메뉴 건너뛰기




Volumn 111, Issue 17, 2014, Pages 6203-6208

[2Fe-2S] cluster transfer in iron-sulfur protein biogenesis

Author keywords

Fe S protein maturation; Monothiol Grxs; NMR; 2Fe 2S cluster transfer mechanism

Indexed keywords

CARRIER PROTEIN; GLUTAREDOXIN; GLUTATHIONE; IRON SULFUR PROTEIN; METALLOCHAPERONE; SCAFFOLD PROTEIN;

EID: 84899624154     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1400102111     Document Type: Article
Times cited : (113)

References (41)
  • 1
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R (2009) Function and biogenesis of iron-sulphur proteins. Nature 460(7257): 831-838.
    • (2009) Nature , vol.460 , Issue.7257 , pp. 831-838
    • Lill, R.1
  • 3
    • 83555173402 scopus 로고    scopus 로고
    • Glutathione: A key component of the cytoplasmic labile iron pool
    • Hider RC, Kong XL (2011) Glutathione: A key component of the cytoplasmic labile iron pool. Biometals 24(6):1179-1187.
    • (2011) Biometals , vol.24 , Issue.6 , pp. 1179-1187
    • Hider, R.C.1    Kong, X.L.2
  • 4
    • 84861850380 scopus 로고    scopus 로고
    • Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis
    • Li H, Outten CE (2012) Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis. Biochemistry 51(22):4377-4389.
    • (2012) Biochemistry , vol.51 , Issue.22 , pp. 4377-4389
    • Li, H.1    Outten, C.E.2
  • 6
    • 84873672762 scopus 로고    scopus 로고
    • Monothiol glutaredoxins and A-type proteins: Partners in Fe-S cluster trafficking
    • Mapolelo DT, et al. (2013) Monothiol glutaredoxins and A-type proteins: Partners in Fe-S cluster trafficking. Dalton Trans 42(9):3107-3115.
    • (2013) Dalton Trans , vol.42 , Issue.9 , pp. 3107-3115
    • Mapolelo, D.T.1
  • 7
    • 84866513533 scopus 로고    scopus 로고
    • Monothiol glutaredoxins function in storing and transporting [Fe2S2] clusters assembled on IscU scaffold proteins
    • Shakamuri P, Zhang B, Johnson MK (2012) Monothiol glutaredoxins function in storing and transporting [Fe2S2] clusters assembled on IscU scaffold proteins. J Am Chem Soc 134(37):15213-15216.
    • (2012) J Am Chem Soc , vol.134 , Issue.37 , pp. 15213-15216
    • Shakamuri, P.1    Zhang, B.2    Johnson, M.K.3
  • 8
    • 84863528676 scopus 로고    scopus 로고
    • Glutathione complexed Fe-S centers
    • Qi W, et al. (2012) Glutathione complexed Fe-S centers. J Am Chem Soc 134(26): 10745-10748.
    • (2012) J Am Chem Soc , vol.134 , Issue.26 , pp. 10745-10748
    • Qi, W.1
  • 9
    • 84866153655 scopus 로고    scopus 로고
    • Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxin
    • Wang L, et al. (2012) Glutathione regulates the transfer of iron-sulfur cluster from monothiol and dithiol glutaredoxins to apo ferredoxin. Protein Cell 3(9):714-721.
    • (2012) Protein Cell , vol.3 , Issue.9 , pp. 714-721
    • Wang, L.1
  • 10
    • 84864296714 scopus 로고    scopus 로고
    • The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism
    • Lill R, et al. (2012) The role of mitochondria in cellular iron-sulfur protein biogenesis and iron metabolism. Biochim Biophys Acta 1823(9):1491-1508.
    • (2012) Biochim Biophys Acta , vol.1823 , Issue.9 , pp. 1491-1508
    • Lill, R.1
  • 11
    • 84879562737 scopus 로고    scopus 로고
    • The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation
    • Uzarska MA, Dutkiewicz R, Freibert SA, Lill R, Mühlenhoff U (2013) The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation. Mol Biol Cell 24(12):1830-1841.
    • (2013) Mol Biol Cell , vol.24 , Issue.12 , pp. 1830-1841
    • Uzarska, M.A.1    Dutkiewicz, R.2    Freibert, S.A.3    Lill, R.4    Mühlenhoff, U.5
  • 12
