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Volumn 17, Issue C, 1996, Pages 163-191

Proteolytic Processing of Mitochondrial Precursor Proteins

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EID: 0001649974     PISSN: 15692558     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1569-2558(09)60014-X     Document Type: Article
Times cited : (4)

References (101)
  • 1
    • 0024215473 scopus 로고
    • Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III
    • Affholter J.A., Fried V.A., and Roth R.A. Human insulin-degrading enzyme shares structural and functional homologies with E. coli protease III. Science 242 (1988) 1415-1418
    • (1988) Science , vol.242 , pp. 1415-1418
    • Affholter, J.A.1    Fried, V.A.2    Roth, R.A.3
  • 3
    • 0027941422 scopus 로고
    • Characterization of the mitochondrial processing peptidase of Neurospora crassa
    • Arretz M., Schneider H., Guiard B., Brunner M., and Neupert W. Characterization of the mitochondrial processing peptidase of Neurospora crassa. J. Biol. Chem. 269 (1994) 4959-4967
    • (1994) J. Biol. Chem. , vol.269 , pp. 4959-4967
    • Arretz, M.1    Schneider, H.2    Guiard, B.3    Brunner, M.4    Neupert, W.5
  • 4
    • 0026516458 scopus 로고
    • An unusual active site identified in a family of zinc metalloen-dopeptidases
    • Becker A.B., and Roth R.A. An unusual active site identified in a family of zinc metalloen-dopeptidases. Proc. Natl. Acad. Sci. USA 89 (1992) 3835-3839
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3835-3839
    • Becker, A.B.1    Roth, R.A.2
  • 5
    • 0027263747 scopus 로고
    • Identification of glutamate-169 as the third zinc-binding residue in proteinase III, a member of the family of insulin-degrading enzymes
    • Becker A.B., and Roth R.A. Identification of glutamate-169 as the third zinc-binding residue in proteinase III, a member of the family of insulin-degrading enzymes. Biochem. J. 292 (1993) 137-142
    • (1993) Biochem. J. , vol.292 , pp. 137-142
    • Becker, A.B.1    Roth, R.A.2
  • 6
    • 0025769806 scopus 로고
    • Mitochondrial inner membrane protease I of Saccharomyces cerevisiae shows sequence similarity to the Escherichia coli leader peptidase
    • Behrens M., Michaelis G., and Pratje E. Mitochondrial inner membrane protease I of Saccharomyces cerevisiae shows sequence similarity to the Escherichia coli leader peptidase. Mol. Gen. Genet. 228 (1991) 167-176
    • (1991) Mol. Gen. Genet. , vol.228 , pp. 167-176
    • Behrens, M.1    Michaelis, G.2    Pratje, E.3
  • 7
    • 0004263887 scopus 로고
    • A matrix-localized mitochondrial protease processing cytoplasmically-made precursors to mitochondrial proteins
    • Kroon A.M., and Saccone C. (Eds), Elsevier/North-Holland, Amsterdam
    • Böhni P., Gasser S., Leaver C., and Schatz G. A matrix-localized mitochondrial protease processing cytoplasmically-made precursors to mitochondrial proteins. In: Kroon A.M., and Saccone C. (Eds). The Organization and Expression of the Mitochondrial Genome (1980), Elsevier/North-Holland, Amsterdam 423-433
    • (1980) The Organization and Expression of the Mitochondrial Genome , pp. 423-433
    • Böhni, P.1    Gasser, S.2    Leaver, C.3    Schatz, G.4
  • 8
    • 0028866991 scopus 로고
    • Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase
    • Branda S.S., and Isaya G. Prediction and identification of new natural substrates of the yeast mitochondrial intermediate peptidase. J. Biol. Chem. 270 (1995) 27366-27373
    • (1995) J. Biol. Chem. , vol.270 , pp. 27366-27373
    • Branda, S.S.1    Isaya, G.2
  • 9
    • 0026709336 scopus 로고
    • The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain
    • Braun H.-P., Emmermann M., Kruft V., and Schmitz U.K. The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain. EMBO J. 11 (1992) 3219-3227
    • (1992) EMBO J. , vol.11 , pp. 3219-3227
    • Braun, H.-P.1    Emmermann, M.2    Kruft, V.3    Schmitz, U.K.4
  • 10
    • 0024383393 scopus 로고
    • Synthetic transit peptides inhibit import and processing of mitochondrial precursor proteins
    • Chu T.W., Eftime R., Sztul E., and Strauss A.W. Synthetic transit peptides inhibit import and processing of mitochondrial precursor proteins. J. Biol. Chem. 264 (1989) 9552-9558
    • (1989) J. Biol. Chem. , vol.264 , pp. 9552-9558
    • Chu, T.W.1    Eftime, R.2    Sztul, E.3    Strauss, A.W.4
  • 11
    • 0019568341 scopus 로고
    • Posttranslational uptake and processing of in vitro synthesized ornithine transcarbamoylase precursor by isolated rat liver mitochondria
    • Conboy J.G., and Rosenberg L.E. Posttranslational uptake and processing of in vitro synthesized ornithine transcarbamoylase precursor by isolated rat liver mitochondria. Proc. Natl. Acad. Sci. USA 78 (1981) 3073-3077
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3073-3077
    • Conboy, J.G.1    Rosenberg, L.E.2
  • 12
    • 0018540126 scopus 로고
    • In vitro synthesis of a putative precursor of mitochondrial ornithine transcarbamoylase
    • Conboy J.G., Kalousek F., and Rosenberg L.E. In vitro synthesis of a putative precursor of mitochondrial ornithine transcarbamoylase. Proc. Natl. Acad. Sci. USA 76 (1979) 5724-5727
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5724-5727
    • Conboy, J.G.1    Kalousek, F.2    Rosenberg, L.E.3
  • 13
    • 0020482786 scopus 로고
