Dual Targeting of a Processing Peptidase into Both Endosymbiotic Organelles Mediated by a Transport Signal of Unusual Architecture

被引:18
作者
Baudisch, Bianca [1 ]
Kloesgen, Ralf Bernd [1 ]
机构
[1] Univ Halle Wittenberg, Inst Biol Plant Physiol, D-06120 Halle, Germany
关键词
Protein transport; dual targeting; mitochondria; chloroplasts; mitochondrial processing peptidase; MITOCHONDRIAL PROTEIN IMPORT; PEA GLUTATHIONE-REDUCTASE; TRANSFER-RNA SYNTHETASES; IN-VITRO; PRECURSOR PROTEINS; YEAST MITOCHONDRIA; BETA-SUBUNIT; ARABIDOPSIS; COMPLEX; CHLOROPLASTS;
D O I
10.1093/mp/ssr092
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
As a result of the endosymbiotic gene transfer, the majority of proteins of mitochondria and chloroplasts are encoded in the nucleus and synthesized in the cytosol as precursor proteins carrying N-terminal transport signals for the 're-import' into the respective target organelle. Most of these transport signals are monospecific, although some of them have dual targeting properties, that is, they are recognized both by mitochondria and by chloroplasts as target organelles. We have identified alpha-MPP2, one of the two isoforms of the substrate binding subunit of mitochondrial processing peptidase of Arabidopsis thaliana, as a novel member of this class of nuclear-encoded organelle proteins. As demonstrated by in organello transport experiments with isolated organelles and by in vivo localization studies employing fluorescent chimeric reporter proteins, the N-terminal region of the alpha-MPP2 precursor comprises transport signals for the import into mitochondria as well as into chloroplasts. Both signals are found within the N-terminal 79 residues of the precursor protein, where they occupy partly separated and partly overlapping regions. Deletion mapping combined with in organello and in vivo protein transport studies demonstrate an unusual architecture of this transport signal, suggesting a composition of three functionally separated domains.
引用
收藏
页码:494 / 503
页数:10
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