhcb2.1的N端缺失突变体的导入。结果表明，缺失突变体既没有导入叶绿体，也没有在体外和体内错过线粒体的靶向，表明整个转运肽是正确靶向和错分所必需的。(C)2006年欧洲生化学会联合会。爱思唯尔出版，版权所有。
We have analysed 385 mitochondrial and 567 chloroplastic signal sequences of proteins found in the organellar proteomes of Arabidopsis thaliana. Despite overall similarities, the first 16 residues of transit peptides differ remarkably. To test the hypothesis that the N-terminally truncated transit peptides would redirect chloroplastic precursor proteins to mitochondria, we studied import of the N-terminal deletion mutants of ELIP, PetC and Lhcb2.1. The results show that the deletion mutants were neither imported into chloroplasts nor miss-targeted to mitochondria in vitro and in vivo, showing that the entire transit peptide is necessary for correct targeting as well as miss-sorting. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.