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Volumn 123, Issue 3, 1998, Pages 408-415

Evidence for a novel ATP-dependent protease from the rat liver mitochondrial intermembrane space: Purification and characterisation

Author keywords

ATP; Cysteine protease; Mitochondrial intermembrane space; Proteolysis; Rat

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; ADENOSINE TRIPHOSPHATE DERIVATIVE; ADENOSINE TRIPHOSPHATE MAGNESIUM; CHYMOTRYPSIN; CYSTEINE PROTEINASE; LIVER ENZYME; NUCLEOSIDE TRIPHOSPHATE; PROTEINASE; TRYPTASE; UNCLASSIFIED DRUG;

EID: 0031890186     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021952     Document Type: Article
Times cited : (12)

References (47)
  • 2
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A. and Ciechanover, A. (1992) The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61, 761-807
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 3
  • 4
    • 0028087582 scopus 로고
    • PA700, an ATP-dependent activator of the 20S proteasome, is an ATPase containing multiple members of a nucleotide-binding protein family
    • DeMartino, G.N., Moomaw, C.R., Zagnitko, O.P., Proske, R.J., Chu-Ping, M., Afendis, S.J., Swaffield, J.C., and Slaughter, C.A. (1994) PA700, an ATP-dependent activator of the 20S proteasome, is an ATPase containing multiple members of a nucleotide-binding protein family. J. Biol. Chem. 269, 20878-20884
    • (1994) J. Biol. Chem. , vol.269 , pp. 20878-20884
    • DeMartino, G.N.1    Moomaw, C.R.2    Zagnitko, O.P.3    Proske, R.J.4    Chu-Ping, M.5    Afendis, S.J.6    Swaffield, J.C.7    Slaughter, C.A.8
  • 5
    • 0027053491 scopus 로고
    • The ubiquitin-conjugation system
    • Jentsch, S. (1992) The ubiquitin-conjugation system. Annu. Rev. Genet. 26, 179-207
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 179-207
    • Jentsch, S.1
  • 6
    • 0026055322 scopus 로고
    • Methylated ubiquitin inhibits cyclin degradation in clam embryo extracts
    • Hershko, A., Ganoth, D., Pehrson, J., Palazzo, R.E., and Cohen, L.H. (1991) Methylated ubiquitin inhibits cyclin degradation in clam embryo extracts. J. Biol. Chem. 266, 376-379
    • (1991) J. Biol. Chem. , vol.266 , pp. 376-379
    • Hershko, A.1    Ganoth, D.2    Pehrson, J.3    Palazzo, R.E.4    Cohen, L.H.5
  • 7
    • 0028276554 scopus 로고
    • Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2
    • Ciechanover, A., Shkedy, D., Oren, M., and Bercovich, B. (1994) Degradation of the tumor suppressor protein p53 by the ubiquitin-mediated proteolytic system requires a novel species of ubiquitin-carrier protein, E2. J. Biol. Chem. 269, 9582-9589
    • (1994) J. Biol. Chem. , vol.269 , pp. 9582-9589
    • Ciechanover, A.1    Shkedy, D.2    Oren, M.3    Bercovich, B.4
  • 8
    • 0027264692 scopus 로고
    • Degradation of Mos by the N-terminal proline (Pro2)-dependent ubiquitin pathway on fertilization of Xenopus eggs: Possible significance of natural selection for Pro2 in Mos
    • Nishizawa, M., Furuno, N., Okazaki, K., Tanaka, H., Ogawa, Y., and Sagata, N. (1993) Degradation of Mos by the N-terminal proline (Pro2)-dependent ubiquitin pathway on fertilization of Xenopus eggs: possible significance of natural selection for Pro2 in Mos. EMBO J. 12, 4021-4027
    • (1993) EMBO J. , vol.12 , pp. 4021-4027
    • Nishizawa, M.1    Furuno, N.2    Okazaki, K.3    Tanaka, H.4    Ogawa, Y.5    Sagata, N.6
  • 9
