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Two novel metalloendopeptidases in  Arabidopsis thaliana ,  At PreP1 and  At PreP2, are responsible for the degradation of targeting peptides in mitochondria and chloroplasts. Both  At PreP1 and  At PreP2 contain ambiguous targeting peptides and are dually targeted to both organelles. The proteases also have the capacity to degrade unstructured peptides of up to 65 amino acid residues, but not small proteins. The catalysis occurs in a huge catalytic chamber revealed by the crystal structure of  At PreP1 at 2.1 Å. The enzymes show a preference for basic and small uncharged amino acids or serines at the cleavage sites. Despite similarities in cleavage specificities, cleavage-site recognition differs for both proteases and is context- and structure-dependent. The  At PreP1 and  At PreP2 genes are differentially expressed in  Arabidopsis .

Two novel mitochondrial and chloroplastic targeting-peptide-degrading peptidasomes in A. thaliana , At PreP1 and At PreP2