    • Processing of pre-ornithine transcarbamylase requires a zinc-dependent protease localized to the mitochondrial matrix
    • Conboy J.G., Fenton W.A., and Rosenberg L.E. Processing of pre-ornithine transcarbamylase requires a zinc-dependent protease localized to the mitochondrial matrix. Biochem. Biophys. Res. Commun. 105 (1982) 1-7
    • (1982) Biochem. Biophys. Res. Commun. , vol.105 , pp. 1-7
    • Conboy, J.G.1    Fenton, W.A.2    Rosenberg, L.E.3
  • 14
    • 0026830327 scopus 로고
    • Cloning and nucleotide sequence of opdA, the gene encoding oligopeptidase A in Salmonella typhimurium
    • Conlin C.A., and Miller C.G. Cloning and nucleotide sequence of opdA, the gene encoding oligopeptidase A in Salmonella typhimurium. J. Bacteriol. 174 (1992) 1631-1640
    • (1992) J. Bacteriol. , vol.174 , pp. 1631-1640
    • Conlin, C.A.1    Miller, C.G.2
  • 16
    • 0023818519 scopus 로고
    • 2-terminal domain of the rat and human ornithine carbamyltransferase "targeting" sequences
    • 2-terminal domain of the rat and human ornithine carbamyltransferase "targeting" sequences. J. Biol. Chem. 263 (1988) 5752-5756
    • (1988) J. Biol. Chem. , vol.263 , pp. 5752-5756
    • Côté, C.1    Poirier, J.2    Boulet, D.3    Dionne, G.4    Lacroix, M.5
  • 18
    • 0026800773 scopus 로고
    • Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III
    • Ding L., Becker A.B., Suzuki A., and Roth R.A. Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III. J. Biol. Chem. 267 (1992) 2414-2420
    • (1992) J. Biol. Chem. , vol.267 , pp. 2414-2420
    • Ding, L.1    Becker, A.B.2    Suzuki, A.3    Roth, R.A.4
  • 20
    • 0027225845 scopus 로고
    • Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria
    • Emmermann M., Braun H.-P., Arretz M., and Schmitz U.K. Characterization of the bifunctional cytochrome c reductase-processing peptidase complex from potato mitochondria. J. Biol. Chem. 268 (1993) 18936-18942
    • (1993) J. Biol. Chem. , vol.268 , pp. 18936-18942
    • Emmermann, M.1    Braun, H.-P.2    Arretz, M.3    Schmitz, U.K.4
  • 21
    • 0028072873 scopus 로고
    • The mitochondrial processing peptidase from potato: A self-processing enzyme encoded by two differentially expressed genes
    • Emmermann M., Braun H.P., and Schmitz U.K. The mitochondrial processing peptidase from potato: A self-processing enzyme encoded by two differentially expressed genes. Mol. Gen. Genet. 245 (1994) 237-245
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 237-245
    • Emmermann, M.1    Braun, H.P.2    Schmitz, U.K.3
  • 22
    • 0023046298 scopus 로고
    • Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III
    • Finch P.W., Wilson R.E., Brown K., Hickson I.D., and Emmerson P.T. Complete nucleotide sequence of the Escherichia coli ptr gene encoding protease III. Nucleic Acids Res. 14 (1986) 7695-7703
    • (1986) Nucleic Acids Res. , vol.14 , pp. 7695-7703
    • Finch, P.W.1    Wilson, R.E.2    Brown, K.3    Hickson, I.D.4    Emmerson, P.T.5
  • 25
    • 0025053384 scopus 로고
    • Cleavage-site motifs in mitochondrial targeting peptides
    • Gavel Y., and von Heijne G. Cleavage-site motifs in mitochondrial targeting peptides. Prot. Eng. 4 (1990) 33-37
    • (1990) Prot. Eng. , vol.4 , pp. 33-37
    • Gavel, Y.1    von Heijne, G.2
  • 26
    • 0027264859 scopus 로고
    • Functional reconstitution in Escherichia coli of the yeast mitochondrial matrix peptidase from its two inactive subunits
    • Geli V. Functional reconstitution in Escherichia coli of the yeast mitochondrial matrix peptidase from its two inactive subunits. Proc. Natl. Acad. Sci. USA 90 (1993) 6247-6251
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 6247-6251
    • Geli, V.1
  • 27
    • 0025695998 scopus 로고
    • Mitochondrial protein import
    • Geli V., and Glick B. Mitochondrial protein import. J. Bioenerg. Biomemb. 22 (1990) 725-751
    • (1990) J. Bioenerg. Biomemb. , vol.22 , pp. 725-751
    • Geli, V.1    Glick, B.2
  • 28
    • 0025065290 scopus 로고
    • The MAS-encoded processing protease of yeast mitochondria. Overproduction and characterization of its two nonidentical subunits
    • Geli V., Yang M., Suda K., Lustig A., and Schatz G. The MAS-encoded processing protease of yeast mitochondria. Overproduction and characterization of its two nonidentical subunits. J. Biol. Chem. 265 (1990) 19216-19222
    • (1990) J. Biol. Chem. , vol.265 , pp. 19216-19222
    • Geli, V.1    Yang, M.2    Suda, K.3    Lustig, A.4    Schatz, G.5
  • 29
    • 0025806309 scopus 로고
    • Core I protein of bovine ubiquinol-cytochrome-c reductase; an additional member of the mitochondrial-protein-processing family. Cloning of bovine core I and core II cDNAs and primary structure of the proteins
    • Gencic S., Schagger H., and von Jagow G. Core I protein of bovine ubiquinol-cytochrome-c reductase; an additional member of the mitochondrial-protein-processing family. Cloning of bovine core I and core II cDNAs and primary structure of the proteins. Eur. J. Biochem. 199 (1991) 123-131
    • (1991) Eur. J. Biochem. , vol.199 , pp. 123-131
    • Gencic, S.1    Schagger, H.2    von Jagow, G.3
  • 30
    • 0026323440 scopus 로고
    • Import of proteins into mitochondria
    • Glick B., and Schatz G. Import of proteins into mitochondria. Ann. Rev. Genet. 25 (1991) 21-44
    • (1991) Ann. Rev. Genet. , vol.25 , pp. 21-44
