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Volumn 587, Issue 8, 2013, Pages 1172-1179

Metamorphic protein IscU alternates conformations in the course of its role as the scaffold protein for iron-sulfur cluster biosynthesis and delivery

Author keywords

Conformational equilibrium; Iron sulfur cluster; Metamorphic protein; Peptidyl prolyl peptide bond isomerization; Protein evolution; Protein protein interaction

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CHAPERONE; CYSTATHIONINE GAMMA LYASE; HSCA PROTEIN; HSCB PROTEIN; IRON; ISCU PROTEIN; SCAFFOLD PROTEIN; SULFUR; UNCLASSIFIED DRUG;

EID: 84876034471     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.01.003     Document Type: Review
Times cited : (68)

References (49)
  • 1
    • 0034003112 scopus 로고    scopus 로고
    • Iron-sulfur proteins: Ancient structures, still full of surprises
    • H. Beinert Iron-sulfur proteins: ancient structures, still full of surprises J. Biol. Inorg. Chem. 5 2000 2 15
    • (2000) J. Biol. Inorg. Chem. , vol.5 , pp. 2-15
    • Beinert, H.1
  • 2
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • D.C. Johnson, D.R. Dean, A.D. Smith, and M.K. Johnson Structure, function, and formation of biological iron-sulfur clusters Annu. Rev. Biochem. 74 2005 247 281
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 4
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • R. Lill, and U. Muhlenhoff Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases Annu. Rev. Biochem. 77 2008 669 700
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 6
    • 47249142777 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis and human disease
    • T.A. Rouault, and W.H. Tong Iron-sulfur cluster biogenesis and human disease Trends Genet. 24 2008 398 407
    • (2008) Trends Genet. , vol.24 , pp. 398-407
    • Rouault, T.A.1    Tong, W.H.2
  • 7
    • 77952813340 scopus 로고    scopus 로고
    • Building Fe-S proteins: Bacterial strategies
    • B. Py, and F. Barras Building Fe-S proteins: bacterial strategies Nat. Rev. Microbiol. 8 2010 436 446
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 436-446
    • Py, B.1    Barras, F.2
  • 8
    • 79954617423 scopus 로고    scopus 로고
    • Fe-S clusters, fragile sentinels of the cell
    • B. Py, P.L. Moreau, and F. Barras Fe-S clusters, fragile sentinels of the cell Curr. Opin. Microbiol. 14 2011 218 223
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 218-223
    • Py, B.1    Moreau, P.L.2    Barras, F.3
  • 9
    • 0035977015 scopus 로고    scopus 로고
    • Transfer of sulfur from IscS to IscU during Fe/S cluster assembly
    • H.D. Urbina, J.J. Silberg, K.G. Hoff, and L.E. Vickery Transfer of sulfur from IscS to IscU during Fe/S cluster assembly J. Biol. Chem. 276 2001 44521 44526
    • (2001) J. Biol. Chem. , vol.276 , pp. 44521-44526
    • Urbina, H.D.1    Silberg, J.J.2    Hoff, K.G.3    Vickery, L.E.4
  • 10
    • 33748782301 scopus 로고    scopus 로고
    • HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction
    • K. Chandramouli, and M.K. Johnson HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction Biochemistry 45 2006 11087 11095
    • (2006) Biochemistry , vol.45 , pp. 11087-11095
    • Chandramouli, K.1    Johnson, M.K.2
  • 11
    • 67650033430 scopus 로고    scopus 로고
    • Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB
    • J.H. Kim, A.K. Füzéry, M. Tonelli, D.T. Ta, W.M. Westler, L.E. Vickery, and J.L. Markley Structure and dynamics of the iron-sulfur cluster assembly scaffold protein IscU and its interaction with the cochaperone HscB Biochemistry 48 2009 6062 6071
    • (2009) Biochemistry , vol.48 , pp. 6062-6071
    • Kim, J.H.1    Füzéry, A.K.2    Tonelli, M.3    Ta, D.T.4    Westler, W.M.5    Vickery, L.E.6    Markley, J.L.7
  • 12
    • 0042667020 scopus 로고    scopus 로고
    • Thermotoga maritima IscU. Structural characterization and dynamics of a new class of metallochaperone
    • I. Bertini, J.A. Cowan, C. Del Bianco, C. Luchinat, and S.S. Mansy Thermotoga maritima IscU. Structural characterization and dynamics of a new class of metallochaperone, J. Mol. Biol. 331 2003 907 924
    • (2003) J. Mol. Biol. , vol.331 , pp. 907-924