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κ B1 precursor protein and the activation of NF-κ B
    • Palombella, V.J., Rando, O.J., Goldberg, A.L., and Maniatis, T. (1994) The ubiquitin-proteasome pathway is required for processing the NF-κ B1 precursor protein and the activation of NF-κ B. Cell 78, 773-785
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 10
    • 0028234770 scopus 로고
    • Distinct 19S and 20S subcomplexes of the 26S proteasome and their distribution in the nucleus and the cytoplasm
    • Peters, J.M., Franke, W.W., and Kleinschmidt, J.A. (1994) Distinct 19S and 20S subcomplexes of the 26S proteasome and their distribution in the nucleus and the cytoplasm. J. Biol. Chem. 269, 7709-7718
    • (1994) J. Biol. Chem. , vol.269 , pp. 7709-7718
    • Peters, J.M.1    Franke, W.W.2    Kleinschmidt, J.A.3
  • 11
    • 0027257647 scopus 로고
    • Regulation of selective protein degradation in the endoplasmic reticulum by redox potential
    • Young, J., Kane, L.P., Exley, M., and Wileman, T. (1993) Regulation of selective protein degradation in the endoplasmic reticulum by redox potential. J. Biol. Chem. 268, 19810-19818
    • (1993) J. Biol. Chem. , vol.268 , pp. 19810-19818
    • Young, J.1    Kane, L.P.2    Exley, M.3    Wileman, T.4
  • 13
    • 0020479616 scopus 로고
    • Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria
    • Desautels, M. and Goldberg, A.L. (1982) Demonstration of an ATP-dependent, vanadate-sensitive endoprotease in the matrix of rat liver mitochondria. J. Biol. Chem. 257, 11673-11679
    • (1982) J. Biol. Chem. , vol.257 , pp. 11673-11679
    • Desautels, M.1    Goldberg, A.L.2
  • 14
    • 0005868498 scopus 로고
    • Liver mitochondria contain an ATP-dependent, vanadate-sensitive pathway for the degradation of proteins
    • Desautels, M. and Goldberg, A.L. (1982) Liver mitochondria contain an ATP-dependent, vanadate-sensitive pathway for the degradation of proteins. Proc. Natl. Acad. Sci. USA 79, 1869-1873
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1869-1873
    • Desautels, M.1    Goldberg, A.L.2
  • 15
    • 0022257090 scopus 로고
    • ATP-dependent protease in bovine adrenal cortex
    • Watabe, S. and Kimura, T. (1985) ATP-dependent protease in bovine adrenal cortex. J. Biol. Chem. 260, 5511-5517
    • (1985) J. Biol. Chem. , vol.260 , pp. 5511-5517
    • Watabe, S.1    Kimura, T.2
  • 16
    • 0022383025 scopus 로고
    • Adrenal cortex mitochondrial enzyme with ATP-dependent protease and protein-dependent ATPase activities
    • Watabe, S. and Kimura, T. (1985) Adrenal cortex mitochondrial enzyme with ATP-dependent protease and protein-dependent ATPase activities. J. Biol. Chem. 260, 14498-14504
    • (1985) J. Biol. Chem. , vol.260 , pp. 14498-14504
    • Watabe, S.1    Kimura, T.2
  • 17
    • 0027367968 scopus 로고
    • A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease
    • Wang, N., Gottesman, S., Willingham, M.C., Gottesman, M.M., and Maurizi, M.R. (1993) A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. Proc. Natl. Acad. Sci. USA 90, 11247-11251
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11247-11251
    • Wang, N.1    Gottesman, S.2    Willingham, M.C.3    Gottesman, M.M.4    Maurizi, M.R.5
  • 18
    • 0028362456 scopus 로고
    • Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration
    • Suzuki, C.K., Suda, K., Wang, N., and Schatz, G. (1994) Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration. Science 264, 273-276
