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Volumn 471, Issue 2, 2015, Pages 231-241

Human mitochondrial MIA40 (CHCHD4) is a component of the Fe-S cluster export machinery

Author keywords

CIA; GPAT; HMIA40; Iron export; Iron sulfur (Fe S) cluster; Mitochondria

Indexed keywords

COILED COIL HELIX COILED COIL HELIX DOMAIN CONTAINING 4; HUMAN MITOCHONDRIAL MIA40 PROTEIN; IRON; IRON BINDING PROTEIN; MANGANESE; MITOCHONDRIAL PROTEIN; SULFUR; UNCLASSIFIED DRUG; CARRIER PROTEIN; MIA40 PROTEIN, HUMAN;

EID: 84943223770     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20150012     Document Type: Article
Times cited : (12)

References (44)
  • 1
    • 84858015433 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur clusters in mammalian cells: New insights and relevance to human disease
    • Rouault, T. A. (2012) Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease. Dis. Model. Mech. 5, 155-164
    • (2012) Dis. Model. Mech. , vol.5 , pp. 155-164
    • Rouault, T.A.1
  • 2
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: Ancient structures, still full of surprises
    • Beinert, H. (2000) Iron-sulfur proteins: ancient structures, still full of surprises. J. Biol. Inorg. Chem. 5, 2-15
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 2-15
    • Beinert, H.1
  • 4
    • 35348895032 scopus 로고    scopus 로고
    • DNA repair glycosylases with a [4Fe-4S] cluster: A redox cofactor for DNA-mediated charge transport?
    • Boal, A. K., Yavin, E. and Barton, J. K. (2007) DNA repair glycosylases with a [4Fe-4S] cluster: a redox cofactor for DNA-mediated charge transport? J. Inorg. Biochem. 101, 1913-1921
    • (2007) J. Inorg. Biochem. , vol.101 , pp. 1913-1921
    • Boal, A.K.1    Yavin, E.2    Barton, J.K.3
  • 5
    • 0001531848 scopus 로고    scopus 로고
    • Protein control of redox potentials of iron-sulfur proteins
    • Stephens, P. J., Jollie, D. R. and Warshel, A. (1996) Protein control of redox potentials of iron-sulfur proteins. Chem. Rev. 96, 2491-2514
    • (1996) Chem. Rev. , vol.96 , pp. 2491-2514
    • Stephens, P.J.1    Jollie, D.R.2    Warshel, A.3
  • 7
    • 0032540929 scopus 로고    scopus 로고
    • Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis
    • Knight, S. A., Sepuri, N. B., Pain, D. and Dancis, A. (1998) Mt-Hsp70 homolog, Ssc2p, required for maturation of yeast frataxin and mitochondrial iron homeostasis. J. Biol. Chem. 273, 18389-18393
    • (1998) J. Biol. Chem. , vol.273 , pp. 18389-18393
    • Knight, S.A.1    Sepuri, N.B.2    Pain, D.3    Dancis, A.4
  • 8
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters: Identification of an iscSUA -hscBA -fdx gene cluster from Azotobacter vinelandii
    • Zheng, L., Cash, V. L., Flint, D. H. and Dean, D. R. (1998) Assembly of iron-sulfur clusters: identification of an iscSUA -hscBA -fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273, 13264-13272
    • (1998) J. Biol. Chem. , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 9
  • 10
    • 2942565619 scopus 로고    scopus 로고
    • The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins
    • Balk, J., Pierik, A. J., Netz, D. J., Muhlenhoff, U. and Lill, R. (2004) The hydrogenase-like Nar1p is essential for maturation of cytosolic and nuclear iron-sulphur proteins. EMBO J. 23, 2105-2115
    • (2004) EMBO J. , vol.23 , pp. 2105-2115
    • Balk, J.1    Pierik, A.J.2    Netz, D.J.3    Muhlenhoff, U.4    Lill, R.5
  • 11
    • 33751177803 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes: Components and mechanisms
    • Lill, R. and Muhlenhoff, U. (2006) Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms. Annu. Rev. Cell Dev. Biol. 22, 457-486
    • (2006) Annu. Rev. Cell Dev. Biol. , vol.22 , pp. 457-486
    • Lill, R.1    Muhlenhoff, U.2
  • 12
    • 9744248303 scopus 로고    scopus 로고
    • Iron-sulfur protein maturation in human cells: Evidence for a function of frataxin
