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Volumn 123, Issue 1, 1998, Pages 128-135

Mechanism of mitochondrial import of adenylate kinase isozymes

Author keywords

Adenylate kinase; Bi topological distribution; Co translational import; Mitochondria; Noncleavable protein

Indexed keywords

ADENINE NUCLEOTIDE; ADENYLATE KINASE; CYTOCHROME C; ISOENZYME; LYASE;

EID: 0031914469     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021899     Document Type: Article
Times cited : (57)

References (39)
  • 1
    • 0002555264 scopus 로고
    • Adenylate control and the adenylate energy charge
    • Academic Press, New York
    • Atkinson, D.E. (1977) Adenylate control and the adenylate energy charge in Cellular Energy Metabolism and Its Regulation, pp. 85-107, Academic Press, New York
    • (1977) Cellular Energy Metabolism and Its Regulation , pp. 85-107
    • Atkinson, D.E.1
  • 2
    • 70349640265 scopus 로고
    • Adenylate kinase
    • Boyer, P.D., ed. Academic Press, New York
    • Noda, L. (1973) Adenylate kinase in The Enzymes (Boyer, P.D., ed.) Vol. 8, pp. 279-305, Academic Press, New York
    • (1973) The Enzymes , vol.8 , pp. 279-305
    • Noda, L.1
  • 3
    • 0015496635 scopus 로고
    • Isozymes of adenylate kinase in human tissues
    • Khoo, J.C. and Russell, P.J. (1972) Isozymes of adenylate kinase in human tissues. Biochim. Biophys. Acta 268, 98-101
    • (1972) Biochim. Biophys. Acta , vol.268 , pp. 98-101
    • Khoo, J.C.1    Russell, P.J.2
  • 4
    • 0014081316 scopus 로고
    • The participation of GTP-AMP P-transferase in substrate level phosphate transfer of rat liver mitochondria
    • Heldt, H.W. and Schwalbach, K. (1967) The participation of GTP-AMP P-transferase in substrate level phosphate transfer of rat liver mitochondria. Eur. J. Biochem. 1, 199-206
    • (1967) Eur. J. Biochem. , vol.1 , pp. 199-206
    • Heldt, H.W.1    Schwalbach, K.2
  • 5
    • 0018426491 scopus 로고
    • Distribution of adenylate kinase isozymes in porcine tissues and their subcellular localization
    • Watanabe, K., Itakura, T., and Kubo, S. (1979) Distribution of adenylate kinase isozymes in porcine tissues and their subcellular localization. J. Biochem. 85, 799-805
    • (1979) J. Biochem. , vol.85 , pp. 799-805
    • Watanabe, K.1    Itakura, T.2    Kubo, S.3
  • 6
    • 0026521701 scopus 로고
    • In vivo import of yeast adenylate kinase into mitochondria affected by site-directed mutagenesis
    • Magdolen, V., Schricker, R., Strobel, G., Germaier, H., and Bandolow, W. (1992) In vivo import of yeast adenylate kinase into mitochondria affected by site-directed mutagenesis. FEBS Lett. 299, 267-272
    • (1992) FEBS Lett. , vol.299 , pp. 267-272
    • Magdolen, V.1    Schricker, R.2    Strobel, G.3    Germaier, H.4    Bandolow, W.5
  • 7
    • 0018411282 scopus 로고
    • Mitochondrial GTP:AMP phosphotransferase. 1. Purification and properties
    • Tomasselli, A.G., Schirmer, R.H., and Noda, L.H. (1979) Mitochondrial GTP:AMP phosphotransferase. 1. Purification and properties. Eur. J. Biochem. 93, 257-262
    • (1979) Eur. J. Biochem. , vol.93 , pp. 257-262
    • Tomasselli, A.G.1    Schirmer, R.H.2    Noda, L.H.3
  • 8
    • 0027418855 scopus 로고
    • Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes
    • Tanabe, T., Yamada, M., Noma, T., Kajii, T., and Nakazawa, A. (1993) Tissue-specific and developmentally regulated expression of the genes encoding adenylate kinase isozymes. J. Biochem. 113, 200-207
    • (1993) J. Biochem. , vol.113 , pp. 200-207
    • Tanabe, T.1    Yamada, M.2    Noma, T.3    Kajii, T.4    Nakazawa, A.5
  • 9
    • 0026521425 scopus 로고
    • Characterization of adrenodoxin precursor expressed in Escherichia coli
    • Iwahashi, J., Furuya, S., Mihara, K., and Omura, T. (1992) Characterization of adrenodoxin precursor expressed in Escherichia coli. J. Biochem. 111, 451-455
    • (1992) J. Biochem. , vol.111 , pp. 451-455
    • Iwahashi, J.1    Furuya, S.2    Mihara, K.3    Omura, T.4
  • 13
    • 0026323440 scopus 로고
    • Import of proteins into mitochondria
    • Glick, B. and Schatz, G. (1991) Import of proteins into mitochondria. Annu. Rev. Genet. 25, 21-44
    • (1991) Annu. Rev. Genet. , vol.25 , pp. 21-44
    • Glick, B.1    Schatz, G.2
  • 15
    • 0023664891 scopus 로고
    • Isolation and characterization of two types of cDNA for mitochondrial adenylate kinase and their expression in Escherichia coli
    • Kishi, F., Tanizawa, Y., and Nakazawa, A. (1987) Isolation and characterization of two types of cDNA for mitochondrial adenylate kinase and their expression in Escherichia coli. J. Biol. Chem. 262, 11785-11789
    • (1987) J. Biol. Chem. , vol.262 , pp. 11785-11789
    • Kishi, F.1    Tanizawa, Y.2    Nakazawa, A.3
  • 16
    • 0024818830 scopus 로고
    • Cloning and characterization of cDNA for mitochondrial GTP: AMP phosphotransferase of bovine liver
    • Yamada, M., Shahjahan, M., Tanabe, T., Kishi, F., and Nakazawa, A. (1989) Cloning and characterization of cDNA for mitochondrial GTP: AMP phosphotransferase of bovine liver. J. Biol. Chem. 264, 19192-19199
    • (1989) J. Biol. Chem. , vol.264 , pp. 19192-19199
    • Yamada, M.1    Shahjahan, M.2    Tanabe, T.3    Kishi, F.4    Nakazawa, A.5
  • 17
    • 0028855710 scopus 로고
    • Solution structure of the acetylated and non-cleavable mitochondrial targeting signal of rat chaperonin 10
    • Jarvis, J.A., Ryan, M.T., Hoogenraad, N.J., Craik, D.J., and Hoj, P.B. (1995) Solution structure of the acetylated and non-cleavable mitochondrial targeting signal of rat chaperonin 10. J. Biol. Chem. 270, 1323-1331
    • (1995) J. Biol. Chem. , vol.270 , pp. 1323-1331
    • Jarvis, J.A.1    Ryan, M.T.2    Hoogenraad, N.J.3    Craik, D.J.4    Hoj, P.B.5
  • 18
    • 0026541138 scopus 로고
    • Import of cytochrome c heme lyase into mitochondria: A novel pathway into the intermembrane space
    • Lill, R., Stuart, R.A., Drygas, M.E., Nargang, F.E., and Neupert, W. (1992) Import of cytochrome c heme lyase into mitochondria: a novel pathway into the intermembrane space. EMBO J. 11, 449-456
    • (1992) EMBO J. , vol.11 , pp. 449-456
    • Lill, R.1    Stuart, R.A.2    Drygas, M.E.3    Nargang, F.E.4    Neupert, W.5
  • 19
    • 0025177390 scopus 로고
    • Early steps in mitochondrial protein import: Receptor functions can be substituted by the membrane insertion activity of apocytochrome c
    • Stuart, R.A., Nicholson, D.W., and Neupert, W. (1990) Early steps in mitochondrial protein import: receptor functions can be substituted by the membrane insertion activity of apocytochrome c. Cell 60, 31-43
    • (1990) Cell , vol.60 , pp. 31-43
    • Stuart, R.A.1    Nicholson, D.W.2    Neupert, W.3
  • 21
    • 0026079373 scopus 로고