    • (1994) Science , vol.264 , pp. 273-276
    • Suzuki, C.K.1    Suda, K.2    Wang, N.3    Schatz, G.4
  • 19
    • 0018290938 scopus 로고
    • Proteolysis of the products of mitochondrial protein synthesis in yeast mitochondria and submitochondrial particles
    • Kalnov, S.L., Novikova, L.A., Zubatov, A.S., and Luzikov, V.N. (1979) Proteolysis of the products of mitochondrial protein synthesis in yeast mitochondria and submitochondrial particles. Biochem. J. 182, 195-202
    • (1979) Biochem. J. , vol.182 , pp. 195-202
    • Kalnov, S.L.1    Novikova, L.A.2    Zubatov, A.S.3    Luzikov, V.N.4
  • 20
    • 0028279395 scopus 로고
    • ATP-dependent proteolysis in yeast mitochondria
    • Yasuhara, T., Mera, Y., Nakai, T., and Ohashi, A. (1994) ATP-dependent proteolysis in yeast mitochondria. J. Biochem. 115, 1166-1171
    • (1994) J. Biochem. , vol.115 , pp. 1166-1171
    • Yasuhara, T.1    Mera, Y.2    Nakai, T.3    Ohashi, A.4
  • 21
    • 0028081538 scopus 로고
    • Yta10p is required for the ATP-dependent degradation of polypeptides in the inner membrane of mitochondria
    • Pajic, A., Tauer, R., Feldmann, H., Neupert, W., and Langer, T. (1994) Yta10p is required for the ATP-dependent degradation of polypeptides in the inner membrane of mitochondria. FEBS Lett. 353, 201-206
    • (1994) FEBS Lett. , vol.353 , pp. 201-206
    • Pajic, A.1    Tauer, R.2    Feldmann, H.3    Neupert, W.4    Langer, T.5
  • 22
    • 0029775087 scopus 로고    scopus 로고
    • AAa proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria
    • Leonhard, K., Herrmann, R.A.S., Mannhaupt, G., Neupert, W., and Langer, T. (1996) AAA proteases with catalytic sites on opposite membrane surfaces comprise a proteolytic system for the ATP-dependent degradation of inner membrane proteins in mitochondria. EMBO J. 15, 4218-4229
    • (1996) EMBO J. , vol.15 , pp. 4218-4229
    • Leonhard, K.1    Herrmann, R.A.S.2    Mannhaupt, G.3    Neupert, W.4    Langer, T.5
  • 23
    • 0030008581 scopus 로고    scopus 로고
    • The YTA10-12 complex, an AAA protease with chaperon-like activity in the inner membrane of mitochondria
    • Arlt, H., Tauer, R., Feldmann, H., Neupert, W., and Langer, T. (1996) The YTA10-12 complex, an AAA protease with chaperon-like activity in the inner membrane of mitochondria. Cell 85, 875-885
    • (1996) Cell , vol.85 , pp. 875-885
    • Arlt, H.1    Tauer, R.2    Feldmann, H.3    Neupert, W.4    Langer, T.5
  • 24
    • 0027299142 scopus 로고
    • Two complementary approaches to study peroxisome biogenesis in Saccharomyces cerevisiae: Forward and reversed genetics
    • Kunau, W.H., Beyer, A., Franken, T., Gotte, K., Marzioch, M., Saidowsky, J., Skaletz-Rorowski, A., and Wiebel, F.F. (1993) Two complementary approaches to study peroxisome biogenesis in Saccharomyces cerevisiae: forward and reversed genetics. Biochimie 75, 209-224
    • (1993) Biochimie , vol.75 , pp. 209-224
    • Kunau, W.H.1    Beyer, A.2    Franken, T.3    Gotte, K.4    Marzioch, M.5    Saidowsky, J.6    Skaletz-Rorowski, A.7    Wiebel, F.F.8
  • 25
    • 0029328549 scopus 로고
    • A 200-amino acid ATPase module in search of a basic function
    • Confalonieri, F. and Duguet, M. (1995) A 200-amino acid ATPase module in search of a basic function. BioEssays 17, 639-650
    • (1995) BioEssays , vol.17 , pp. 639-650
    • Confalonieri, F.1    Duguet, M.2
  • 26