    • Stehling, O., Elsasser, H. P., Bruckel, B., Muhlenhoff, U. and Lill, R. (2004) Iron-sulfur protein maturation in human cells: evidence for a function of frataxin. Hum. Mol. Genet. 13, 3007-3015
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 3007-3015
    • Stehling, O.1    Elsasser, H.P.2    Bruckel, B.3    Muhlenhoff, U.4    Lill, R.5
  • 13
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • Kispal, G., Csere, P., Prohl, C. and Lill, R. (1999) The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18, 3981-3989
    • (1999) EMBO J. , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 14
    • 4344595102 scopus 로고    scopus 로고
    • Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae
    • Muhlenhoff, U., Balk, J., Richhardt, N., Kaiser, J. T., Sipos, K., Kispal, G. and Lill, R. (2004) Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae. J. Biol. Chem. 279, 36906-36915
    • (2004) J. Biol. Chem. , vol.279 , pp. 36906-36915
    • Muhlenhoff, U.1    Balk, J.2    Richhardt, N.3    Kaiser, J.T.4    Sipos, K.5    Kispal, G.6    Lill, R.7
  • 15
    • 0030608677 scopus 로고    scopus 로고
    • The ABC transporter Atm1p is required for mitochondrial iron homeostasis
    • Kispal, G., Csere, P., Guiard, B. and Lill, R. (1997) The ABC transporter Atm1p is required for mitochondrial iron homeostasis. FEBS Lett. 418, 346-350
    • (1997) FEBS Lett. , vol.418 , pp. 346-350
    • Kispal, G.1    Csere, P.2    Guiard, B.3    Lill, R.4
  • 16
    • 0028855545 scopus 로고
    • An ABC transporter in the mitochondrial inner membrane is required for normal growth of yeast
    • Leighton, J. and Schatz, G. (1995) An ABC transporter in the mitochondrial inner membrane is required for normal growth of yeast. EMBO J. 14, 188-195
    • (1995) EMBO J. , vol.14 , pp. 188-195
    • Leighton, J.1    Schatz, G.2
  • 17
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill, R. (2009) Function and biogenesis of iron-sulphur proteins. Nature 460, 831-838
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 18
  • 19
    • 84856853161 scopus 로고    scopus 로고
    • Mitochondrial disulfide relay: Redox-regulated protein import into the intermembrane space
    • Herrmann, J. M. and Riemer, J. (2012) Mitochondrial disulfide relay: redox-regulated protein import into the intermembrane space. J. Biol. Chem. 287, 4426-4433
    • (2012) J. Biol. Chem. , vol.287 , pp. 4426-4433
    • Herrmann, J.M.1    Riemer, J.2
  • 20
    • 27144438677 scopus 로고    scopus 로고
    • Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c
    • Allen, S., Balabanidou, V., Sideris, D. P., Lisowsky, T. and Tokatlidis, K. (2005) Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c. J. Mol. Biol. 353, 937-944
    • (2005) J. Mol. Biol. , vol.353 , pp. 937-944
    • Allen, S.1    Balabanidou, V.2    Sideris, D.P.3    Lisowsky, T.4    Tokatlidis, K.5
  • 22
    • 59449099000 scopus 로고    scopus 로고
    • Structural and functional roles of the conserved cysteine residues of the redox-regulated import receptor Mia40 in the intermembrane space of mitochondria
    • Terziyska, N., Grumbt, B., Kozany, C. and Hell, K. (2009) Structural and functional roles of the conserved cysteine residues of the redox-regulated import receptor Mia40 in the intermembrane space of mitochondria. J. Biol. Chem. 284, 1353-1363
    • (2009) J. Biol. Chem. , vol.284 , pp. 1353-1363
    • Terziyska, N.1    Grumbt, B.2    Kozany, C.3    Hell, K.4
  • 23
    • 26244466764 scopus 로고    scopus 로고
    • Functional and mutational characterization of human MIA40 acting during import into the mitochondrial intermembrane space
    • Hofmann, S., Rothbauer, U., Muhlenbein, N., Baiker, K., Hell, K. and Bauer, M. F. (2005) Functional and mutational characterization of human MIA40 acting during import into the mitochondrial intermembrane space. J. Mol. Biol. 353, 517-528
    • (2005) J. Mol. Biol. , vol.353 , pp. 517-528
    • Hofmann, S.1    Rothbauer, U.2    Muhlenbein, N.3    Baiker, K.4    Hell, K.5    Bauer, M.F.6