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • Mühlenhoff U, Gerber J, Richhardt N, Lill R (2003) Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J 22(18): 4815-4825.
    • (2003) EMBO J , vol.22 , Issue.18 , pp. 4815-4825
    • Mühlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 13
    • 0036226063 scopus 로고    scopus 로고
    • Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes
    • Rodríguez-Manzaneque MT, Tamarit J, Bellí G, Ros J, Herrero E (2002) Grx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes. Mol Biol Cell 13(4):1109-1121.
    • (2002) Mol Biol Cell , vol.13 , Issue.4 , pp. 1109-1121
    • Rodríguez-Manzaneque, M.T.1    Tamarit, J.2    Bellí, G.3    Ros, J.4    Herrero, E.5
  • 14
    • 40749086415 scopus 로고    scopus 로고
    • Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes
    • Gelling C, Dawes IW, Richhardt N, Lill R, Mühlenhoff U (2008) Mitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes. Mol Cell Biol 28(5):1851-1861.
    • (2008) Mol Cell Biol , vol.28 , Issue.5 , pp. 1851-1861
    • Gelling, C.1    Dawes, I.W.2    Richhardt, N.3    Lill, R.4    Mühlenhoff, U.5
  • 15
    • 78651265091 scopus 로고    scopus 로고
    • The crystal structure of human GLRX5: Iron-sulfur cluster coordination, tetrameric assembly and monomer activity
    • Johansson C, et al. (2011) The crystal structure of human GLRX5: Iron-sulfur cluster coordination, tetrameric assembly and monomer activity. Biochem J 433(2):303-311.
    • (2011) Biochem J , vol.433 , Issue.2 , pp. 303-311
    • Johansson, C.1
  • 16
    • 3042641171 scopus 로고    scopus 로고
    • Evolution and cellular function of monothiol glutaredoxins: Involvement in iron-sulphur cluster assembly
    • Vilella F, et al. (2004) Evolution and cellular function of monothiol glutaredoxins: Involvement in iron-sulphur cluster assembly. Comp Funct Genomics 5(4):328-341.
    • (2004) Comp Funct Genomics , vol.5 , Issue.4 , pp. 328-341
    • Vilella, F.1
  • 17
    • 76349122676 scopus 로고    scopus 로고
    • Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast
    • Kim KD, Chung WH, Kim HJ, Lee KC, Roe JH (2010) Monothiol glutaredoxin Grx5 interacts with Fe-S scaffold proteins Isa1 and Isa2 and supports Fe-S assembly and DNA integrity in mitochondria of fission yeast. Biochem Biophys Res Commun 392(3): 467-472.
    • (2010) Biochem Biophys Res Commun , vol.392 , Issue.3 , pp. 467-472
    • Kim, K.D.1    Chung, W.H.2    Kim, H.J.3    Lee, K.C.4    Roe, J.H.5
  • 18
    • 0036934396 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: Characterization of Schizosaccharomyces pombe Isa1
    • Wu G, et al. (2002) Iron-sulfur cluster biosynthesis: characterization of Schizosaccharomyces pombe Isa1. J Biol Inorg Chem 7(4-5):526-532.
    • (2002) J Biol Inorg Chem , vol.7 , Issue.4-5 , pp. 526-532
    • Wu, G.1
  • 19
    • 80955125480 scopus 로고    scopus 로고
    • Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins
    • Mühlenhoff U, Richter N, Pines O, Pierik AJ, Lill R (2011) Specialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins. J Biol Chem 286(48):41205-41216.
    • (2011) J Biol Chem , vol.286 , Issue.48 , pp. 41205-41216
    • Mühlenhoff, U.1    Richter, N.2    Pines, O.3    Pierik, A.J.4    Lill, R.5
  • 20
    • 0034107324 scopus 로고    scopus 로고
    • Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis
    • Jensen LT, Culotta VC (2000) Role of Saccharomyces cerevisiae ISA1 and ISA2 in iron homeostasis. Mol Cell Biol 20(11):3918-3927.
    • (2000) Mol Cell Biol , vol.20 , Issue.11 , pp. 3918-3927
    • Jensen, L.T.1    Culotta, V.C.2
  • 21
    • 84859400502 scopus 로고    scopus 로고