    • Bertini, I.1    Cowan, J.A.2    Del Bianco, C.3    Luchinat, C.4    Mansy, S.S.5
  • 13
    • 1642274382 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: Biochemical characterization of the conformational dynamics of Thermotoga maritima IscU and the relevance for cellular cluster assembly
    • S.S. Mansy, S.P. Wu, and J.A. Cowan Iron-sulfur cluster biosynthesis: biochemical characterization of the conformational dynamics of Thermotoga maritima IscU and the relevance for cellular cluster assembly J. Biol. Chem. 279 2004 10469 10475
    • (2004) J. Biol. Chem. , vol.279 , pp. 10469-10475
    • Mansy, S.S.1    Wu, S.P.2    Cowan, J.A.3
  • 16
    • 84870538240 scopus 로고    scopus 로고
    • Metamorphic protein IscU changes conformation by cis-trans isomerizations of two peptidyl-prolyl peptide bonds
    • Z. Dai, M. Tonelli, and J.L. Markley Metamorphic protein IscU changes conformation by cis-trans isomerizations of two peptidyl-prolyl peptide bonds Biochemistry 51 2012 9595 9602
    • (2012) Biochemistry , vol.51 , pp. 9595-9602
    • Dai, Z.1    Tonelli, M.2    Markley, J.L.3
  • 17
    • 46649088364 scopus 로고    scopus 로고
    • Biochemistry-metamorphic proteins
    • A.G. Murzin Biochemistry-metamorphic proteins Science 320 2008 1725 1726
    • (2008) Science , vol.320 , pp. 1725-1726
    • Murzin, A.G.1
  • 18
    • 84862965275 scopus 로고    scopus 로고
    • Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase
    • J.H. Kim, M. Tonelli, and J.L. Markley Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase Proc. Natl. Acad. Sci. U.S.A. 109 2012 454 459
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 454-459
    • Kim, J.H.1    Tonelli, M.2    Markley, J.L.3
  • 19
    • 52049096425 scopus 로고    scopus 로고
    • The asymmetric trimeric architecture of [2Fe-2S] IscU: Implications for its scaffolding during iron-sulfur cluster biosynthesis
    • Y. Shimomura, K. Wada, K. Fukuyama, and Y. Takahashi The asymmetric trimeric architecture of [2Fe-2S] IscU: implications for its scaffolding during iron-sulfur cluster biosynthesis J. Mol. Biol. 383 2008 133 143
    • (2008) J. Mol. Biol. , vol.383 , pp. 133-143
    • Shimomura, Y.1    Wada, K.2    Fukuyama, K.3    Takahashi, Y.4
  • 20
    • 84866139470 scopus 로고    scopus 로고
    • Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU)
    • J.H. Kim, M. Tonelli, R.O. Frederick, D.C. Chow, and J.L. Markley Specialized Hsp70 chaperone (HscA) binds preferentially to the disordered form, whereas J-protein (HscB) binds preferentially to the structured form of the iron-sulfur cluster scaffold protein (IscU) J. Biol. Chem. 287 2012 31406 31413
    • (2012) J. Biol. Chem. , vol.287 , pp. 31406-31413
    • Kim, J.H.1    Tonelli, M.2    Frederick, R.O.3    Chow, D.C.4    Markley, J.L.5
  • 21
    • 84863894674 scopus 로고    scopus 로고
    • Three-dimensional structure and determinants of stability of the iron-sulfur cluster scaffold protein IscU from Escherichia coli
    • J.H. Kim, M. Tonelli, T. Kim, and J.L. Markley three-dimensional structure and determinants of stability of the iron-sulfur cluster scaffold protein IscU from Escherichia coli Biochemistry 51 2012 5557 5563
    • (2012) Biochemistry , vol.51 , pp. 5557-5563
    • Kim, J.H.1    Tonelli, M.2    Kim, T.3    Markley, J.L.4
  • 24
    • 34250187112 scopus 로고    scopus 로고
    • In vitro activation of apo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU [Fe-S] cluster scaffolding protein
    • M.C. Unciuleac, K. Chandramouli, S. Naik, S. Mayer, B.H. Huynh, M.K. Johnson, and D.R. Dean In vitro activation of apo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU [Fe-S] cluster scaffolding protein Biochemistry 46 2007 6812 6821
    • (2007) Biochemistry , vol.46 , pp. 6812-6821
    • Unciuleac, M.C.1    Chandramouli, K.2    Naik, S.3    Mayer, S.4    Huynh, B.H.5    Johnson, M.K.6    Dean, D.R.7
  • 25
    • 38849198557 scopus 로고    scopus 로고
    • Characterization and crystallization of an IscU-type scaffold protein with bound [2Fe-2S] cluster from the hyperthermophile Aquifex aeolicus