  • 25
    • 66649106947 scopus 로고    scopus 로고
    • Augmenter of liver regeneration: Substrate specificity of a flavin-dependent oxidoreductase from the mitochondrial intermembrane space
    • Daithankar, V. N., Farrell, S. R. and Thorpe, C. (2009) Augmenter of liver regeneration: substrate specificity of a flavin-dependent oxidoreductase from the mitochondrial intermembrane space. Biochemistry 48, 4828-4837
    • (2009) Biochemistry , vol.48 , pp. 4828-4837
    • Daithankar, V.N.1    Farrell, S.R.2    Thorpe, C.3
  • 26
    • 84884270447 scopus 로고    scopus 로고
    • Identification and characterization of mitochondrial Mia40 as an iron-sulfur protein
    • Spiller, M. P., Ang, S. K., Ceh-Pavia, E., Fisher, K., Wang, Q., Rigby, S. E. and Lu, H. (2013) Identification and characterization of mitochondrial Mia40 as an iron-sulfur protein. Biochem. J. 455, 27-35
    • (2013) Biochem. J. , vol.455 , pp. 27-35
    • Spiller, M.P.1    Ang, S.K.2    Ceh-Pavia, E.3    Fisher, K.4    Wang, Q.5    Rigby, S.E.6    Lu, H.7
  • 28
    • 84921875052 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase 2 reversibly regulates Mge1, a cochaperone of mitochondrial Hsp70 during oxidative stress
    • Allu, P. K., Marada, A., Boggula, Y., Karri, S., Krishnamoorthy, T. and Sepuri, N. B. (2015) Methionine sulfoxide reductase 2 reversibly regulates Mge1, a cochaperone of mitochondrial Hsp70 during oxidative stress. Mol. Biol. Cell 26, 406-419
    • (2015) Mol. Biol. Cell , vol.26 , pp. 406-419
    • Allu, P.K.1    Marada, A.2    Boggula, Y.3    Karri, S.4    Krishnamoorthy, T.5    Sepuri, N.B.6
  • 29
    • 84892772006 scopus 로고    scopus 로고
    • Perturbation of apoptosis upon binding of tRNA to the heme domain of cytochrome c
    • Gorla, M. and Sepuri, N. B. (2014) Perturbation of apoptosis upon binding of tRNA to the heme domain of cytochrome c. Apoptosis 19, 259-268
    • (2014) Apoptosis , vol.19 , pp. 259-268
    • Gorla, M.1    Sepuri, N.B.2
  • 30
    • 0020725989 scopus 로고
    • Characterization of periplasmic hydrogenase from Desulfovibrio vulgaris Miyazaki K
    • Aketagawa, J., Kobayashi, K. and Ishimoto, M. (1983) Characterization of periplasmic hydrogenase from Desulfovibrio vulgaris Miyazaki K. J. Biochem. 93, 755-762
    • (1983) J. Biochem. , vol.93 , pp. 755-762
    • Aketagawa, J.1    Kobayashi, K.2    Ishimoto, M.3
  • 31
    • 14844290234 scopus 로고    scopus 로고
    • Evidence that the Streptomyces developmental protein WhiD, a member of the WhiB family, binds a [4Fe-4S] cluster
    • Jakimowicz, P., Cheesman, M. R., Bishai, W. R., Chater, K. F., Thomson, A. J. and Buttner, M. J. (2005) Evidence that the Streptomyces developmental protein WhiD, a member of the WhiB family, binds a [4Fe-4S] cluster. J. Biol. Chem. 280, 8309-8315
    • (2005) J. Biol. Chem. , vol.280 , pp. 8309-8315
    • Jakimowicz, P.1    Cheesman, M.R.2    Bishai, W.R.3    Chater, K.F.4    Thomson, A.J.5    Buttner, M.J.6
  • 32
    • 84874066734 scopus 로고    scopus 로고
    • The import of the transcription factor STAT3 into mitochondria depends on GRIM-19, a component of the electron transport chain
    • Tammineni, P., Anugula, C., Mohammed, F., Anjaneyulu, M., Larner, A. C. and Sepuri, N. B. (2013) The import of the transcription factor STAT3 into mitochondria depends on GRIM-19, a component of the electron transport chain. J. Biol. Chem. 288, 4723-4732
    • (2013) J. Biol. Chem. , vol.288 , pp. 4723-4732
    • Tammineni, P.1    Anugula, C.2    Mohammed, F.3    Anjaneyulu, M.4    Larner, A.C.5    Sepuri, N.B.6
  • 33
    • 0019319179 scopus 로고
    • Mitochondrial iron not bound in heme and iron-sulfur centers: Estimation, compartmentation and redox state
    • Tangeras, A., Flatmark, T., Backstrom, D. and Ehrenberg, A. (1980) Mitochondrial iron not bound in heme and iron-sulfur centers: estimation, compartmentation and redox state. Biochim. Biophys. Acta 589, 162-175