    • 0029554658 scopus 로고
    • Identification of a novel ATP-dependent proteolytic activity in mitochondrial intermembrane space
    • Sitte, N., Drung, I., and Dubiel, W. (1995) Identification of a novel ATP-dependent proteolytic activity in mitochondrial intermembrane space. Biochem. Mol. Biol. Int. 36, 871-881
    • (1995) Biochem. Mol. Biol. Int. , vol.36 , pp. 871-881
    • Sitte, N.1    Drung, I.2    Dubiel, W.3
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. (1976) A rapid and sensitive method for quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 284
    • (1976) Anal. Biochem. , vol.72 , pp. 284
    • Bradford, M.1
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 84988074679 scopus 로고
    • Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels
    • Blum, H., Beier, H., and Gross, H.J. (1987) Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8, 93-99
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2    Gross, H.J.3
  • 30
    • 0018786839 scopus 로고
    • Labeling of proteins by reductive methylation using sodium cyanoborohydride
    • Jentoft, N. and Dearborn, D.G. (1979) Labeling of proteins by reductive methylation using sodium cyanoborohydride. J. Biol. Chem. 254, 4359-4365
    • (1979) J. Biol. Chem. , vol.254 , pp. 4359-4365
    • Jentoft, N.1    Dearborn, D.G.2
  • 31
    • 0024843661 scopus 로고
    • Macroxyproteinase (M.O.P.): A 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells
    • Pacifici, R.E., David, C.S., and Davies, K.J.A. (1989) Macroxyproteinase (M.O.P.): A 670 kDa proteinase complex that degrades oxidatively denatured proteins in red blood cells. Free Rad. Biol. Med. 7, 521-536
    • (1989) Free Rad. Biol. Med. , vol.7 , pp. 521-536
    • Pacifici, R.E.1    David, C.S.2    Davies, K.J.A.3
  • 32
    • 0026486168 scopus 로고
    • Subunit 4 of the 26S protease is a member of a novel eukaryotic ATPase family
    • Dubiel, W., Ferrell, K., Pratt, G., and Rechsteiner, M. (1992) Subunit 4 of the 26S protease is a member of a novel eukaryotic ATPase family. J. Biol. Chem. 267, 22699-22702
    • (1992) J. Biol. Chem. , vol.267 , pp. 22699-22702
    • Dubiel, W.1    Ferrell, K.2    Pratt, G.3    Rechsteiner, M.4
  • 33
    • 0025870685 scopus 로고
    • ATP-promoted interaction between ClpA and ClpP in activation of Clp protease from Escherichia coli
    • Maurizi, M. (1991) ATP-promoted interaction between ClpA and ClpP in activation of Clp protease from Escherichia coli. Biochem. Soc. Trans. 19, 719-723
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 719-723
    • Maurizi, M.1
  • 35
    • 0013533949 scopus 로고
    • The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La
    • Chung, C.H. and Goldberg, A.L. (1981) The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La. Proc. Natl. Acad. Sci. USA 78, 4931-4935
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4931-4935
    • Chung, C.H.1    Goldberg, A.L.2
  • 36
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K., and Goldberg, A.L. (1996) Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 37
    • 0027379663 scopus 로고
    • ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease la from Escherichia coli
    • Fischer, H. and Glockshuber, R. (1993) ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli. J. Biol. Chem. 268, 22502-22507
    • (1993) J. Biol. Chem. , vol.268 , pp. 22502-22507
    • Fischer, H.1    Glockshuber, R.2
