Mitochondrial processing peptidases

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1592, Issue 1, 2002, Pages 63-77

  Gakh, Oleksandr ^a   Cavadini, Patrizia ^a   Isaya, Grazia ^a  

^a MAYO CLINIC   (United States)

Author keywords

Mitochondrion; Presequence; Processing peptidase; Protein import

Indexed keywords

CHAPERONE; ISOENZYME; MEMBRANE PROTEIN; PEPTIDASE; POLYPEPTIDE;

AMINO ACID SEQUENCE; CYTOPLASM; MITOCHONDRION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN MOTIF; PROTEIN PURIFICATION; PROTEIN TARGETING; REVIEW; SEQUENCE HOMOLOGY; SPECIES DIFFERENCE; UNINDEXED SEQUENCE;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; ESCHERICHIA COLI; HUMANS; INTRACELLULAR MEMBRANES; METALLOENDOPEPTIDASES; MITOCHONDRIA; MITOCHONDRIAL PROTEINS; MOLECULAR SEQUENCE DATA; PHYLOGENY; PROTEIN PRECURSORS; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0037009089     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4889(02)00265-3     Document Type: Review

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16. 1 complex in plants
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29. 1 complex in Saccharomyces cerevisiae
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31. The ornithine transcarbamylase leader peptide directs mitochondrial import through both its midportion structure and net positive charge
32. Structural requirement for recognition of the precursor proteins by the mitochondrial processing peptidase
33. Analysis of elements in the substrate required for processing by mitochondrial processing peptidase
34. Mutant alcohol dehydrogenase (ADH III) presequences that affect both in vitro mitochondrial import and in vitro processing by the matrix protease
35. Arginine residues in the extension peptide are required for cleavage of a precursor by mitochondrial processing peptidase. Demonstration using synthetic peptide as a substrate
36. Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide
37. Substrate recognition by mitochondrial processing peptidase toward the malate dehydrogenase precursor
38. Importance of residues carboxyl terminal relative to the cleavage site in substrates of mitochondrial processing peptidase for their specific recognition and cleavage
39. Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase
40. Two-step processing of human frataxin by mitochondrial processing peptidase: The precursor and intermediate form are cleaved at different rates
41. Solution structure of the acetylated and noncleavable mitochondrial targeting signal of rat chaperonin 10
42. Structure of the signal sequences for two mitochondrial matrix proteins that are not proteolytically processed upon import
43. Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences
44. Amino-terminal octapeptides function as recognition signals for the mitochondrial intermediate peptidase
45. Mitochondrial protein import: Identification of processing peptidase and of PEP, a processing enhancing protein
46. Import of proteins into yeast mitochondria: The purified matrix processing protease contains two subunits which are encoded by the nuclear MAS1 and MAS2 genes
47. Purification and characterization of a processing protease from rat liver mitochondria
48. The general mitochondrial matrix processing protease from rat liver: Structural characterization of the catalytic subunit
49. The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain
50. 1-complex of the respiratory chain
51. 1 complex in Spinacia oleracea
52. Functional reconstitution in Escherichia coli of the yeast mitochondrial matrix peptidase from its two inactive subunits
53. Rat liver mitochondrial processing peptidase. Both alpha- and beta-subunits are required for activity
54. Complementation between mitochondrial processing peptidase (MPP) subunits from different species
55. 1 complex of bovine heart mitochondria
56. 1 complex
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61. The MAS-encoded processing protease of yeast mitochondria. Interaction of the purified enzyme with signal peptides and a purified precursor protein
62. The mitochondrial processing peptidase behaves as a zinc-metallopeptidase
63. Removal and replacement of metal ions in metallopeptidases
64. Two nuclear mutations that block mitochondrial protein import in yeast
65. A yeast mutant temperature-sensitive for mitochondrial assembly is deficient in a mitochondrial protease activity that cleaves imported precursor polypeptides
66. MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease
67. The processing peptidase of yeast mitochondria: The two co-operating components MPP and PEP are structurally related
68. Matrix processing peptidase of mitochondria. Structure-function relationships
69. The beta subunit of the mitochondrial processing peptidase from rat liver: Cloning and sequencing of a cDNA and comparison with a proposed family of metallopeptidases
70. Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria
71. Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning
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80. A putative metal-binding site in the beta subunit of rat mitochondrial processing peptidase is essential for its catalytic activity
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97. Som1, a third component of the yeast mitochondrial inner membrane peptidase complex that contains Imp1 and Imp2
98. A nuclear mutation prevents processing of a mitochondrially encoded membrane protein in Saccharomyces cerevisiae
99. 2 by isolated yeast mitochondria
100. 5 reductase to two locations within yeast mitochondria
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102. One nuclear gene controls the removal of transient pre-sequences from two yeast proteins: One encoded by the nuclear the other by the mitochondrial genome
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123. 1 complex of Saccharomyces cerevisiae
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125. 1 complex in Saccharomyces cerevisiae
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