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Volumn 125, Issue 20, 2012, Pages 4876-4855

Cofactor-dependent maturation of mammalian sulfite oxidase links two mitochondrial import pathways

Author keywords

Folding trap; Heme; Intermembrane space; Molybdenum cofactor; Sulfite oxidase

Indexed keywords

HEME; INNER MEMBRANE PEPTIDASE; LACTATE DEHYDROGENASE (CYTOCHROME); PEPTIDASE; PROTEINASE K; SULFITE OXIDASE; UNCLASSIFIED DRUG;

EID: 84871140998     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.110114     Document Type: Article
Times cited : (49)

References (38)
  • 1
    • 0019197177 scopus 로고
    • The transport of proteins into yeast mitochondria. Kinetics and pools.
    • Ades, I. Z. and Butow, R. A. (1980). The transport of proteins into yeast mitochondria. Kinetics and pools. J. Biol. Chem. 255, 9925-9935.
    • (1980) J. Biol. Chem. , vol.255 , pp. 9925-9935
    • Ades, I.Z.1    Butow, R.A.2
  • 2
    • 0033615958 scopus 로고    scopus 로고
    • The TOM core complex: the general protein import pore of the outer membrane of mitochondria
    • Ahting, U., Thun, C., Hegerl, R., Typke, D., Nargang, F. E., Neupert, W. and Nussberger, S. (1999). The TOM core complex: the general protein import pore of the outer membrane of mitochondria. J. Cell Biol. 147, 959-968.
    • (1999) J. Cell Biol. , vol.147 , pp. 959-968
    • Ahting, U.1    Thun, C.2    Hegerl, R.3    Typke, D.4    Nargang, F.E.5    Neupert, W.6    Nussberger, S.7
  • 6
    • 0015502188 scopus 로고
    • Hepatic sulfite oxidase. Congruency in mitochondria of prosthetic groups and activity
    • Cohen, H. J., Betcher-Lange, S., Kessler, D. L. and Rajagopalan, K. V. (1972). Hepatic sulfite oxidase. Congruency in mitochondria of prosthetic groups and activity. J. Biol. Chem. 247, 7759-7766.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7759-7766
    • Cohen, H.J.1    Betcher-Lange, S.2    Kessler, D.L.3    Rajagopalan, K.V.4
  • 7
    • 0024971440 scopus 로고
    • Isolation, in the intact state, of the pterin molybdenum cofactor from xanthine oxidase
    • Deistung, J. and Bray, R. C. (1989). Isolation, in the intact state, of the pterin molybdenum cofactor from xanthine oxidase. Biochem. J. 263, 477-483.
    • (1989) Biochem. J. , vol.263 , pp. 477-483
    • Deistung, J.1    Bray, R.C.2
  • 8
    • 0024279426 scopus 로고
    • Coupling of heme attachment to import of cytochrome c into yeast mitochondria. Studies with heme lyase-deficient mitochondria and altered apocytochromes c
    • Dumont, M. E., Ernst, J. F. and Sherman, F. (1988). Coupling of heme attachment to import of cytochrome c into yeast mitochondria. Studies with heme lyase-deficient mitochondria and altered apocytochromes c. J. Biol. Chem. 263, 15928-15937.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15928-15937
    • Dumont, M.E.1    Ernst, J.F.2    Sherman, F.3
  • 9
    • 0032718476 scopus 로고    scopus 로고
    • Two distinct mechanisms drive protein translocation across the mitochondrial outer membrane in the late step of the cytochrome b(2) import pathway
    • Esaki, M., Kanamori, T., Nishikawa, S. and Endo, T. (1999). Two distinct mechanisms drive protein translocation across the mitochondrial outer membrane in the late step of the cytochrome b(2) import pathway. Proc. Natl. Acad. Sci. USA 96, 11770-11775.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11770-11775
    • Esaki, M.1    Kanamori, T.2    Nishikawa, S.3    Endo, T.4