  • 38
    • 0023655017 scopus 로고
    • Purification of two high molecular weight proteases from rabbit reticulocyte lysate
    • Hough, R., Pratt, G., and Rechsteiner, M. (1987) Purification of two high molecular weight proteases from rabbit reticulocyte lysate. J. Biol. Chem. 262, 8303-8313
    • (1987) J. Biol. Chem. , vol.262 , pp. 8303-8313
    • Hough, R.1    Pratt, G.2    Rechsteiner, M.3
  • 39
    • 0026601663 scopus 로고
    • Proteases and protein degradation in E. coli
    • Maurizi, M.R. (1992) Proteases and protein degradation in E. coli. Experientia 48, 78-201
    • (1992) Experientia , vol.48 , pp. 78-201
    • Maurizi, M.R.1
  • 40
    • 0023393591 scopus 로고
    • Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La
    • Hwang, B.J., Park, W.J., Chung, C.H., and Goldberg, A.L. (1987) Escherichia coli contains a soluble ATP-dependent protease (Ti) distinct from protease La. Proc. Natl. Acad. Sci. USA 84, 5550-5554
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 5550-5554
    • Hwang, B.J.1    Park, W.J.2    Chung, C.H.3    Goldberg, A.L.4
  • 41
    • 0023184358 scopus 로고
    • A multiple-component, ATP-dependent protease from Escherichia coli
    • Katayama-Fujimura, Y., Gottesman, S., and Maurizi, M.R. (1987) A multiple-component, ATP-dependent protease from Escherichia coli. J. Biol. Chem. 262, 4477-4485
    • (1987) J. Biol. Chem. , vol.262 , pp. 4477-4485
    • Katayama-Fujimura, Y.1    Gottesman, S.2    Maurizi, M.R.3
  • 42
    • 0029186099 scopus 로고
    • Subunits of the regulatory complex of the 26S protease
    • Dubiel, W., Ferrell, K., and Rechsteiner, M. (1995) Subunits of the regulatory complex of the 26S protease. Mol. Biol. Rep. 21, 27-34
    • (1995) Mol. Biol. Rep. , vol.21 , pp. 27-34
    • Dubiel, W.1    Ferrell, K.2    Rechsteiner, M.3
  • 43
    • 0025360846 scopus 로고
    • The ATP-dependent Clp protease of Escherichia coli sequence of Clpa and identification of a Clp-specific substrate
    • Gottesman, S., Clark, W.P., and Maurizi, M. (1990) The ATP-dependent Clp protease of Escherichia coli sequence of ClpA and identification of a Clp-specific substrate. J. Biol. Chem. 265, 7886-7893
    • (1990) J. Biol. Chem. , vol.265 , pp. 7886-7893
    • Gottesman, S.1    Clark, W.P.2    Maurizi, M.3
  • 45
    • 0024794326 scopus 로고
    • ATP-dependent proteolysis of mitochondria of reticulocytes
    • Dubiel, W. and Rapoport, S.M. (1989) ATP-dependent proteolysis of mitochondria of reticulocytes. Cell. Biol. Rev. 20/21, 505-521
    • (1989) Cell. Biol. Rev. , vol.20-21 , pp. 505-521
    • Dubiel, W.1    Rapoport, S.M.2
  • 46
    • 0020474899 scopus 로고
    • Characteristics of an ATP-dependent proteolytic system of rat liver mitochondria
    • Rapoport, S.M., Dubiel, W., and Mueller, M. (1982) Characteristics of an ATP-dependent proteolytic system of rat liver mitochondria. FEBS Lett. 147, 93-96
    • (1982) FEBS Lett. , vol.147 , pp. 93-96
    • Rapoport, S.M.1    Dubiel, W.2    Mueller, M.3
  • 47
    • 0025348364 scopus 로고
    • SIMFIT: A microcomputer software-tool kit for modellistic studies in biochemistry
    • Holzhuetter, H.-G. and Colosimo, A. (1990) SIMFIT: A microcomputer software-tool kit for modellistic studies in biochemistry. Comput. Appl. Biosci. 6, 23-28
    • (1990) Comput. Appl. Biosci. , vol.6 , pp. 23-28
    • Holzhuetter, H.-G.1    Colosimo, A.2


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