    • The human mitochondrial ISCA1, ISCA2, and IBA57 proteins are required for [4Fe-4S] protein maturation
    • Sheftel AD, et al. (2012) The human mitochondrial ISCA1, ISCA2, and IBA57 proteins are required for [4Fe-4S] protein maturation. Mol Biol Cell 23(7):1157-1166.
    • (2012) Mol Biol Cell , vol.23 , Issue.7 , pp. 1157-1166
    • Sheftel, A.D.1
  • 22
    • 79960992428 scopus 로고    scopus 로고
    • Arabidopsis chloroplastic glutaredoxin C5 as a model to explore molecular determinants for iron-sulfur cluster binding into glutaredoxins
    • Couturier J, et al. (2011) Arabidopsis chloroplastic glutaredoxin C5 as a model to explore molecular determinants for iron-sulfur cluster binding into glutaredoxins. J Biol Chem 286(31):27515-27527.
    • (2011) J Biol Chem , vol.286 , Issue.31 , pp. 27515-27527
    • Couturier, J.1
  • 23
    • 67650077717 scopus 로고    scopus 로고
    • Structural basis for delivery of the intact [Fe2S2] cluster by monothiol glutaredoxin
    • Iwema T, et al. (2009) Structural basis for delivery of the intact [Fe2S2] cluster by monothiol glutaredoxin. Biochemistry 48(26):6041-6043.
    • (2009) Biochemistry , vol.48 , Issue.26 , pp. 6041-6043
    • Iwema, T.1
  • 24
    • 34250633648 scopus 로고    scopus 로고
    • Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1
    • Rouhier N, et al. (2007) Functional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1. Proc Natl Acad Sci USA 104(18):7379-7384.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.18 , pp. 7379-7384
    • Rouhier, N.1
  • 25
    • 84876904219 scopus 로고    scopus 로고
    • Molecular view of an electron transfer process essential for ironsulfur protein biogenesis
    • Banci L, et al. (2013) Molecular view of an electron transfer process essential for ironsulfur protein biogenesis. Proc Natl Acad Sci USA 110(18):7136-7141.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.18 , pp. 7136-7141
    • Banci, L.1
  • 26
    • 84896697447 scopus 로고    scopus 로고
    • The IR-(15)N-HSQC-AP experiment: A new tool for NMR spectroscopy of paramagnetic molecules
    • Ciofi-Baffoni S, Gallo A, Muzzioli R, Piccioli M (2014) The IR-(15)N-HSQC-AP experiment: A new tool for NMR spectroscopy of paramagnetic molecules. J Biomol NMR 58(2):123-128.
    • (2014) J Biomol NMR , vol.58 , Issue.2 , pp. 123-128
    • Ciofi-Baffoni, S.1    Gallo, A.2    Muzzioli, R.3    Piccioli, M.4
  • 27
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • Lill R, Mühlenhoff U (2008) Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases. Annu Rev Biochem 77:669-700.
    • (2008) Annu Rev Biochem , vol.77 , pp. 669-700
    • Lill, R.1    Mühlenhoff, U.2
  • 28
    • 33745517607 scopus 로고    scopus 로고
    • A new class of [2Fe-2S]-cluster-containing protoporphyrin (IX) ferrochelatases
    • Shepherd M, Dailey TA, Dailey HA (2006) A new class of [2Fe-2S]-cluster-containing protoporphyrin (IX) ferrochelatases. Biochem J 397(1):47-52.
    • (2006) Biochem J , vol.397 , Issue.1 , pp. 47-52
    • Shepherd, M.1    Dailey, T.A.2    Dailey, H.A.3
  • 29
    • 33745295120 scopus 로고    scopus 로고
    • The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction
    • Banci L, et al. (2006) The Atx1-Ccc2 complex is a metal-mediated protein-protein interaction. Nat Chem Biol 2(7):367-368.
    • (2006) Nat Chem Biol , vol.2 , Issue.7 , pp. 367-368
    • Banci, L.1
  • 30
    • 77954687479 scopus 로고    scopus 로고
    • Cellular copper distribution: A mechanistic systems biology approach
    • Banci L, Bertini I, Cantini F, Ciofi-Baffoni S (2010) Cellular copper distribution: A mechanistic systems biology approach. Cell Mol Life Sci 67(15):2563-2589.
