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Dual targeting and function of a protease in mitochondria and chloroplasts.


ABSTRACT: 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.

SUBMITTER: Bhushan S 

PROVIDER: S-EPMC1326381 | biostudies-literature | 2003 Nov

REPOSITORIES: biostudies-literature

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Dual targeting and function of a protease in mitochondria and chloroplasts.

Bhushan Shashi S   Lefebvre Benoit B   Ståhl Annelie A   Wright Sarah J SJ   Bruce Barry D BD   Boutry Marc M   Glaser Elzbieta E  

EMBO reports 20031024 11


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 G  ...[more]

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