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Volumn 16, Issue 13, 2007, Pages 1534-1540

In vivo maturation of human frataxin

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; FRATAXIN;

EID: 34447318623     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddm102     Document Type: Article
Times cited : (101)

References (38)
  • 3
    • 0035920101 scopus 로고    scopus 로고
    • Sticky DNA, a self-associated complex formed at long GAA*TTC repeats in intron 1 of the frataxin gene, inhibits transcription
    • Sakamoto, N., Ohshima, K., Montermini, L., Pandolfo, M. and Wells, R.D. (2001) Sticky DNA, a self-associated complex formed at long GAA*TTC repeats in intron 1 of the frataxin gene, inhibits transcription. J. Biol. Chem., 276, 27171-27177.
    • (2001) J. Biol. Chem , vol.276 , pp. 27171-27177
    • Sakamoto, N.1    Ohshima, K.2    Montermini, L.3    Pandolfo, M.4    Wells, R.D.5
  • 5
    • 2942744572 scopus 로고    scopus 로고
    • Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
    • Yoon, T. and Cowan, J.A. (2004) Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis. J. Biol. Chem. 279, 25943-25946.
    • (2004) J. Biol. Chem , vol.279 , pp. 25943-25946
    • Yoon, T.1    Cowan, J.A.2
  • 6
    • 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
  • 7
    • 0036472291 scopus 로고    scopus 로고
    • Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
    • Cavadini, P., O'Neill, H.A., Benada, O. and Isaya, G. (2002) Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia. Hum. Mol. Genet., 11, 217-227.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 217-227
    • Cavadini, P.1    O'Neill, H.A.2    Benada, O.3    Isaya, G.4
  • 8
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau, A.L., O'Neill, H.A., Kennedy, M.C., Ikeda-Saito, M., Isaya, G. and Szweda, L.I. (2004) Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science, 305, 242-245.
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 14
    • 0035976855 scopus 로고    scopus 로고
    • Manganese superoxide dismutase induction by iron is impaired in Friedreich ataxia cells
    • Jiralerspong, S., Ge, B., Hudson, T.J. and Pandolfo, M. (2001) Manganese superoxide dismutase induction by iron is impaired in Friedreich ataxia cells. FEBS Lett., 509, 101-105.
    • (2001) FEBS Lett , vol.509 , pp. 101-105
    • Jiralerspong, S.1    Ge, B.2    Hudson, T.J.3    Pandolfo, M.4
  • 15
    • 0033054177 scopus 로고    scopus 로고
    • The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • Wong, A., Yang, J., Cavadini, P., Gellera, C., Lonnerdal, B., Taroni, F. and Cortopassi, G. (1999) The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet., 8, 425-430.
    • (1999) Hum. Mol. Genet , vol.8 , pp. 425-430
    • Wong, A.1    Yang, J.2    Cavadini, P.3    Gellera, C.4    Lonnerdal, B.5    Taroni, F.6    Cortopassi, G.7
  • 17
    • 33745222541 scopus 로고    scopus 로고
    • A pool of extramitochondrial frataxin that promotes cell survival
    • Condò, I., Ventura, N., Malisan, F., Tomassini, B. and Testi, R. (2006) A pool of extramitochondrial frataxin that promotes cell survival. J. Biol. Chem., 281, 16750-16756.
    • (2006) J. Biol. Chem , vol.281 , pp. 16750-16756
    • Condò, I.1    Ventura, N.2    Malisan, F.3    Tomassini, B.4    Testi, R.5
  • 19
    • 1442324707 scopus 로고    scopus 로고
    • Friedreich ataxia mouse models with progressive cerebellar and sensory ataxia reveal autophagic neurodegeneration in dorsal root ganglia
    • Simon, D., Seznec, H., Gansmuller, A., Carelle, N., Weber, P., Metzger, D., Rustin, P., Koenig, M. and Puccio, H. (2004) Friedreich ataxia mouse models with progressive cerebellar and sensory ataxia reveal autophagic neurodegeneration in dorsal root ganglia. J. Neurosci., 24, 1987-1995.
    • (2004) J. Neurosci , vol.24 , pp. 1987-1995
    • Simon, D.1    Seznec, H.2    Gansmuller, A.3    Carelle, N.4    Weber, P.5    Metzger, D.6    Rustin, P.7    Koenig, M.8    Puccio, H.9
  • 21
    • 0031656903 scopus 로고    scopus 로고
    • Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase
    • Koutnikova, H., Campuzano, V. and Koenig, M. (1998) Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase. Hum. Mol. Genet., 7, 1485-1489.
    • (1998) Hum. Mol. Genet , vol.7 , pp. 1485-1489
    • Koutnikova, H.1    Campuzano, V.2    Koenig, M.3
  • 22
    • 0034731447 scopus 로고    scopus 로고
    • Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates
    • Cavadini, P., Adamec, J., Taroni, F., Gakh, O. and Isaya, G. (2000) Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates. J. Biol. Chem., 275, 41469-41475.
    • (2000) J. Biol. Chem , vol.275 , pp. 41469-41475
    • Cavadini, P.1    Adamec, J.2    Taroni, F.3    Gakh, O.4    Isaya, G.5
  • 24
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault, T.A. and Tong, W.H. (2005) Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat. Rev. Mol. Cell. Biol., 6 345-351.
    • (2005) Nat. Rev. Mol. Cell. Biol , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 25
    • 0033529554 scopus 로고    scopus 로고
    • Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidase
