Two novel mitochondrial and chloroplastic targeting-peptide-degrading peptidasomes in A. thaliana, AtPreP1 and AtPreP2
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Elzbieta Glaser
Abstract
Two novel metalloendopeptidases in Arabidopsis thaliana, AtPreP1 and AtPreP2, are responsible for the degradation of targeting peptides in mitochondria and chloroplasts. Both AtPreP1 and AtPreP2 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 AtPreP1 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 AtPreP1 and AtPreP2 genes are differentially expressed in Arabidopsis.
References
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©2006 by Walter de Gruyter Berlin New York
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Artikel in diesem Heft
- Highlight: Redox signaling – mechanisms and biological impact
- Paper of the Year 2005: Award to Vanessa Ferreira Merino
- Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism
- Hypoxia and lipid signaling
- Glutathione peroxidases and redox-regulated transcription factors
- Redox regulation of the hypoxia-inducible factor
- The l-arginine nitric oxide pathway: avenue for a multiple-level approach to assess vascular function
- Protein oxidation and proteolysis
- Mitochondrial signaling, TOR, and life span
- Pathogenetic interplay between osmotic and oxidative stress: the hepatic encephalopathy paradigm
- Regulation of redox-sensitive exofacial protein thiols in CHO cells
- N-Ethylmaleimide-sensitive factor: a redox sensor in exocytosis
- Aspects of the biological redox chemistry of cysteine: from simple redox responses to sophisticated signalling pathways
- Singlet oxygen inactivates protein tyrosine phosphatase-1B by oxidation of the active site cysteine
- Regulatory effects of the mitochondrial energetic status on mitochondrial p66Shc
- Air pollution-associated fly ash particles induce fibrotic mechanisms in primary fibroblasts
- Incinerator fly ash provokes alteration of redox equilibrium and liberation of arachidonic acid in vitro
- Unique neuronal functions of cathepsin L and cathepsin B in secretory vesicles: biosynthesis of peptides in neurotransmission and neurodegenerative disease
- Two novel mitochondrial and chloroplastic targeting-peptide-degrading peptidasomes in A. thaliana, AtPreP1 and AtPreP2
- Switch from actin α1 to α2 expression and upregulation of biomarkers for pressure overload and cardiac hypertrophy in taurine-deficient mouse heart
- Human RBM28 protein is a specific nucleolar component of the spliceosomal snRNPs
- The β12-β13 loop is a key regulatory element for the activity and properties of the catalytic domain of protein phosphatase 1 and 2B
- DNA-binding properties of the recombinant high-mobility-group-like AT-hook-containing region from human BRG1 protein
- Papaya glutamine cyclotransferase shows a singular five-fold β-propeller architecture that suggests a novel reaction mechanism
- First identification of a phosphorylcholine-substituted protein from Caenorhabditis elegans: isolation and characterization of the aspartyl protease ASP-6
- The human cathelicidin peptide LL-37 and truncated variants induce segregation of lipids and proteins in the plasma membrane of Candida albicans
- Specificity of human cathepsin S determined by processing of peptide substrates and MHC class II-associated invariant chain
- Mast cell-dependent activation of pro matrix metalloprotease 2: a role for serglycin proteoglycan-dependent mast cell proteases