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Dual targeting and function of a protease in mitochondria and chloroplasts

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Bhushan, S Lefebvre, Benoit [UCL] Stahl, A Wright, SJ Bruce, BD Boutry, Marc [UCL] Glaser, E

Here we show, using the green fluorescent protein (GFP) fusion system, that an Arabidopsis thaliana zinc-metalloprotease (AtZn-MP) is targeted to both mitochondria and chloroplasts. A deletion mutant lacking the amino-terminal 28 residues, with translation initiation at the second methionine residue, was imported into chloroplasts only. However, a mutated form of the full-length targeting peptide, in which the second methionine residue is changed to leucine, was imported to both organelles. No GFP fluorescence was detected when a frame-shift mutation was introduced between the first and second ATG codons of the Zn-MP-GFP construct, suggesting no alternative translational initiation. Our results show that the dual targeting of the Zn-MP is due to an ambiguous targeting peptide. Furthermore, we show that the recombinant AtZn-MP degrades mitochondrial and chloroplastic targeting peptides, indicating its function as a signal peptide degrading protease in both mitochondria and chloroplasts.

Document type Article de périodique (Journal article) – Article de recherche
Publication date 2003
Language Anglais
Journal information "EMBO Reports" - Vol. 4, no. 11, p. 1073-1078 (2003)
Peer reviewed yes
Publisher Nature Publishing Group (London)
issn 1469-221X
e-issn 1469-3178
Publication status Publié
Affiliation UCL - AGRO/CABI - Département de chimie appliquée et des bio-industries
Links
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Bibliographic reference Bhushan, S ; Lefebvre, Benoit ; Stahl, A ; Wright, SJ ; Bruce, BD ; et. al. Dual targeting and function of a protease in mitochondria and chloroplasts. In: EMBO Reports, Vol. 4, no. 11, p. 1073-1078 (2003)
Permanent URL http://hdl.handle.net/2078.1/40681