    • Glick, B.1    Schatz, G.2
  • 31
    • 0022292059 scopus 로고
    • 2)
    • 2). EMBO J. 4 (1985) 3265-3272
    • (1985) EMBO J. , vol.4 , pp. 3265-3272
    • Guiard, B.1
  • 32
    • 0025232326 scopus 로고
    • Separate nuclear genes encode sarcomere-specific and ubiquitous human mitochondrial creatine kinase isozymes
    • Haas R.C., and Strauss A.W. Separate nuclear genes encode sarcomere-specific and ubiquitous human mitochondrial creatine kinase isozymes. J. Biol. Chem. 265 (1990) 6921-6927
    • (1990) J. Biol. Chem. , vol.265 , pp. 6921-6927
    • Haas, R.C.1    Strauss, A.W.2
  • 33
    • 0026825857 scopus 로고
    • Cloning and nucleotide sequence of the Salmonella typhimurium dcp gene encoding dipeptidyl carboxypeptidase
    • Hamilton S., and Miller C.G. Cloning and nucleotide sequence of the Salmonella typhimurium dcp gene encoding dipeptidyl carboxypeptidase. J. Bacteriol. 174 (1992) 1626-1630
    • (1992) J. Bacteriol. , vol.174 , pp. 1626-1630
    • Hamilton, S.1    Miller, C.G.2
  • 34
    • 0018792980 scopus 로고
    • Biosynthesis of mitochondrial citrate synthase in Neurospora crassa
    • Harmey M.A., and Neupert W. Biosynthesis of mitochondrial citrate synthase in Neurospora crassa. FEBS Lett. 108 (1979) 385-389
    • (1979) FEBS Lett. , vol.108 , pp. 385-389
    • Harmey, M.A.1    Neupert, W.2
  • 35
    • 0022895277 scopus 로고
    • Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase
    • Hartl F.-U., Schmidt B., Wachter E., Weiss H., and Neupert W. Transport into mitochondria and intramitochondrial sorting of the Fe/S protein of ubiquinol-cytochrome c reductase. Cell 47 (1986) 939-951
    • (1986) Cell , vol.47 , pp. 939-951
    • Hartl, F.-U.1    Schmidt, B.2    Wachter, E.3    Weiss, H.4    Neupert, W.5
  • 37
    • 0024276898 scopus 로고
    • Mitochondrial protein import: Identification of processing peptidase and of PEP, a processing enhancing protein
    • Hawlitschek G., Schneider H., Schmidt B., Tropschug M., Hartl F.-U., and Neupert W. Mitochondrial protein import: Identification of processing peptidase and of PEP, a processing enhancing protein. Cell 53 (1988) 795-806
    • (1988) Cell , vol.53 , pp. 795-806
    • Hawlitschek, G.1    Schneider, H.2    Schmidt, B.3    Tropschug, M.4    Hartl, F.-U.5    Neupert, W.6
  • 38
    • 0024688488 scopus 로고
    • Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: Leader peptides cleaved by two matrix proteases share a three-amino acid motif
    • Hendrick J.P., Hodges P.E., and Rosenberg L.E. Survey of amino-terminal proteolytic cleavage sites in mitochondrial precursor proteins: Leader peptides cleaved by two matrix proteases share a three-amino acid motif. Proc. Natl. Acad. Sci. USA 86 (1989) 4056-4060
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4056-4060
    • Hendrick, J.P.1    Hodges, P.E.2    Rosenberg, L.E.3
  • 39
    • 0022260057 scopus 로고
    • Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor
    • Horwich A.L., Kalousek F., and Rosenberg L.E. Arginine in the leader peptide is required for both import and proteolytic cleavage of a mitochondrial precursor. Proc. Natl. Acad. Sci. USA 82 (1985) 4930-4933
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4930-4933
    • Horwich, A.L.1    Kalousek, F.2    Rosenberg, L.E.3
  • 40
    • 0022534459 scopus 로고
    • Targeting of pre-omithine transcarbamylase to mitochondria: Definition of critical regions and residues in the leader peptide
    • Horwich A.L., Kalousek F., Fenton W.A., Pollock R.A., and Rosenberg L.E. Targeting of pre-omithine transcarbamylase to mitochondria: Definition of critical regions and residues in the leader peptide. Cell 44 (1986) 451-459
    • (1986) Cell , vol.44 , pp. 451-459
    • Horwich, A.L.1    Kalousek, F.2    Fenton, W.A.3    Pollock, R.A.4    Rosenberg, L.E.5
  • 41
    • 0023583701 scopus 로고
    • The ornithine transcarbamylase leader peptide directs mitochondrial import through both its midportion structure and net positive charge
    • Horwich A.L., Kalousek F., Fenton W.A., Furtak K., Pollock R.A., and Rosenberg L.E. The ornithine transcarbamylase leader peptide directs mitochondrial import through both its midportion structure and net positive charge. J. Cell Biol. 105 (1987) 669-677
    • (1987) J. Cell Biol. , vol.105 , pp. 669-677
    • Horwich, A.L.1    Kalousek, F.2    Fenton, W.A.3    Furtak, K.4    Pollock, R.A.5    Rosenberg, L.E.6
  • 42
    • 0022108729 scopus 로고
    • The first twelve amino acids (less than half of the pre-sequence) of an imported mitochondrial protein can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrix
    • Hurt E.C., Pesold-Hurt B., Suda K., Oppliger W., and Schatz G. The first twelve amino acids (less than half of the pre-sequence) of an imported mitochondrial protein can direct mouse cytosolic dihydrofolate reductase into the yeast mitochondrial matrix. EMBO J. 4 (1985) 2061-2068
    • (1985) EMBO J. , vol.4 , pp. 2061-2068
    • Hurt, E.C.1    Pesold-Hurt, B.2    Suda, K.3    Oppliger, W.4    Schatz, G.5
  • 43
    • 0023154716 scopus 로고
    • Amino-terminal deletions in the presequence of an imported mitochondrial protein block the targeting function and proteolytic cleavage of the presequence at the carboxy terminus