    • Y. Shimomura, H. Kamikubo, Y. Nishi, T. Masako, M. Kataoka, Y. Kobayashi, K. Fukuyama, and Y. Takahashi Characterization and crystallization of an IscU-type scaffold protein with bound [2Fe-2S] cluster from the hyperthermophile Aquifex aeolicus J. Biochem. 142 2007 577 586
    • (2007) J. Biochem. , vol.142 , pp. 577-586
    • Shimomura, Y.1    Kamikubo, H.2    Nishi, Y.3    Masako, T.4    Kataoka, M.5    Kobayashi, Y.6    Fukuyama, K.7    Takahashi, Y.8
  • 26
  • 27
    • 0034686765 scopus 로고    scopus 로고
    • A mutant human IscU protein contains a stable [2Fe-2S](2+) center of possible functional significance
    • M.W. Foster, S.S. Mansy, J. Hwang, J.E. Penner-Hahn, K.K. Surerus, and J.A. Cowan A mutant human IscU protein contains a stable [2Fe-2S](2+) center of possible functional significance J. Am. Chem. Soc. 122 2000 6805 6806
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 6805-6806
    • Foster, M.W.1    Mansy, S.S.2    Hwang, J.3    Penner-Hahn, J.E.4    Surerus, K.K.5    Cowan, J.A.6
  • 28
    • 0037118671 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Kinetic analysis of [2Fe-2S] cluster transfer from holo ISU to apo Fd: Role of redox chemistry and a conserved aspartate
    • S.P. Wu, G. Wu, K.K. Surerus, and J.A. Cowan Iron-sulfur cluster biosynthesis. Kinetic analysis of [2Fe-2S] cluster transfer from holo ISU to apo Fd: role of redox chemistry and a conserved aspartate Biochemistry 41 2002 8876 8885
    • (2002) Biochemistry , vol.41 , pp. 8876-8885
    • Wu, S.P.1    Wu, G.2    Surerus, K.K.3    Cowan, J.A.4
  • 29
    • 4644221775 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: Toward an understanding of cellular machinery and molecular mechanism
    • S.S. Mansy, and J.A. Cowan Iron-sulfur cluster biosynthesis: toward an understanding of cellular machinery and molecular mechanism Acc. Chem. Res. 37 2004 719 725
    • (2004) Acc. Chem. Res. , vol.37 , pp. 719-725
    • Mansy, S.S.1    Cowan, J.A.2
  • 30
    • 0015560095 scopus 로고
    • Carbon-13 and proton nuclear magnetic resonance observations of the conformation of poly(l-proline) in aqueous salt solutions
    • D.E. Dorman, D.A. Torchia, and F.A. Bovey Carbon-13 and proton nuclear magnetic resonance observations of the conformation of poly(l-proline) in aqueous salt solutions Macromolecules 6 1973 80 82
    • (1973) Macromolecules , vol.6 , pp. 80-82
    • Dorman, D.E.1    Torchia, D.A.2    Bovey, F.A.3
  • 33
    • 77951666856 scopus 로고    scopus 로고
    • Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts
    • Y. Shen, and A. Bax Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts J. Biomol. NMR 46 2010 199 204
    • (2010) J. Biomol. NMR , vol.46 , pp. 199-204
    • Shen, Y.1    Bax, A.2
  • 35
    • 33845182844 scopus 로고
    • 2D chemical-exchange NMR-spectroscopy by proton-detected heteronuclear correlation
    • G.T. Montelione, and G. Wagner 2D chemical-exchange NMR-spectroscopy by proton-detected heteronuclear correlation J. Am. Chem. Soc. 111 1989 3096 3098
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 3096-3098
    • Montelione, G.T.1    Wagner, G.2
  • 36
    • 20444393525 scopus 로고    scopus 로고
    • Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds
    • P. Schanda, and B. Brutscher Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds J. Am. Chem. Soc. 127 2005 8014 8015
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 8014-8015
    • Schanda, P.1    Brutscher, B.2
  • 37
    • 4444346912 scopus 로고    scopus 로고
    • Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC
    • J.R. Cupp-Vickery, J.C. Peterson, D.T. Ta, and L.E. Vickery Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC J. Mol. Biol. 342 2004 1265 1278
    • (2004) J. Mol. Biol. , vol.342 , pp. 1265-1278
    • Cupp-Vickery, J.R.1    Peterson, J.C.2    Ta, D.T.3    Vickery, L.E.4
  • 38
    • 0029871766 scopus 로고    scopus 로고
    • A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding
    • J. Tsai, and M.G. Douglas A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding J. Biol. Chem. 271 1996 9347 9354
    • (1996) J. Biol. Chem. , vol.271 , pp. 9347-9354
    • Tsai, J.1    Douglas, M.G.2
  • 39
