Targeting of bacterial chloramphenicol acetyltransferase to mitochondria in transgenic plants View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1987-07

AUTHORS

Marc Boutry, Ferenc Nagy, Carsten Poulsen, Kazuko Aoyagi, Nam-Hai Chua

ABSTRACT

Most mitochondrial proteins are encoded by nuclear genes and are synthesized as precursors containing a presequence at the N terminus. In yeast and in mammalian cells, the function of the presequence in mitochondrial targeting has been revealed by chimaeric gene studies. Fusion of a mitochondrial presequence to a foreign protein coding sequence enables the protein to be imported into mitochondria in vitro as well as in vivo. Whether plant mitochondrial presequences function in the same way has been unknown. We have previously isolated and characterized a nuclear gene (atp2-1) from Nicotiana plumbaginifolia that encodes the beta-subunit of the mitochondrial ATP synthase. We have constructed a chimaeric gene comprising a putative atp2-1 presequence fused to the bacterial chloramphenicol acetyltransferase (CAT) coding sequence and introduced it into the tobacco genome. We report here that a segment of 90 amino acids of the N terminus of the beta-subunit precursor is sufficient for the specific targeting of the CAT protein to mitochondria in transgenic plants. Our results demonstrate a high specificity for organelle targeting in plant cells. More... »

PAGES

340-342

Journal

TITLE

Nature

ISSUE

6128

VOLUME

328

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/328340a0

    DOI

    http://dx.doi.org/10.1038/328340a0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1051691717

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/3474528


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