    • Hurt E.C., Allison D.S., Müller U., and Schatz G. Amino-terminal deletions in the presequence of an imported mitochondrial protein block the targeting function and proteolytic cleavage of the presequence at the carboxy terminus. J. Biol. Chem. 262 (1987) 1420-1424
    • (1987) J. Biol. Chem. , vol.262 , pp. 1420-1424
    • Hurt, E.C.1    Allison, D.S.2    Müller, U.3    Schatz, G.4
  • 44
    • 0023697403 scopus 로고
    • Mitochondrial import and processing of mutant human ornithine transcarbamylase precursors in cultured cells
    • Isaya G., Fenton W.A., Hendrick J.P., Furtak K., Kalousek F., and Rosenberg L.E. Mitochondrial import and processing of mutant human ornithine transcarbamylase precursors in cultured cells. Mol. Cell. Biol. 8 (1988) 5150-5158
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5150-5158
    • Isaya, G.1    Fenton, W.A.2    Hendrick, J.P.3    Furtak, K.4    Kalousek, F.5    Rosenberg, L.E.6
  • 45
    • 0025821619 scopus 로고
    • Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide
    • Isaya G., Kalousek F., Fenton W.A., and Rosenberg L.E. Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide. J. Cell Biol. 113 (1991) 65-76
    • (1991) J. Cell Biol. , vol.113 , pp. 65-76
    • Isaya, G.1    Kalousek, F.2    Fenton, W.A.3    Rosenberg, L.E.4
  • 46
    • 0026657150 scopus 로고
    • Amino-terminal octapeptides function as recognition signals for the mitochondrial intermediate peptidase
    • Isaya G., Kalousek F., and Rosenberg L.E. Amino-terminal octapeptides function as recognition signals for the mitochondrial intermediate peptidase. J. Biol. Chem. 267 (1992) 7904-7910
    • (1992) J. Biol. Chem. , vol.267 , pp. 7904-7910
    • Isaya, G.1    Kalousek, F.2    Rosenberg, L.E.3
  • 47
    • 0026639993 scopus 로고
    • Sequence analysis of rat mitochondrial intermediate peptidase: Similarity to zinc metallopeptidases and to a putative yeast homologue
    • Isaya G., Kalousek F., and Rosenberg L.E. Sequence analysis of rat mitochondrial intermediate peptidase: Similarity to zinc metallopeptidases and to a putative yeast homologue. Proc. Natl. Acad. Sci. USA 89 (1992) 8317-8321
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8317-8321
    • Isaya, G.1    Kalousek, F.2    Rosenberg, L.E.3
  • 48
    • 0028049547 scopus 로고
    • MIP1, a new yeast gene homologous to the rat mitochondrial intermediate peptidase gene, is required for oxidative metabolism in Saccharomyces cerevisiae.
    • Isaya G., Miklos D., and Rollins R.A. MIP1, a new yeast gene homologous to the rat mitochondrial intermediate peptidase gene, is required for oxidative metabolism in Saccharomyces cerevisiae. Mol. Cell. Biol. 14 (1994) 5603-5616
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5603-5616
    • Isaya, G.1    Miklos, D.2    Rollins, R.A.3
  • 49
    • 0029101104 scopus 로고
    • Mammalian mitochondrial intermediate peptidase: Gene structure of a putative homologue from the fungus Schizophyllum commune and relationship to bacterial and eukaryotic thiol-dependent metallo-peptidases
    • Isaya G., Rollins R.A., Shen G.P., Hanson L.C., Ullrich R.C., and Novotny C.P. Mammalian mitochondrial intermediate peptidase: Gene structure of a putative homologue from the fungus Schizophyllum commune and relationship to bacterial and eukaryotic thiol-dependent metallo-peptidases. Genomics 28 (1995) 450-461
    • (1995) Genomics , vol.28 , pp. 450-461
    • Isaya, G.1    Rollins, R.A.2    Shen, G.P.3    Hanson, L.C.4    Ullrich, R.C.5    Novotny, C.P.6
  • 50
    • 0028934057 scopus 로고
    • Cytochrome c reductase from potato does not comprise three core proteins but contains an additional low-molecular-mass subunit
    • Jänsch L., Kruft V., Schmitz U.K., and Braun H.-P. Cytochrome c reductase from potato does not comprise three core proteins but contains an additional low-molecular-mass subunit. Eur. J. Biochem. 228 (1995) 878-885
    • (1995) Eur. J. Biochem. , vol.228 , pp. 878-885
    • Jänsch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.-P.4
  • 51
    • 0026638856 scopus 로고
    • Rat liver mitochondrial intermediate peptidase (MIP): Purification and initial characterization
    • Kalousek F., Isaya G., and Rosenberg L.E. Rat liver mitochondrial intermediate peptidase (MIP): Purification and initial characterization. EMBO J. 11 (1992) 2803-2809
    • (1992) EMBO J. , vol.11 , pp. 2803-2809
    • Kalousek, F.1    Isaya, G.2    Rosenberg, L.E.3
  • 52
    • 0027222799 scopus 로고
    • Uniform nomenclature for the mitochondrial peptidases cleaving precursors of mitochondrial proteins
    • Kalousek F., Neupert W., Omura T., Schatz G., and Schmitz U.K. Uniform nomenclature for the mitochondrial peptidases cleaving precursors of mitochondrial proteins. Trends Biochem. Sci. 18 (1993) 249
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 249
    • Kalousek, F.1    Neupert, W.2    Omura, T.3    Schatz, G.4    Schmitz, U.K.5
  • 53
    • 4244182845 scopus 로고
    • Rat liver mitochondrial processing peptidase: site-directed mutagenesis of zinc binding motif
    • Kalousek F., Rysavy P., and Striebel H.-M. Rat liver mitochondrial processing peptidase: site-directed mutagenesis of zinc binding motif. Mol. Biol. Cell 5 (1994) 475a
    • (1994) Mol. Biol. Cell , vol.5
    • Kalousek, F.1    Rysavy, P.2    Striebel, H.-M.3
  • 54
    • 0020426098 scopus 로고
