메뉴 건너뛰기




Volumn 345, Issue 3, 2005, Pages 433-439

Supramolecular assemblies of human frataxin are formed via subunit-subunit interactions mediated by a non-conserved amino-terminal region

Author keywords

assembly; frataxin; iron; IscU; mitochondria

Indexed keywords

FRATAXIN; IRON; MONOMER; OLIGOMER; POLYMER; PROTEIN; PROTEIN ISCU; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 9644284455     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.10.074     Document Type: Article
Times cited : (53)

References (21)
  • 2
    • 13344270899 scopus 로고    scopus 로고
    • Friedreich's ataxia: Autosomal recessive disease caused by an intronic GAA triplet repeat expansion
    • V. Campuzano, L. Montermini, M.D. Molto, L. Pianese, M. Cossee, and F. Cavalcanti Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion Science 271 1996 1423 1427
    • (1996) Science , vol.271 , pp. 1423-1427
    • Campuzano, V.1    Montermini, L.2    Molto, M.D.3    Pianese, L.4    Cossee, M.5    Cavalcanti, F.6
  • 3
    • 0034731447 scopus 로고    scopus 로고
    • Two-step processing of human frataxin by mitochondrial processing peptidase: Precursor and intermediate forms are cleaved at different rates
    • P. Cavadini, J. Adamec, F. Taroni, O. Gakh, and G. Isaya Two-step processing of human frataxin by mitochondrial processing peptidase: precursor and intermediate forms are cleaved at different rates J. Biol. Chem. 275 2000 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
  • 4
  • 5
    • 0036472291 scopus 로고    scopus 로고
    • Assembly and iron binding properties of human frataxin, the protein deficient in Friedreich ataxia
    • P. Cavadini, H.A. O'Neill, O. Benada, and G. Isaya Assembly and iron binding properties of human frataxin, the protein deficient in Friedreich ataxia Hum. Mol. Genet. 33 2002 217 227
    • (2002) Hum. Mol. Genet. , vol.33 , pp. 217-227
    • Cavadini, P.1    O'Neill, H.A.2    Benada, O.3    Isaya, G.4
  • 7
    • 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
    • T. Yoon, and J.A. Cowan 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 2003 6078 6084
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 8
    • 0042232045 scopus 로고    scopus 로고
    • Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation
    • S. Park, O. Gakh, H.A. O'Neill, A. Mangravita, H. Nichol, G.C. Ferreira, and G. Isaya Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation J. Biol. Chem. 278 2003 31340 31351
    • (2003) J. Biol. Chem. , vol.278 , pp. 31340-31351
    • Park, S.1    Gakh, O.2    O'Neill, H.A.3    Mangravita, A.4    Nichol, H.5    Ferreira, G.C.6    Isaya, G.7
  • 9
    • 2942744572 scopus 로고    scopus 로고
    • Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
    • T. Yoon, and J.A. Cowan Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis J. Biol. Chem. 279 2004 25943 25946
    • (2004) J. Biol. Chem. , vol.279 , pp. 25943-25946
    • Yoon, T.1    Cowan, J.A.2
  • 10
    • 3042763187 scopus 로고    scopus 로고
    • A novel role of frataxin as an iron chaperone protein required for pro-oxidant induced modulation of mitochondrial aconitase activity
    • A.L. Bulteau, H.A. O'Neill, M.C. Kennedy, M. Ikeda-Saito, G. Isaya, and L.I. Szweda A novel role of frataxin as an iron chaperone protein required for pro-oxidant induced modulation of mitochondrial aconitase activity Science 305 2004 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
  • 11
    • 0036667986 scopus 로고    scopus 로고
    • A structural approach to understanding the iron-binding properties of phylogenetically different frataxins
    • S. Adinolfi, M. Trifuoggi, A.S. Politou, S. Martin, and A. Pastore A structural approach to understanding the iron-binding properties of phylogenetically different frataxins Hum. Mol. Genet. 11 2002 1865 1877