    • 33745217828 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis: Characterization of Escherichia coli CyaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU
    • G. Layer, S. Ollagnier-de Choudens, Y. Sanakis, and M. Fontecave Iron-sulfur cluster biosynthesis: characterization of Escherichia coli CyaY as an iron donor for the assembly of [2Fe-2S] clusters in the scaffold IscU J. Biol. Chem. 281 2006 16256 16263
    • (2006) J. Biol. Chem. , vol.281 , pp. 16256-16263
    • Layer, G.1    Ollagnier-De Choudens, S.2    Sanakis, Y.3    Fontecave, M.4
  • 41
    • 84859178535 scopus 로고    scopus 로고
    • Effector role reversal during evolution: The case of frataxin in Fe-S cluster biosynthesis
    • J. Bridwell-Rabb, C. Iannuzzi, A. Pastore, and D.P. Barondeau Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis Biochemistry 51 2012 2506 2514
    • (2012) Biochemistry , vol.51 , pp. 2506-2514
    • Bridwell-Rabb, J.1    Iannuzzi, C.2    Pastore, A.3    Barondeau, D.P.4
  • 42
    • 78049305276 scopus 로고    scopus 로고
    • Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex
    • C.L. Tsai, and D.P. Barondeau Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex Biochemistry 49 2010 9132 9139
    • (2010) Biochemistry , vol.49 , pp. 9132-9139
    • Tsai, C.L.1    Barondeau, D.P.2
  • 43
    • 0030029817 scopus 로고    scopus 로고
    • DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen
    • B.A. Lazazzera, H. Beinert, N. Khoroshilova, M.C. Kennedy, and P.J. Kiley DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen J. Biol. Chem. 271 1996 2762 2768
    • (1996) J. Biol. Chem. , vol.271 , pp. 2762-2768
    • Lazazzera, B.A.1    Beinert, H.2    Khoroshilova, N.3    Kennedy, M.C.4    Kiley, P.J.5
  • 44
    • 0038351831 scopus 로고    scopus 로고
    • Crystal structure of IscS, a cysteine desulfurase from Escherichia coli
    • J.R. Cupp-Vickery, H. Urbina, and L.E. Vickery Crystal structure of IscS, a cysteine desulfurase from Escherichia coli J. Mol. Biol. 330 2003 1049 1059
    • (2003) J. Mol. Biol. , vol.330 , pp. 1049-1059
    • Cupp-Vickery, J.R.1    Urbina, H.2    Vickery, L.E.3
  • 45
    • 1842526422 scopus 로고    scopus 로고
    • Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli
    • J.R. Cupp-Vickery, J.J. Silberg, D.T. Ta, and L.E. Vickery Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli J. Mol. Biol. 338 2004 127 137
    • (2004) J. Mol. Biol. , vol.338 , pp. 127-137
    • Cupp-Vickery, J.R.1    Silberg, J.J.2    Ta, D.T.3    Vickery, L.E.4
  • 46
    • 0141844533 scopus 로고    scopus 로고
    • Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system
    • K.G. Hoff, J.R. Cupp-Vickery, and L.E. Vickery Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system J. Biol. Chem. 278 2003 37582 37589
    • (2003) J. Biol. Chem. , vol.278 , pp. 37582-37589
    • Hoff, K.G.1    Cupp-Vickery, J.R.2    Vickery, L.E.3
  • 47
    • 0034255455 scopus 로고    scopus 로고
    • The cysteine desulfurase IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
    • C.J. Schwartz, O. Djaman, J.A. Imlay, and P.J. Kiley The cysteine desulfurase IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli Proc. Natl. Acad. Sci. U.S.A. 97 2000 9009 9014
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 9009-9014
    • Schwartz, C.J.1    Djaman, O.2    Imlay, J.A.3    Kiley, P.J.4
  • 48
    • 0035910560 scopus 로고    scopus 로고
    • The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli
    • J.J. Silberg, K.G. Hoff, T.L. Tapley, and L.E. Vickery The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli J. Biol. Chem. 276 2001 1696 1700
    • (2001) J. Biol. Chem. , vol.276 , pp. 1696-1700
    • Silberg, J.J.1    Hoff, K.G.2    Tapley, T.L.3    Vickery, L.E.4
  • 49
    • 11144224094 scopus 로고    scopus 로고
    • Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU
    • J.J. Silberg, T.L. Tapley, K.G. Hoff, and L.E. Vickery Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU J. Biol. Chem. 279 2004 53924 53931
    • (2004) J. Biol. Chem. , vol.279 , pp. 53924-53931
    • Silberg, J.J.1    Tapley, T.L.2    Hoff, K.G.3    Vickery, L.E.4


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