    • Nucleotide sequence of the yeast nuclear gene for cytochrome c peroxidase precursor. Functional implications of the pre-sequence for protein transport into mitochondria
    • Kaput J., Goltz S., and Blobel G. Nucleotide sequence of the yeast nuclear gene for cytochrome c peroxidase precursor. Functional implications of the pre-sequence for protein transport into mitochondria. J. Biol. Chem. 257 (1982) 15054-15058
    • (1982) J. Biol. Chem. , vol.257 , pp. 15054-15058
    • Kaput, J.1    Goltz, S.2    Blobel, G.3
  • 55
    • 0027178356 scopus 로고
    • Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15
    • Kawabata S.-I., Nakagawa K., Muta T., Iwanaga S., and Davie E.W. Rabbit liver microsomal endopeptidase with substrate specificity for processing proproteins is structurally related to rat testes metalloendopeptidase 24.15. J. Biol. Chem. 268 (1993) 12498-12503
    • (1993) J. Biol. Chem. , vol.268 , pp. 12498-12503
    • Kawabata, S.-I.1    Nakagawa, K.2    Muta, T.3    Iwanaga, S.4    Davie, E.W.5
  • 56
    • 0029005231 scopus 로고
    • A putative metal-binding site in the β subunit of rat mitochondrial processing peptidase is essential for its catalytic activity
    • Kitada S., Shimokata K., Niidome T., Ogishima T., and Ito A. A putative metal-binding site in the β subunit of rat mitochondrial processing peptidase is essential for its catalytic activity. J. Biochem. 117 (1995) 1148-1150
    • (1995) J. Biochem. , vol.117 , pp. 1148-1150
    • Kitada, S.1    Shimokata, K.2    Niidome, T.3    Ogishima, T.4    Ito, A.5
  • 57
    • 0025147397 scopus 로고
    • The general mitochondrial matrix processing protease from rat liver: Structural characterization of the catalytic subunit
    • Kleiber J., Kalousek F., Swaroop M., and Rosenberg L.E. The general mitochondrial matrix processing protease from rat liver: Structural characterization of the catalytic subunit. Proc. Natl. Acad. Sci. USA 87 (1990) 7978-7982
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7978-7982
    • Kleiber, J.1    Kalousek, F.2    Swaroop, M.3    Rosenberg, L.E.4
  • 58
    • 0019877638 scopus 로고
    • Pre-ornithine transcarbamylse: Properties of the cytoplasmic precursor of a mitochondrial matrix enzyme
    • Kraus J.P., Conboy J.G., and Rosenberg L.E. Pre-ornithine transcarbamylse: Properties of the cytoplasmic precursor of a mitochondrial matrix enzyme. J. Biol. Chem. 256 (1981) 10739-10742
    • (1981) J. Biol. Chem. , vol.256 , pp. 10739-10742
    • Kraus, J.P.1    Conboy, J.G.2    Rosenberg, L.E.3
  • 59
    • 0006078510 scopus 로고
    • Different structures in the amino-terminal domain of the ornithine trascarbamylase leader peptide are involved in mitochondrial import and carboxyl-terminal cleavage
    • Kraus J.P., Novotny J., Kalousek F., Swaroop M., and Rosenberg L.E. Different structures in the amino-terminal domain of the ornithine trascarbamylase leader peptide are involved in mitochondrial import and carboxyl-terminal cleavage. Proc. Natl. Acad. Sci. USA 85 (1988) 8905-8909
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8905-8909
    • Kraus, J.P.1    Novotny, J.2    Kalousek, F.3    Swaroop, M.4    Rosenberg, L.E.5
  • 60
    • 0025080986 scopus 로고
    • Cloning an expression of the cDNA for a Drosophila insulin-degrading enzyme
    • Kuo W.-L., Gehm B.D., and Rosner M.R. Cloning an expression of the cDNA for a Drosophila insulin-degrading enzyme. Mol. Endo. 90 (1990) 1580-1591
    • (1990) Mol. Endo. , vol.90 , pp. 1580-1591
    • Kuo, W.-L.1    Gehm, B.D.2    Rosner, M.R.3
  • 62
    • 0020490478 scopus 로고
    • 1-ATPase subunit precursor in mitochondria
    • 1-ATPase subunit precursor in mitochondria. J. Biol. Chem. 257 (1982) 3177-3182
    • (1982) J. Biol. Chem. , vol.257 , pp. 3177-3182
    • McAda, P.C.1    Douglas, M.G.2
  • 63
    • 0018791408 scopus 로고
    • Synthesis of a larger precursor for the proteolipid subunit of the mitochondrial ATPase complex of Neurospora crassa in a cell-free wheat germ system
    • Michel R., Wachter E., and Sebald W. Synthesis of a larger precursor for the proteolipid subunit of the mitochondrial ATPase complex of Neurospora crassa in a cell-free wheat germ system. FEBS Lett. 101 (1979) 373-376
    • (1979) FEBS Lett. , vol.101 , pp. 373-376
    • Michel, R.1    Wachter, E.2    Sebald, W.3
  • 64
    • 0020108755 scopus 로고
    • A mitochondrial protease that cleaves the precursor of ornithine carbamoyl transferase
    • Miura S., Mori M., Amaya Y., and Tatibana M. A mitochondrial protease that cleaves the precursor of ornithine carbamoyl transferase. Eur. J. Biochem. 122 (1982) 641-647
    • (1982) Eur. J. Biochem. , vol.122 , pp. 641-647
    • Miura, S.1    Mori, M.2    Amaya, Y.3    Tatibana, M.4
  • 65
    • 0025375003 scopus 로고
    • Mutant alcohol dehydrogenase (ADH III) presequences that affect both in vitro mitochondrial import and in vitro processing by the matrix protease
    • Mooney D.T., Pilgrim D.B., and Young E.T. Mutant alcohol dehydrogenase (ADH III) presequences that affect both in vitro mitochondrial import and in vitro processing by the matrix protease. Mol. Cell. Biol. 10 (1990) 2801-2808
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2801-2808
    • Mooney, D.T.1    Pilgrim, D.B.2    Young, E.T.3
  • 66
    • 0019158243 scopus 로고
    • Characterization of a protease apparently involved in processing of pre-ornithine transcarbamylase of rat liver