  • 12
    • 0027332553 scopus 로고
    • Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP
    • Glick, B. S., Wachter, C., Reid, G. A. and Schatz, G. (1993). Import of cytochrome b2 to the mitochondrial intermembrane space: the tightly folded heme-binding domain makes import dependent upon matrix ATP. Protein Sci. 2, 1901-1917.
    • (1993) Protein Sci. , vol.2 , pp. 1901-1917
    • Glick, B.S.1    Wachter, C.2    Reid, G.A.3    Schatz, G.4
  • 13
    • 33845952893 scopus 로고    scopus 로고
    • Identification of the missing component in the mitochondrial benzamidoxime prodrug-converting system as a novel molybdenum enzyme
    • Havemeyer, A., Bittner, F., Wollers, S., Mendel, R., Kunze, T. and Clement, B. (2006). Identification of the missing component in the mitochondrial benzamidoxime prodrug-converting system as a novel molybdenum enzyme. J. Biol. Chem. 281, 34796-34802.
    • (2006) J. Biol. Chem. , vol.281 , pp. 34796-34802
    • Havemeyer, A.1    Bittner, F.2    Wollers, S.3    Mendel, R.4    Kunze, T.5    Clement, B.6
  • 14
    • 0016613097 scopus 로고
    • Cytoplasmic type 80S ribosomes associated with yeast mitochondria. IV. Attachment of ribosomes to the outer membrane of isolated mitochondria
    • Kellems, R. E., Allison, V. F. and Butow, R. A. (1975). Cytoplasmic type 80S ribosomes associated with yeast mitochondria. IV. Attachment of ribosomes to the outer membrane of isolated mitochondria. J. Cell Biol. 65, 1-14.
    • (1975) J. Cell Biol. , vol.65 , pp. 1-14
    • Kellems, R.E.1    Allison, V.F.2    Butow, R.A.3
  • 16
    • 0032475958 scopus 로고    scopus 로고
    • Import into mitochondria, folding and retrograde movement of fumarase in yeast
    • Knox, C., Sass, E., Neupert, W. and Pines, O. (1998). Import into mitochondria, folding and retrograde movement of fumarase in yeast. J. Biol. Chem. 273, 25587-25593.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25587-25593
    • Knox, C.1    Sass, E.2    Neupert, W.3    Pines, O.4
  • 17
    • 77949891886 scopus 로고    scopus 로고
    • Identification and biochemical characterization of molybdenum cofactor-binding proteins from Arabidopsis thaliana
    • Kruse, T., Gehl, C., Geisler, M., Lehrke, M., Ringel, P., Hallier, S., Hänsch, R. and Mendel, R. R. (2010). Identification and biochemical characterization of molybdenum cofactor-binding proteins from Arabidopsis thaliana. J. Biol. Chem. 285, 6623-6635.
    • (2010) J. Biol. Chem. , vol.285 , pp. 6623-6635
    • Kruse, T.1    Gehl, C.2    Geisler, M.3    Lehrke, M.4    Ringel, P.5    Hallier, S.6    Hänsch, R.7    Mendel, R.R.8
  • 18
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R. F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 19
    • 0043239359 scopus 로고    scopus 로고
    • Import of small Tim proteins into the mitochondrial intermembrane space
    • Lutz, T., Neupert, W. and Herrmann, J. M. (2003). Import of small Tim proteins into the mitochondrial intermembrane space. EMBO J. 22, 4400-4408.
    • (2003) EMBO J. , vol.22 , pp. 4400-4408
    • Lutz, T.1    Neupert, W.2    Herrmann, J.M.3
  • 20
    • 0027104001 scopus 로고
    • Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy
    • Manders, E. M., Stap, J., Brakenhoff, G. J., van Driel, R. and Aten, J. A. (1992). Dynamics of three-dimensional replication patterns during the S-phase, analysed by double labelling of DNA and confocal microscopy. J. Cell Sci. 103, 857-862.