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1865-1877
    • Adinolfi, S.1    Trifuoggi, M.2    Politou, A.S.3    Martin, S.4    Pastore, A.5
  • 12
    • 0019816427 scopus 로고
    • Ferritin polymers and the formation of haemosiderin
    • T.G. Hoy, and A. Jacobs Ferritin polymers and the formation of haemosiderin Br. J. Haematol. 49 1981 593 602
    • (1981) Br. J. Haematol. , vol.49 , pp. 593-602
    • Hoy, T.G.1    Jacobs, A.2
  • 13
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1
    • J. Gerber, U. Muhlenhoff, and R. Lill An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1 EMBO Rep. 4 2003 906 911
    • (2003) EMBO Rep. , vol.4 , pp. 906-911
    • Gerber, J.1    Muhlenhoff, U.2    Lill, R.3
  • 14
    • 1642573170 scopus 로고    scopus 로고
    • Mitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae
    • A. Ramazzotti, V. Vanmansart, and F. Foury Mitochondrial functional interactions between frataxin and Isu1p, the iron-sulfur cluster scaffold protein, in Saccharomyces cerevisiae FEBS Letters 557 2004 215 220
    • (2004) FEBS Letters , vol.557 , pp. 215-220
    • Ramazzotti, A.1    Vanmansart, V.2    Foury, F.3
  • 16
    • 3142722152 scopus 로고    scopus 로고
    • The heme synthesis defect of mutants impaired in mitochondrial iron-sulfur protein biogenesis is caused by reversible inhibition of ferrochelatase
    • H. Lange, U. Muhlenhoff, M. Denzel, G. Kispal, and R. Lill The heme synthesis defect of mutants impaired in mitochondrial iron-sulfur protein biogenesis is caused by reversible inhibition of ferrochelatase J. Biol. Chem. 279 2004 29101 29108
    • (2004) J. Biol. Chem. , vol.279 , pp. 29101-29108
    • Lange, H.1    Muhlenhoff, U.2    Denzel, M.3    Kispal, G.4    Lill, R.5
  • 17
    • 0037197897 scopus 로고    scopus 로고
    • Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: Implications for the mechanism of iron-sulfur cluster assembly
    • S. Kato, H. Mihara, T. Kurihara, Y. Takahashi, U. Tokumoto, T. Yoshimura, and N. Esaki Cys-328 of IscS and Cys-63 of IscU are the sites of disulfide bridge formation in a covalently bound IscS/IscU complex: implications for the mechanism of iron-sulfur cluster assembly Proc. Natl Acad. Sci. USA 99 2002 5948 5952
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 5948-5952
    • Kato, S.1    Mihara, H.2    Kurihara, T.3    Takahashi, Y.4    Tokumoto, U.5    Yoshimura, T.6    Esaki, N.7
  • 19
    • 9644255849 scopus 로고    scopus 로고
    • Assembly of human frataxin is a mechanism to detoxify redox-active iron
    • in press.
    • O'Neill, H. A., Gakh, O., Park, S., Cui, J., Mooney, S. M., Sampson, M. et al. (2004). Assembly of human frataxin is a mechanism to detoxify redox-active iron. Biochemistry, in press.
    • (2004) Biochemistry
    • O'Neill, H.A.1    Gakh, O.2    Park, S.3    Cui, J.4    Mooney, S.M.5    Sampson, M.6
  • 20
    • 0034661480 scopus 로고    scopus 로고
    • Towards a structural understanding of Friedreich's ataxia: The solution structure of frataxin
    • G. Musco, G. Stier, B. Kolmerer, S. Adinolfi, S. Martin, and T. Frenkiel Towards a structural understanding of Friedreich's ataxia: the solution structure of frataxin Struct. Fold. Des. 8 2000 695 707
    • (2000) Struct. Fold. Des. , vol.8 , pp. 695-707
    • Musco, G.1    Stier, G.2    Kolmerer, B.3    Adinolfi, S.4    Martin, S.5    Frenkiel, T.6
  • 21
    • 9644279682 scopus 로고    scopus 로고
    • Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo
    • K. Aloria, B. Schilke, A. Andrew, and E.A. Craig Iron-induced oligomerization of yeast frataxin homologue Yfh1 is dispensable in vivo EMBO Rep. 5 2004 1096 1101
    • (2004) EMBO Rep. , vol.5 , pp. 1096-1101
    • Aloria, K.1    Schilke, B.2    Andrew, A.3    Craig, E.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.