    • (2010) Cell Mol Life Sci , vol.67 , Issue.15 , pp. 2563-2589
    • Banci, L.1    Bertini, I.2    Cantini, F.3    Ciofi-Baffoni, S.4
  • 31
    • 79959522180 scopus 로고    scopus 로고
    • Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-dependent mitochondrial protein trapping machinery
    • Banci L, et al. (2011) Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-dependent mitochondrial protein trapping machinery. Chem Biol 18(6): 794-804.
    • (2011) Chem Biol , vol.18 , Issue.6 , pp. 794-804
    • Banci, L.1
  • 32
    • 84892366922 scopus 로고    scopus 로고
    • Human anamorsin binds [2Fe-2S] clusters with unique electronic properties
    • Banci L, et al. (2013) Human anamorsin binds [2Fe-2S] clusters with unique electronic properties. J Biol Inorg Chem 18(8):883-893.
    • (2013) J Biol Inorg Chem , vol.18 , Issue.8 , pp. 883-893
    • Banci, L.1
  • 33
    • 84876034471 scopus 로고    scopus 로고
    • Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron-sulfur cluster biosynthesis and delivery
    • Markley JL, et al. (2013) Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron-sulfur cluster biosynthesis and delivery. FEBS Lett 587(8):1172-1179.
    • (2013) FEBS Lett , vol.587 , Issue.8 , pp. 1172-1179
    • Markley, J.L.1
  • 34
    • 4644221775 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: Toward an understanding of cellular machinery and molecular mechanism
    • Mansy SS, Cowan JA (2004) Iron-sulfur cluster biosynthesis: Toward an understanding of cellular machinery and molecular mechanism. Acc Chem Res 37(9):719-725.
    • (2004) Acc Chem Res , vol.37 , Issue.9 , pp. 719-725
    • Mansy, S.S.1    Cowan, J.A.2
  • 35
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones, an intracellular shuttle service for metal ions
    • O'Halloran TV, Culotta VC (2000) Metallochaperones, an intracellular shuttle service for metal ions. J Biol Chem 275(33):25057-25060.
    • (2000) J Biol Chem , vol.275 , Issue.33 , pp. 25057-25060
    • O'Halloran, T.V.1    Culotta, V.C.2
  • 37
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4):213-223.
    • (2009) J Biomol NMR , vol.44 , Issue.4 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 38
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T, Güntert P, Wüthrich K (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319(1):209-227.
    • (2002) J Mol Biol , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 39
    • 84862614975 scopus 로고    scopus 로고
    • Univ of California, San Francisco
    • Case DA, et al. (2012) AMBER 1 (Univ of California, San Francisco)
    • (2012) AMBER 1
    • Case, D.A.1
  • 40
    • 80051920557 scopus 로고    scopus 로고
    • A Grid-enabled web portal for NMR structure refinement with AMBER
    • Bertini I, Case DA, Ferella L, Giachetti A, Rosato A (2011) A Grid-enabled web portal for NMR structure refinement with AMBER. Bioinformatics 27(17):2384-2390.
    • (2011) Bioinformatics , vol.27 , Issue.17 , pp. 2384-2390
    • Bertini, I.1    Case, D.A.2    Ferella, L.3    Giachetti, A.4    Rosato, A.5
  • 41
    • 13844271894 scopus 로고    scopus 로고
    • Paramagnetic NMR spectroscopy and density functional calculations in the analysis of the geometric and electronic structures of iron-sulfur proteins
    • Machonkin TE, Westler WM, Markley JL (2005) Paramagnetic NMR spectroscopy and density functional calculations in the analysis of the geometric and electronic structures of iron-sulfur proteins. Inorg Chem 44(4):779-797.
    • (2005) Inorg Chem , vol.44 , Issue.4 , pp. 779-797
    • Machonkin, T.E.1    Westler, W.M.2    Markley, J.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.