    • Mori M., Miura S., Tatibana M., and Cohen P.P. Characterization of a protease apparently involved in processing of pre-ornithine transcarbamylase of rat liver. Proc. Natl. Acad. Sci. USA 77 (1980) 7044-7048
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7044-7048
    • Mori, M.1    Miura, S.2    Tatibana, M.3    Cohen, P.P.4
  • 67
    • 0027967490 scopus 로고
    • Arginine residues in the extension peptide are required for cleavage of a precursor by mitochondrial processing peptidase: Demonstration using synthetic peptide as a substrate
    • Niidome T., Kitada S., Shimokata K., Ogishima T., and Ito A. Arginine residues in the extension peptide are required for cleavage of a precursor by mitochondrial processing peptidase: Demonstration using synthetic peptide as a substrate. J. Biol. Chem. 269 (1994) 24719-24722
    • (1994) J. Biol. Chem. , vol.269 , pp. 24719-24722
    • Niidome, T.1    Kitada, S.2    Shimokata, K.3    Ogishima, T.4    Ito, A.5
  • 68
    • 0024508003 scopus 로고
    • Import and processing of precursor to mitochondrial aspartate aminotransferase. Structure-function relationship of the presequence
    • Nishi T., Nagashima F., Tanase S., Fukumoto Y., Joh T., Shimada K., Matsukado Y., Ushio Y., and Morino Y. Import and processing of precursor to mitochondrial aspartate aminotransferase. Structure-function relationship of the presequence. J. Biol. Chem. 264 (1989) 6044-6051
    • (1989) J. Biol. Chem. , vol.264 , pp. 6044-6051
    • Nishi, T.1    Nagashima, F.2    Tanase, S.3    Fukumoto, Y.4    Joh, T.5    Shimada, K.6    Matsukado, Y.7    Ushio, Y.8    Morino, Y.9
  • 69
    • 0027752461 scopus 로고
    • A mitochondrial protease with two catalytic subunits of nonoverlapping specificities
    • Nunnari J., Fox T.D., and Walter P. A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science 262 (1993) 1997-2003
    • (1993) Science , vol.262 , pp. 1997-2003
    • Nunnari, J.1    Fox, T.D.2    Walter, P.3
  • 70
    • 0023608016 scopus 로고
    • An extremely acidic amino-terminal presequence of the precursor for the human mitochondrial hinge protein
    • Ohta S., Goto K., Arai H., and Kagawa Y. An extremely acidic amino-terminal presequence of the precursor for the human mitochondrial hinge protein. FEBS Lett. 226 (1987) 171-175
    • (1987) FEBS Lett. , vol.226 , pp. 171-175
    • Ohta, S.1    Goto, K.2    Arai, H.3    Kagawa, Y.4
  • 71
    • 0026572003 scopus 로고
    • The complete DNA sequence of yeast chromosome III
    • Oliver S.G., et al. The complete DNA sequence of yeast chromosome III. Nature 357 (1992) 38-46
    • (1992) Nature , vol.357 , pp. 38-46
    • Oliver, S.G.1
  • 72
    • 0024468352 scopus 로고
    • Purification and characterization of a processing protease from rat liver mitochondria
    • Ou W.-J., Ito A., Okazaki H., and Omura T. Purification and characterization of a processing protease from rat liver mitochondria. EMBO J. 8 (1989) 2605-2612
    • (1989) EMBO J. , vol.8 , pp. 2605-2612
    • Ou, W.-J.1    Ito, A.2    Okazaki, H.3    Omura, T.4
  • 73
    • 0027992732 scopus 로고
    • Structural requirement for recognition of the precursor proteins by the mitochondrial processing peptidase
    • Ou W.-J., Kumamoto T., Mihara K., Kitada S., Niidome T., Ito A., and Omura T. Structural requirement for recognition of the precursor proteins by the mitochondrial processing peptidase. J. Biol. Chem. 269 (1994) 24673-24678
    • (1994) J. Biol. Chem. , vol.269 , pp. 24673-24678
    • Ou, W.-J.1    Kumamoto, T.2    Mihara, K.3    Kitada, S.4    Niidome, T.5    Ito, A.6    Omura, T.7
  • 75
    • 0027265225 scopus 로고
    • The β subunit of the mitochondrial processing peptidase from rat liver: Cloning and sequencing of a cDNA and comparison with a proposed family of metallopeptidases
    • Paces V., Rosenberg L.E., Fenton W.A., and Kalousek F. The β subunit of the mitochondrial processing peptidase from rat liver: Cloning and sequencing of a cDNA and comparison with a proposed family of metallopeptidases. Proc. Natl. Acad. Sci. USA 90 (1993) 5355-5358
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5355-5358
    • Paces, V.1    Rosenberg, L.E.2    Fenton, W.A.3    Kalousek, F.4
  • 76
    • 0025007049 scopus 로고
    • Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15
    • Pierotti A., Dong K.-W., Glucksman M.J., Orlowski M., and Roberts J.L. Molecular cloning and primary structure of rat testes metalloendopeptidase EC 3.4.24.15. Biochemistry 29 (1990) 10323-10329
    • (1990) Biochemistry , vol.29 , pp. 10323-10329
    • Pierotti, A.1    Dong, K.-W.2    Glucksman, M.J.3    Orlowski, M.4    Roberts, J.L.5
  • 77
    • 0024119655 scopus 로고
    • The processing peptidase of yeast mitochondria: The two cooperating components MPP and PEP are structurally related
    • Pollock R.A., Hartl F.-U., Cheng M.Y., Ostermann J., Horwich A., and Neupert W. The processing peptidase of yeast mitochondria: The two cooperating components MPP and PEP are structurally related. EMBO J. 7 (1988) 3493-3500
    • (1988) EMBO J. , vol.7 , pp. 3493-3500
    • Pollock, R.A.1    Hartl, F.-U.2    Cheng, M.Y.3    Ostermann, J.4    Horwich, A.5    Neupert, W.6
  • 78
    • 0020653565 scopus 로고
    • A nuclear mutation prevents processing of a mitochondrially encoded membrane protein in Saccharomyces cerevisiae.