    • The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution
    • Diederichs, K. and Schulz, G.E. (1991) The refined structure of the complex between adenylate kinase from beef heart mitochondrial matrix and its substrate AMP at 1.85 Å resolution. J. Mol. Biol. 217, 541-549
    • (1991) J. Mol. Biol. , vol.217 , pp. 541-549
    • Diederichs, K.1    Schulz, G.E.2
  • 22
    • 0000463084 scopus 로고
    • Lactic dehydrogenases (crystalline)
    • Stolzenbach, F. (1966) Lactic dehydrogenases (crystalline). Methods Enzymol. 9, 278-288
    • (1966) Methods Enzymol. , vol.9 , pp. 278-288
    • Stolzenbach, F.1
  • 23
    • 0003187798 scopus 로고
    • Recognition of respiratory chain enzyme systems. XI. Use of artificial electron acceptors in the assay of succinate-dehydrogenating enzymes
    • King, T.E. (1963) Recognition of respiratory chain enzyme systems. XI. Use of artificial electron acceptors in the assay of succinate-dehydrogenating enzymes. J. Biol. Chem. 238, 4032-4036
    • (1963) J. Biol. Chem. , vol.238 , pp. 4032-4036
    • King, T.E.1
  • 24
    • 0024203558 scopus 로고
    • Reconstitution of mitochondrial protein transport with purified ornithine carbamoyltransferase precursor expressed in Escherichia coli
    • Murakami, K., Amaya, Y., Takiguchi, M., Ebina, Y., and Mori, M. (1988) Reconstitution of mitochondrial protein transport with purified ornithine carbamoyltransferase precursor expressed in Escherichia coli. J. Biol. Chem. 263, 18437-18442
    • (1988) J. Biol. Chem. , vol.263 , pp. 18437-18442
    • Murakami, K.1    Amaya, Y.2    Takiguchi, M.3    Ebina, Y.4    Mori, M.5
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilising the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for quantitation of microgram quantities of protein utilising the principle of protein-dye binding. Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 77049233362 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization
    • Chance, B. and Williams, G.R. (1955) Respiratory enzymes in oxidative phosphorylation. I. Kinetics of oxygen utilization. J. Biol. Chem. 217, 383-393
    • (1955) J. Biol. Chem. , vol.217 , pp. 383-393
    • Chance, B.1    Williams, G.R.2
  • 28
    • 0021770917 scopus 로고
    • Efficient in vivo synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter
    • Melton, D.A., Krieg, P.A., Rebagliati, M.R., Maniatis, T., Zinn, K., and Green, M.R. (1984) Efficient in vivo synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res. 12, 7035-7056
    • (1984) Nucleic Acids Res. , vol.12 , pp. 7035-7056
    • Melton, D.A.1    Krieg, P.A.2    Rebagliati, M.R.3    Maniatis, T.4    Zinn, K.5    Green, M.R.6
  • 29
    • 0017191401 scopus 로고
    • An efficient mRNA dependent translational system from reticulocyte lysates
    • Pelham, H.R.B. and Jackson, R.J. (1976) An efficient mRNA dependent translational system from reticulocyte lysates. Eur. J. Biochem. 67, 247-256
    • (1976) Eur. J. Biochem. , vol.67 , pp. 247-256
    • Pelham, H.R.B.1    Jackson, R.J.2
  • 30
    • 0019887935 scopus 로고
    • Cell-free translation of carbamyl phosphate synthetase I and ornithine transcarbamylase messenger RNAs of rat liver. Effect of dietary protein and fasting on translatable mRNA levels