    • Branda, S.S., Cavadini, P., Adamec, J., Kalousek, F., Taroni, F. and Isaya, G. (1999) Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidase. J. Biol. Chem., 274, 22763-22769.
    • (1999) J. Biol. Chem , vol.274 , pp. 22763-22769
    • Branda, S.S.1    Cavadini, P.2    Adamec, J.3    Kalousek, F.4    Taroni, F.5    Isaya, G.6
  • 26
    • 0032695778 scopus 로고    scopus 로고
    • Maturation of frataxin within mammalian and yeast mitochondria: One-step processing by matrix processing peptidase
    • Gordon, D.M., Shi, Q., Dancis, A. and Pain, D. (1999) Maturation of frataxin within mammalian and yeast mitochondria: One-step processing by matrix processing peptidase. Hum. Mol. Genet., 8, 2255-2262.
    • (1999) Hum. Mol. Genet , vol.8 , pp. 2255-2262
    • Gordon, D.M.1    Shi, Q.2    Dancis, A.3    Pain, D.4
  • 27
    • 0034940401 scopus 로고    scopus 로고
    • Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences
    • Taylor, A.B., Smith, B.S., Kitada, S., Kojima, K., Miyaura, H., Otwinowski, Z., Ito, A. and Deisenhofer, J. (2001) Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences. Structure, 9, 615-625.
    • (2001) Structure , vol.9 , pp. 615-625
    • Taylor, A.B.1    Smith, B.S.2    Kitada, S.3    Kojima, K.4    Miyaura, H.5    Otwinowski, Z.6    Ito, A.7    Deisenhofer, J.8
  • 28
    • 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. (1987) Import of rat ornithine transcarbamylase precursor into mitochondria: Two-step processing of the leader peptide. J. Cell. Biol., 105, 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
  • 29
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio, H., Simon, D., Cossée, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P. and Koenig, M. (2001) Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet., 27, 181-186.
    • (2001) Nat. Genet , vol.27 , pp. 181-186
    • Puccio, H.1    Simon, D.2    Cossée, M.3    Criqui-Filipe, P.4    Tiziano, F.5    Melki, J.6    Hindelang, C.7    Matyas, R.8    Rustin, P.9    Koenig, M.10
  • 30
    • 0037126057 scopus 로고    scopus 로고
    • Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: Evidence that Yfh1p affects Fe-S cluster synthesis
    • Chen, O.S., Hemenway, S. and Kaplan, J. (2002) Inhibition of Fe-S cluster biosynthesis decreases mitochondrial iron export: Evidence that Yfh1p affects Fe-S cluster synthesis. Proc. Natl Acad. Sci. USA, 99, 12321-12326.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12321-12326
    • Chen, O.S.1    Hemenway, S.2    Kaplan, J.3
  • 31
    • 0037613459 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins
    • Yoon, T. and Cowan, J.A. (2003) Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. J. Am. Chem. Soc., 125, 6078-6084.
    • (2003) J. Am. Chem. Soc , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 32
    • 17844393112 scopus 로고    scopus 로고
    • Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/ reperfusion
    • Bulteau, A.L., Lundberg, K.C., Ikeda-Saito, M., Isaya, G. and Szweda, L.I. (2005) Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/ reperfusion. Proc. Natl Acad. Sci. USA, 102, 5987-5991.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5987-5991
    • Bulteau, A.L.1    Lundberg, K.C.2    Ikeda-Saito, M.3    Isaya, G.4    Szweda, L.I.5
  • 35
    • 34247643174 scopus 로고    scopus 로고
    • N-terminal iron-mediated self-cleavage of human frataxin: Regulation of iron binding and complex formation with target proteins
    • Yoon, T., Dizin, E. and Cowan, J.A. (2007) N-terminal iron-mediated self-cleavage of human frataxin: Regulation of iron binding and complex formation with target proteins. J. Biol. Inorg. Chem., 12, 535-542.
    • (2007) J. Biol. Inorg. Chem , vol.12 , pp. 535-542
    • Yoon, T.1    Dizin, E.2    Cowan, J.A.3
  • 36
    • 9644284455 scopus 로고    scopus 로고
    • Supramolecular assemblies of human frataxin are formed via subunit-subunit interactions mediated by a non-conserved amino-terminal region
    • O'Neill, H.A., Gakh, O. and Isaya, G. (2005) Supramolecular assemblies of human frataxin are formed via subunit-subunit interactions mediated by a non-conserved amino-terminal region. J. Mol. Biol., 345 433-439.
    • (2005) J. Mol. Biol , vol.345 , pp. 433-439
    • O'Neill, H.A.1    Gakh, O.2    Isaya, G.3
  • 37
    • 9644279682 scopus 로고    scopus 로고
    • Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo
    • Aloria, K., Schilke, B., Andrew, A. and Craig, E.A. (2004) Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo. EMBO Rep., 5, 1096-1101.
    • (2004) EMBO Rep , vol.5 , pp. 1096-1101
    • Aloria, K.1    Schilke, B.2    Andrew, A.3    Craig, E.A.4
  • 38
    • 31544445770 scopus 로고    scopus 로고
    • Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity
    • Gakh, O., Park, S., Liu, G., Macomber, L., Imlay, J.A., Ferreira, G.C. and Isaya, G. (2006) Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity. Hum. Mol. Genet., 15, 467-479.
    • (2006) Hum. Mol. Genet , vol.15 , pp. 467-479
    • Gakh, O.1    Park, S.2    Liu, G.3    Macomber, L.4    Imlay, J.A.5    Ferreira, G.C.6    Isaya, G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.