    • Pratje E., Mannhaupt G., Michaelis G., and Beyreuther K. A nuclear mutation prevents processing of a mitochondrially encoded membrane protein in Saccharomyces cerevisiae. EMBO J. 2 (1983) 1049-1054
    • (1983) EMBO J. , vol.2 , pp. 1049-1054
    • Pratje, E.1    Mannhaupt, G.2    Michaelis, G.3    Beyreuther, K.4
  • 79
    • 0025828357 scopus 로고
    • Homologues of insulinase, a new superfamily of metalloen-dopeptidases
    • Rawlings N.D., and Barrett A.J. Homologues of insulinase, a new superfamily of metalloen-dopeptidases. Biochem. J. 275 (1991) 389-391
    • (1991) Biochem. J. , vol.275 , pp. 389-391
    • Rawlings, N.D.1    Barrett, A.J.2
  • 80
    • 0028246650 scopus 로고
    • Rat liver mitochondrial processing peptidase (MPP): Both α- and β- subunits are required for activity
    • Saavedra-Alanis V.M., Rysavy P., Rosenberg L.E., and Kalousek F. Rat liver mitochondrial processing peptidase (MPP): Both α- and β- subunits are required for activity. J. Biol. Chem. 269 (1994) 9284-9288
    • (1994) J. Biol. Chem. , vol.269 , pp. 9284-9288
    • Saavedra-Alanis, V.M.1    Rysavy, P.2    Rosenberg, L.E.3    Kalousek, F.4
  • 82
    • 0021753883 scopus 로고
    • Processing peptidase of Neurospora mitochondria. Two-step cleavage of imported ATPase subunit 9
    • Schmidt B., Wachter E., Sebald W., and Neupert W. Processing peptidase of Neurospora mitochondria. Two-step cleavage of imported ATPase subunit 9. Eur. J. Biochem. 144 (1984) 581-588
    • (1984) Eur. J. Biochem. , vol.144 , pp. 581-588
    • Schmidt, B.1    Wachter, E.2    Sebald, W.3    Neupert, W.4
  • 83
    • 0026098773 scopus 로고
    • Inner membrane protease I, an enzyme mediating intramitochondrial protein sorting in yeast
    • Schneider A., Behrens M., Scherer P., Pratje E., Michaelis G., and Schatz G. Inner membrane protease I, an enzyme mediating intramitochondrial protein sorting in yeast. EMBO J. 10 (1991) 247-254
    • (1991) EMBO J. , vol.10 , pp. 247-254
    • Schneider, A.1    Behrens, M.2    Scherer, P.3    Pratje, E.4    Michaelis, G.5    Schatz, G.6
  • 84
    • 0028362616 scopus 로고
    • Purified inner membrane protease I of yeast mitochondria is a heterodimer
    • Schneider A., Oppliger W., and Jenö P. Purified inner membrane protease I of yeast mitochondria is a heterodimer. J. Biol. Chem. 269 (1994) 8635-8638
    • (1994) J. Biol. Chem. , vol.269 , pp. 8635-8638
    • Schneider, A.1    Oppliger, W.2    Jenö, P.3
  • 85
    • 0025312373 scopus 로고
    • Matrix processing peptidase of mitochondria: Structure-function relationship
    • Schneider H., Arretz M., Wachter E., and Neupert W. Matrix processing peptidase of mitochondria: Structure-function relationship. J. Biol. Chem. 265 (1990) 9881-9887
    • (1990) J. Biol. Chem. , vol.265 , pp. 9881-9887
    • Schneider, H.1    Arretz, M.2    Wachter, E.3    Neupert, W.4
  • 86
    • 0026693806 scopus 로고
    • Primary structure, import and assembly of the yeast homologue of succinate dehydrogenase flavoprotein
    • Schulke N., Blobel G., and Pain D. Primary structure, import and assembly of the yeast homologue of succinate dehydrogenase flavoprotein. Proc. Natl. Acad. Sci. USA 89 (1992) 8011-8015
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8011-8015
    • Schulke, N.1    Blobel, G.2    Pain, D.3
  • 88
    • 77956715117 scopus 로고    scopus 로고
    • Mutational analysis of both subunits from rat mitochondrial processing peptidase (MPP)
    • Submitted
    • Striebel, H.-M., Rysavy, P., Adamec, J., Spizek, J., & Kalousek, F. (1996). Mutational analysis of both subunits from rat mitochondrial processing peptidase (MPP). Submitted
    • (1996)
    • Striebel, H.-M.1    Rysavy, P.2    Adamec, J.3    Spizek, J.4    Kalousek, F.5
  • 89
    • 0026662008 scopus 로고
    • Molecular cloning of porcine soluble angiotensin-binding protein
    • Sugiura N., Hagiwara H., and Hirose S. Molecular cloning of porcine soluble angiotensin-binding protein. J. Biol. Chem. 267 (1992) 18067-18072
    • (1992) J. Biol. Chem. , vol.267 , pp. 18067-18072
    • Sugiura, N.1    Hagiwara, H.2    Hirose, S.3
  • 90
    • 0023571665 scopus 로고
    • Import of rat ornithine transcarbamylase precursor into mitochondria: Two-step processing of the leader peptide
    • Sztul E.S., Hendrick J.P., Kraus J.P., Wall D., Kalousek F., and Rosenberg L.E. Import of rat ornithine transcarbamylase precursor into mitochondria: Two-step processing of the leader peptide. J. Cell Biol. 105 (1987) 2631-2639
