Targeting of bacterial chloramphenicol acetyltransferase to mitochondria in transgenic plants

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

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Pages (from-to)340-342
Number of pages3
JournalNature
Volume328
Issue number6128
DOIs
Publication statusPublished - 23 Jul 1987

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