    • (1992) J. Cell Sci. , vol.103 , pp. 857-862
    • Manders, E.M.1    Stap, J.2    Brakenhoff, G.J.3    van Driel, R.4    Aten, J.A.5
  • 21
    • 0037119407 scopus 로고    scopus 로고
    • Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice
    • Mattiazzi, M., D'Aurelio, M., Gajewski, C. D., Martushova, K., Kiaei, M., Beal, M. F. and Manfredi, G. (2002). Mutated human SOD1 causes dysfunction of oxidative phosphorylation in mitochondria of transgenic mice. J. Biol. Chem. 277, 29626-29633.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29626-29633
    • Mattiazzi, M.1    D'Aurelio, M.2    Gajewski, C.D.3    Martushova, K.4    Kiaei, M.5    Beal, M.F.6    Manfredi, G.7
  • 23
    • 0023889423 scopus 로고
    • A mutant of Neurospora crassa deficient in cytochrome c heme lyase activity cannot import cytochrome c into mitochondria
    • Nargang, F. E., Drygas, M. E., Kwong, P. L., Nicholson, D. W. and Neupert, W. (1988). A mutant of Neurospora crassa deficient in cytochrome c heme lyase activity cannot import cytochrome c into mitochondria. J. Biol. Chem. 263, 9388-9394.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9388-9394
    • Nargang, F.E.1    Drygas, M.E.2    Kwong, P.L.3    Nicholson, D.W.4    Neupert, W.5
  • 24
    • 0015186726 scopus 로고
    • Invitro formation of assimilatory reduced nicotinamide adenine dinucleotide phosphate: nitrate reductase from a Neurospora mutant and a component of molybdenum-enzymes
    • Nason, A., Lee, K. Y., Pan, S. S., Ketchum, P. A., Lamberti, A. and DeVries, J. (1971). Invitro formation of assimilatory reduced nicotinamide adenine dinucleotide phosphate: nitrate reductase from a Neurospora mutant and a component of molybdenum-enzymes. Proc. Natl. Acad. Sci. USA 68, 3242-3246.
    • (1971) Proc. Natl. Acad. Sci. USA , vol.68 , pp. 3242-3246
    • Nason, A.1    Lee, K.Y.2    Pan, S.S.3    Ketchum, P.A.4    Lamberti, A.5    DeVries, J.6
  • 25
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert, W. and Herrmann, J. M. (2007). Translocation of proteins into mitochondria. Annu. Rev. Biochem. 76, 723-749.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 26
    • 0030964105 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: signals, mechanisms and regulation
    • Nigg, E. A. (1997). Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 386, 779-787.
    • (1997) Nature , vol.386 , pp. 779-787
    • Nigg, E.A.1
  • 27
    • 0027752461 scopus 로고
    • A mitochondrial protease with two catalytic subunits of nonoverlapping specificities
    • Nunnari, J., Fox, T. D. and Walter, P. (1993). A mitochondrial protease with two catalytic subunits of nonoverlapping specificities. Science 262, 1997-2004.
    • (1993) Science , vol.262 , pp. 1997-2004
    • Nunnari, J.1    Fox, T.D.2    Walter, P.3
  • 28
    • 0021381391 scopus 로고
    • Transport of the precursor for sulfite oxidase into intermembrane space of liver mitochondria: characterization of import and processing activities
    • Ono, H. and Ito, A. (1984). Transport of the precursor for sulfite oxidase into intermembrane space of liver mitochondria: characterization of import and processing activities. J. Biochem. 95, 345-352.
    • (1984) J. Biochem. , vol.95 , pp. 345-352
    • Ono, H.1    Ito, A.2
  • 29
    • 0029882611 scopus 로고    scopus 로고
    • Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli
    • Palmer, T., Santini, C.-L., Iobbi-Nivol, C., Eaves, D. J., Boxer, D. H. and Giordano, G. (1996). Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli. Mol. Microbiol. 20, 875-884.
    • (1996) Mol. Microbiol. , vol.20 , pp. 875-884
    • Palmer, T.1    Santini, C.-L.2    Iobbi-Nivol, C.3    Eaves, D.J.4    Boxer, D.H.5    Giordano, G.6
  • 30
    • 0035166780 scopus 로고    scopus 로고
    • A mutation in the gene for the neurotransmitter receptor-clustering protein gephyrin causes a novel form of molybdenum cofactor deficiency
    • Reiss, J., Gross-Hardt, S., Christensen, E., Schmidt, P., Mendel, R. R. and Schwarz, G. (2001). A mutation in the gene for the neurotransmitter receptor-clustering protein gephyrin causes a novel form of molybdenum cofactor deficiency. Am. J. Hum. Genet. 68, 208-213.
    • (2001) Am. J. Hum. Genet. , vol.68 , pp. 208-213
    • Reiss, J.1    Gross-Hardt, S.2    Christensen, E.3    Schmidt, P.4    Mendel, R.R.5    Schwarz, G.6
  • 31
    • 0035824654 scopus 로고    scopus 로고
    • Mitochondrial and cytosolic isoforms of yeast fumarase are derivatives of a single translation product and have identical amino termini
    • Sass, E., Blachinsky, E., Karniely, S. and Pines, O. (2001). Mitochondrial and cytosolic isoforms of yeast fumarase are derivatives of a single translation product and have identical amino termini. J. Biol. Chem. 276, 46111-46117.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46111-46117
    • Sass, E.1    Blachinsky, E.2    Karniely, S.3    Pines, O.4
  • 32
    • 28844475146 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis and deficiency
    • Schwarz, G. (2005). Molybdenum cofactor biosynthesis and deficiency. Cell. Mol. Life Sci. 62, 2792-2810.
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2792-2810
    • Schwarz, G.1
  • 33
    • 33745933654 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis and molybdenum enzymes
    • Schwarz, G. and Mendel, R. R. (2006). Molybdenum cofactor biosynthesis and molybdenum enzymes. Annu. Rev. Plant Biol. 57, 623-647.
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 623-647
    • Schwarz, G.1    Mendel, R.R.2
  • 34
    • 68949107281 scopus 로고    scopus 로고
    • Molybdenum cofactors, enzymes and pathways
    • Schwarz, G., Mendel, R. R. and Ribbe, M. W. (2009). Molybdenum cofactors, enzymes and pathways. Nature 460, 839-847.
    • (2009) Nature , vol.460 , pp. 839-847
    • Schwarz, G.1    Mendel, R.R.2    Ribbe, M.W.3
  • 35
    • 47749130013 scopus 로고    scopus 로고
    • Splice-specific functions of gephyrin in molybdenum cofactor biosynthesis
    • Smolinsky, B., Eichler, S. A., Buchmeier, S., Meier, J. C. and Schwarz, G. (2008). Splice-specific functions of gephyrin in molybdenum cofactor biosynthesis. J. Biol. Chem. 283, 17370-17379.
    • (2008) J. Biol. Chem. , vol.283 , pp. 17370-17379
    • Smolinsky, B.1    Eichler, S.A.2    Buchmeier, S.3    Meier, J.C.4    Schwarz, G.5
  • 36
    • 33646807833 scopus 로고    scopus 로고
    • Mammalian cysteine metabolism: new insights into regulation of cysteine metabolism
    • Stipanuk, M. H., Dominy, J. E., Jr, Lee, J. I. and Coloso, R. M. (2006). Mammalian cysteine metabolism: new insights into regulation of cysteine metabolism. J. Nutr. 136 Suppl, 1652S-1659S.
    • (2006) J. Nutr. , vol.136 SUPPL
    • Stipanuk, M.H.1    Dominy Jr., J.E.2    Lee, J.I.3    Coloso, R.M.4


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