    • (1987) J. Cell Biol. , vol.105 , pp. 2631-2639
    • Sztul, E.S.1    Hendrick, J.P.2    Kraus, J.P.3    Wall, D.4    Kalousek, F.5    Rosenberg, L.E.6
  • 92
    • 0025303335 scopus 로고
    • Zinc coordination, function, and structure of zinc enzymes and other proteins
    • Vallee B.L., and Auld D.S. Zinc coordination, function, and structure of zinc enzymes and other proteins. Biochemistry 29 (1990) 5647-5659
    • (1990) Biochemistry , vol.29 , pp. 5647-5659
    • Vallee, B.L.1    Auld, D.S.2
  • 93
    • 0021430549 scopus 로고
    • The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: A protein with an extremely high content of acidic amino acids
    • van Loon A.P.G.M., De Groot R.J., De Haan M., Dekker A., and Grivell L.A. The DNA sequence of the nuclear gene coding for the 17-kd subunit VI of the yeast ubiquinol-cytochrome c reductase: A protein with an extremely high content of acidic amino acids. EMBO J. 3 (1984) 1039-1043
    • (1984) EMBO J. , vol.3 , pp. 1039-1043
    • van Loon, A.P.G.M.1    De Groot, R.J.2    De Haan, M.3    Dekker, A.4    Grivell, L.A.5
  • 94
    • 0022481113 scopus 로고
    • The presequences of two imported mitochondrial proteins contain information for intracellular and intramitochondrial sorting
    • van Loon A.P.G.M., Brändli A.W., and Schatz G. The presequences of two imported mitochondrial proteins contain information for intracellular and intramitochondrial sorting. Cell 44 (1986) 801-812
    • (1986) Cell , vol.44 , pp. 801-812
    • van Loon, A.P.G.M.1    Brändli, A.W.2    Schatz, G.3
  • 96
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • von Heiñìe G., Steppuhn J., and Herrmann R.G. Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 180 (1989) 535-545
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • von Heiñìe, G.1    Steppuhn, J.2    Herrmann, R.G.3
  • 97
    • 0024008659 scopus 로고
    • MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease
    • Witte C., Jensen R.E., Yaffe M.P., and Schatz G. MAS1, a gene essential for yeast mitochondrial assembly, encodes a subunit of the mitochondrial processing protease. EMBO J. 7 (1988) 1439-1447
    • (1988) EMBO J. , vol.7 , pp. 1439-1447
    • Witte, C.1    Jensen, R.E.2    Yaffe, M.P.3    Schatz, G.4
  • 98
    • 0000856498 scopus 로고
    • Two nuclear mutations that block mitochondrial protein import in yeast
    • Yaffe M.P., and Schatz G. Two nuclear mutations that block mitochondrial protein import in yeast. Proc. Natl. Acad. Sci. USA 81 (1984) 4819-4823
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 4819-4823
    • Yaffe, M.P.1    Schatz, G.2
  • 99
    • 0022110323 scopus 로고
    • A yeast mutant temperature-sensitive for mitochondrial assembly is deficient in a mitochondrial protease activity that cleaves imported precursor polypeptides
    • Yaffe M.P., Ohta S., and Schatz G. A yeast mutant temperature-sensitive for mitochondrial assembly is deficient in a mitochondrial protease activity that cleaves imported precursor polypeptides. EMBO J. 4 (1985) 2069-2074
    • (1985) EMBO J. , vol.4 , pp. 2069-2074
    • Yaffe, M.P.1    Ohta, S.2    Schatz, G.3
  • 100
    • 0024254118 scopus 로고
    • Import of proteins into yeast mitochondria: The purified matrix processing protease contains two subunits which are encoded by the nuclear MAS1 and MAS2 genes
    • Yang M., Jensen R.E., Yaffe M.P., Oppliger W., and Schatz G. Import of proteins into yeast mitochondria: The purified matrix processing protease contains two subunits which are encoded by the nuclear MAS1 and MAS2 genes. EMBO J. 7 (1988) 3857-3862
    • (1988) EMBO J. , vol.7 , pp. 3857-3862
    • Yang, M.1    Jensen, R.E.2    Yaffe, M.P.3    Oppliger, W.4    Schatz, G.5
  • 101
    • 0025735353 scopus 로고
    • The MAS-encoded processing protease of yeast mitochondria. Interaction of the purified enzyme with signal peptides and purified precursor protein
    • Yang M., Geli V., Oppliger W., Suda K., James P., and Schatz G. The MAS-encoded processing protease of yeast mitochondria. Interaction of the purified enzyme with signal peptides and purified precursor protein. J. Biol. Chem. 266 (1991) 6416-6423
    • (1991) J. Biol. Chem. , vol.266 , pp. 6416-6423
    • Yang, M.1    Geli, V.2    Oppliger, W.3    Suda, K.4    James, P.5    Schatz, G.6


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