    • (1980) Biochim. Biophys. Acta , vol.589 , pp. 162-175
    • Tangeras, A.1    Flatmark, T.2    Backstrom, D.3    Ehrenberg, A.4
  • 34
    • 49849095991 scopus 로고    scopus 로고
    • Xanthine oxidase and mitochondria contribute to vascular superoxide anion generation in DOCA-salt hypertensive rats
    • Viel, E. C., Benkirane, K., Javeshghani, D., Touyz, R. M. and Schiffrin, E. L. (2008) Xanthine oxidase and mitochondria contribute to vascular superoxide anion generation in DOCA-salt hypertensive rats. Am. J. Physiol. Heart Circ. Physiol. 295, H281-H288
    • (2008) Am. J. Physiol. Heart Circ. Physiol. , vol.295 , pp. H281-H288
    • Viel, E.C.1    Benkirane, K.2    Javeshghani, D.3    Touyz, R.M.4    Schiffrin, E.L.5
  • 35
    • 63449114461 scopus 로고    scopus 로고
    • Reliable assay for measuring complex I activity in human blood lymphocytes and skin fibroblasts
    • de Wit, L. E. and Sluiter, W. (2009) Reliable assay for measuring complex I activity in human blood lymphocytes and skin fibroblasts. Methods Enzymol. 456, 169-181
    • (2009) Methods Enzymol. , vol.456 , pp. 169-181
    • De Wit, L.E.1    Sluiter, W.2
  • 37
    • 0035933791 scopus 로고    scopus 로고
    • Iron-sulfur cluster assembly: Characterization of IscA and evidence for a specific and functional complex with ferredoxin
    • Ollagnier-de-Choudens, S., Mattioli, T., Takahashi, Y. and Fontecave, M. (2001) Iron-sulfur cluster assembly: characterization of IscA and evidence for a specific and functional complex with ferredoxin. J. Biol. Chem. 276, 22604-22607
    • (2001) J. Biol. Chem. , vol.276 , pp. 22604-22607
    • Ollagnier-De-Choudens, S.1    Mattioli, T.2    Takahashi, Y.3    Fontecave, M.4
  • 38
    • 84885117582 scopus 로고    scopus 로고
    • Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)
    • Cai, K., Frederick, R. O., Kim, J. H., Reinen, N. M., Tonelli, M. and Markley, J. L. (2013) Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU). J. Biol. Chem. 288, 28755-28770
    • (2013) J. Biol. Chem. , vol.288 , pp. 28755-28770
    • Cai, K.1    Frederick, R.O.2    Kim, J.H.3    Reinen, N.M.4    Tonelli, M.5    Markley, J.L.6
  • 39
    • 0037214441 scopus 로고    scopus 로고
    • Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion
    • Varghese, S., Tang, Y. and Imlay, J. A. (2003) Contrasting sensitivities of Escherichia coli aconitases A and B to oxidation and iron depletion. J. Bacteriol. 185, 221-230
    • (2003) J. Bacteriol. , vol.185 , pp. 221-230
    • Varghese, S.1    Tang, Y.2    Imlay, J.A.3
  • 41
    • 0037397764 scopus 로고    scopus 로고
    • Formation of iron-sulfur clusters in bacteria: An emerging field in bioinorganic chemistry
    • Frazzon, J. and Dean, D. R. (2003) Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry. Curr. Opin. Chem. Biol. 7, 166-173
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 166-173
    • Frazzon, J.1    Dean, D.R.2
  • 43
    • 34147165135 scopus 로고    scopus 로고
    • RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload
    • Cavadini, P., Biasiotto, G., Poli, M., Levi, S., Verardi, R., Zanella, I., Derosas, M., Ingrassia, R., Corrado, M. and Arosio, P. (2007) RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload. Blood 109, 3552-3559
    • (2007) Blood , vol.109 , pp. 3552-3559
    • Cavadini, P.1    Biasiotto, G.2    Poli, M.3    Levi, S.4    Verardi, R.5    Zanella, I.6    Derosas, M.7    Ingrassia, R.8    Corrado, M.9    Arosio, P.10
  • 44
    • 0034866458 scopus 로고    scopus 로고
    • An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins
    • Lange, H., Lisowsky, T., Gerber, J., Muhlenhoff, U., Kispal, G. and Lill, R. (2001) An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep. 2, 715-720
    • (2001) EMBO Rep. , vol.2 , pp. 715-720
    • Lange, H.1    Lisowsky, T.2    Gerber, J.3    Muhlenhoff, U.4    Kispal, G.5    Lill, R.6


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