    • Mori, M., Miura, S., Tatibana, M., and Cohen, P.P. (1981) Cell-free translation of carbamyl phosphate synthetase I and ornithine transcarbamylase messenger RNAs of rat liver. Effect of dietary protein and fasting on translatable mRNA levels. J. Biol. Chem. 256, 4127-4132
    • (1981) J. Biol. Chem. , vol.256 , pp. 4127-4132
    • Mori, M.1    Miura, S.2    Tatibana, M.3    Cohen, P.P.4
  • 31
    • 77956990868 scopus 로고
    • Reduction of disulfide bonds in proteins with dithiothreitol
    • Konigsberg, W. (1972) Reduction of disulfide bonds in proteins with dithiothreitol. Methods Enzymol. 25, 185-188
    • (1972) Methods Enzymol. , vol.25 , pp. 185-188
    • Konigsberg, W.1
  • 32
    • 0345346100 scopus 로고
    • The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins
    • Crestfield, A.M., Moore, S., and Stein, W. (1963) The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J. Biol. Chem. 238, 622-627
    • (1963) J. Biol. Chem. , vol.238 , pp. 622-627
    • Crestfield, A.M.1    Moore, S.2    Stein, W.3
  • 33
    • 0014310452 scopus 로고
    • Enzymatic properties of the inner and outer membranes of rat liver mitochondria
    • Schnaitman, C. and Greenawalt, J.W. (1968) Enzymatic properties of the inner and outer membranes of rat liver mitochondria. J. Cell Biol. 38, 158-175
    • (1968) J. Cell Biol. , vol.38 , pp. 158-175
    • Schnaitman, C.1    Greenawalt, J.W.2
  • 35
    • 0027505809 scopus 로고
    • Coupling of cytosolic protein synthesis and mitochondrial protein import in yeast
    • Fujiki, M. and Verner, K. (1993) Coupling of cytosolic protein synthesis and mitochondrial protein import in yeast. J. Biol. Chem. 268, 1914-1920
    • (1993) J. Biol. Chem. , vol.268 , pp. 1914-1920
    • Fujiki, M.1    Verner, K.2
  • 36
    • 0027482105 scopus 로고
    • Co-translational protein import into mitochondria: An alternative view
    • Verner, K. (1993) Co-translational protein import into mitochondria: an alternative view. Trends. Biochem. Sci. 18, 366-371
    • (1993) Trends. Biochem. Sci. , vol.18 , pp. 366-371
    • Verner, K.1
  • 37
    • 0024423930 scopus 로고
    • Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins
    • Huber, R. and Carrell, R.W. (1989) Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Biochemistry 28, 8951-8966
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 38
    • 0030064680 scopus 로고    scopus 로고
    • A two-step recognition of signal sequences determines the translocation efficiency of proteins
    • Belin, D., Bost, S., Vassalli, J.D., and Strub, K. (1996) A two-step recognition of signal sequences determines the translocation efficiency of proteins. EMBO J. 3, 468-478
    • (1996) EMBO J. , vol.3 , pp. 468-478
    • Belin, D.1    Bost, S.2    Vassalli, J.D.3    Strub, K.4
  • 39
    • 0025191301 scopus 로고
    • Evidence for compartmentalized adenylate kinase catalysis serving a high energy phophoryl transfer function in rat skeletal muscle
    • Zeleznikar, R.J., Heyman, R.A., Graeff, R.M., Walseth, T.F., Dawis, S.M., Butz, E.A., and Goldberg, N.D. (1990) Evidence for compartmentalized adenylate kinase catalysis serving a high energy phophoryl transfer function in rat skeletal muscle. J. Biol. Chem. 265, 300-311
    • (1990) J. Biol. Chem. , vol.265 , pp. 300-311
    • Zeleznikar, R.J.1    Heyman, R.A.2    Graeff, R.M.3    Walseth, T.F.4    Dawis, S.M.5    Butz, E.A.6    Goldberg, N.D.7


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