3.4.24.64 COX IV precursor + H2O - 3.4.24.64 epidermal growth factor receptor preprotein + H2O - 3.4.24.64 mitochondrial carrier protein + H2O the N-terminal extension of plant mitochondrial carrier proteins is removed by two-step processing. The first cleavage is by the mitochondrial processing peptidase 3.4.24.64 mitochondrial glycerol-3-phosphate dehydrogenase + H2O - 3.4.24.64 mitochondrial matrix protein precursor + H2O - 3.4.24.64 additional information removes amino-terminal matrix-targeting sequences from imported mitochondrial precursor proteins during or after translocation across mitochondrial membranes 3.4.24.64 additional information polypeptides destined to be imported from cytosol into mitochondrial matrix or inner mitochondrial membrane, critical step in the import of nuclear encoded precursor proteins into mitochondria 3.4.24.64 additional information plays an essential role in mitochondrial protein import 3.4.24.64 additional information mitochondrial processing peptidase is essential for viability of Caenorhabditis elegans 3.4.24.64 additional information mitosomal substrates of the enzyme are processed to mature proteins in Antonospora locustae with a simplified processing complex, overview 3.4.24.64 additional information the enzyme genetically interacts with prohibitins in the inner mitochondrial membrane and links the function of prohibitins to the F1FO-ATP synthase complex 3.4.24.64 additional information the enzyme specifically recognizes mitochondrial preproteins and removes their basic N-terminal signal prepeptides 3.4.24.64 additional information the mitochondrial processing peptidase removes leader peptides of preproteins after import into the mitochondrial matrix space to increase protein stability, enzyme inhibition leads to degradation of the unprocessed preproteins in the mitochondrial matrix space, overview 3.4.24.64 additional information cleavage site specificity of the major mitochondrial processing peptidase for removal of N-terminal presequences from mitochondrial proteins during maturation, global analysis of the N-proteome of yeast mitochondria, method, overview. For a number of proteins such as Gif1 and Pdb1, more than one N-terminus exist, therefore two truncated versions of the proteins are synthesized and compared to the in organello processing product, product identification by LC-MS/MS analysis 3.4.24.64 additional information isoform Plsp1 forms a stable complex with PGRL1 in Arabidopsis thylakoids 3.4.24.64 additional information the enzyme specifically cleaves off presequences from mitochondrial precursor proteins 3.4.24.64 Nfs1 + H2O MPP cleaves the precursor between Phe33 and Tyr34, Nfs1 processing, overview 3.4.24.64 nuclear-encoded polyprotein precursor + H2O the nuclear-encoded protein RPS14 (ribosomal protein S14) of rice mitochondria is synthesized in the cytosol as a polyprotein consisting of a large N-terminal domain comprising preSDHB (succinate dehydrogenase B precursor) and the C-terminal RPS14. After the preSDHB–RPS14 polyprotein is transported into the mitochondrial matrix, the protein is processed into three peptides: the N-terminal prepeptide, the SDHB domain and the C-terminal mature RPS14. MPP (mitochondrial processing peptidase) plays an essential role in processing of the polyprotein. Purified yeast MPP cleaves both the N-terminal presequence and the connector region between SDHB and RPS14. The connector region is processed more rapidly than the presequence. The cleavage site between SDHB and RPS14 is located in an MPPprocessing motif. MPP interacts with multiple sites in the region, possibly in a similar manner to the interaction with the N-terminal presequence. In addition, MPP preferentially recognizes the unfolded structure of preSDHB–RPS14. In mitochondria, MPP may recognize the stretched poly-protein during passage of the precursor through the translocational apparatus in the inner membrane, and cleaves the connecting region between the SDHB and RPS14 domains even before processing of the presequence 3.4.24.64 pea glutathione reductase + H2O signal peptide is cleaved off by the mitochondrial processing peptidase. Removal of 30 N-terminal amino acid residues of the signal peptide (GRD1–30) greatly stimulates processing activity. Constructs with a deletion of an additional ten amino acid residues (GRD1–40) and deletion of 22 amino acid residues in the middle of the GR signal sequence (GRD30–52) are not celeaved by MPP. Mutations within two amino acid residues on either side of the processing site have inhibitory effect on processing by MPP with a nearly complete inhibition for mutations at position K1. Mutation of positively charged residues in the C-terminal half of the GR targeting peptide inhibit processing by MPP 3.4.24.64 phosphatase and tensin homologue-induced kinase 1 + H2O - 3.4.24.64 pre-F1FO-ATP synthase + H2O on one hand, Atp23 serves as a processing peptidase and mediates the maturation of the mitochondrially-encoded FO-subunit Atp6 after its insertion into the inner membrane, on the other hand, independent of its proteolytic activity, Atp23 promotes the association of mature Atp6 with Atp9 oligomers with chaperone activity, overview, the assembly step is thus under the control of two substrate-specific chaperones, Atp10 and Atp23, which act on opposite sides of the inner membrane, modelling of assembly, overview 3.4.24.64 presequence-containing protein + H2O - 3.4.24.64 processing enhancing protein precursor + H2O -