메뉴 건너뛰기




Volumn 47, Issue 48, 2008, Pages 12795-12801

Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; DATA STORAGE EQUIPMENT; DICHROISM; HYDROLYSIS; OPTICAL PROPERTIES; SULFUR;

EID: 57049159293     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801565j     Document Type: Article
Times cited : (96)

References (27)
  • 1
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson, D. C., Dean, D. R., Smith, A. D., and Johnson, M. K. (2005) Structure, function, and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 74, 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
  • 2
    • 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
  • 3
    • 44549087696 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis in bacteria: Mechanisms of cluster assembly and transfer
    • Fontecave, M., and Ollagnier-de-Choudens, S. (2008) Iron-sulfur cluster biosynthesis in bacteria: mechanisms of cluster assembly and transfer. Arch. Biochem. Biophys. 474, 226-237.
    • (2008) Arch. Biochem. Biophys , vol.474 , pp. 226-237
    • Fontecave, M.1    Ollagnier-de-Choudens, S.2
  • 4
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: Mechanisms, connected processes, and diseases
    • Lill, R., and 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
  • 6
    • 34247124148 scopus 로고    scopus 로고
    • Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation
    • Vickery, L. E., and Cupp-Vickery, J. R. (2007) Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation. Crit. Rev. Biochem. Mol. Biol. 42, 95-111.
    • (2007) Crit. Rev. Biochem. Mol. Biol , vol.42 , pp. 95-111
    • Vickery, L.E.1    Cupp-Vickery, J.R.2
  • 7
    • 0037178878 scopus 로고    scopus 로고
    • Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU
    • Hoff, K. G., Ta, D. T., Tapley, T. L., Silberg, J. J., and Vickery, L. E. (2002) Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU. J. Biol. Chem. 277, 27353-27359.
    • (2002) J. Biol. Chem , vol.277 , pp. 27353-27359
    • Hoff, K.G.1    Ta, D.T.2    Tapley, T.L.3    Silberg, J.J.4    Vickery, L.E.5
  • 8
    • 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
    • Hoff, K. G., Cupp-Vickery, J. R., and Vickery, L. E. (2003) Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system. J. Biol. Chem. 278, 37582-37589.
    • (2003) J. Biol. Chem , vol.278 , pp. 37582-37589
    • Hoff, K.G.1    Cupp-Vickery, J.R.2    Vickery, L.E.3
  • 9
    • 0042531776 scopus 로고    scopus 로고
    • Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart
    • Dutkiewicz, R., Schilke, B., Knieszner, H., Walter, W., Craig, E. A., and Marszalek, J. (2003) Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart. J. Biol. Chem. 278, 29719-29727.
    • (2003) J. Biol. Chem , vol.278 , pp. 29719-29727
    • Dutkiewicz, R.1    Schilke, B.2    Knieszner, H.3    Walter, W.4    Craig, E.A.5    Marszalek, J.6
  • 10
    • 3142716203 scopus 로고    scopus 로고
    • Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function
    • Dutkiewicz, R., Schilke, B., Cheng, S., Knieszner, H., Craig, E. A., and Marszalek, J. (2004) Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function. J. Biol. Chem. 279, 29167-29174.
    • (2004) J. Biol. Chem , vol.279 , pp. 29167-29174
    • Dutkiewicz, R.1    Schilke, B.2    Cheng, S.3    Knieszner, H.4    Craig, E.A.5    Marszalek, J.6
  • 11
    • 4444346912 scopus 로고    scopus 로고
    • Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC
    • Cupp-Vickery, J. R., Peterson, J. C., Ta, D. T., and Vickery, L. E. (2004). Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC. J. Mol. Biol. 342, 265-1278.
    • (2004) J. Mol. Biol , vol.342 , pp. 265-1278
    • Cupp-Vickery, J.R.1    Peterson, J.C.2    Ta, D.T.3    Vickery, L.E.4
  • 12
    • 0034608935 scopus 로고    scopus 로고
    • Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli
    • Hoff, K. G., Silberg, J. J., and Vickery, L. E. (2000) Interaction of the iron-sulfur cluster assembly protein IscU with the Hsc66/Hsc20 molecular chaperone system of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 97, 7790-7795.
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 7790-7795
    • Hoff, K.G.1    Silberg, J.J.2    Vickery, L.E.3
  • 13
    • 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., and Lill, R. (2003) Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 22, 4815-4825.
    • (2003) EMBO J , vol.22 , pp. 4815-4825
    • Mühlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 14
    • 33646342998 scopus 로고    scopus 로고
    • The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p
    • Dutkiewicz, R., Marszalek, J., Schilke, B., Craig, E. A., Lill, R., and Muhlenhoff, U. (2006) The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p. J. Biol. Chem. 281, 7801-7808.
    • (2006) J. Biol. Chem , vol.281 , pp. 7801-7808
    • Dutkiewicz, R.1    Marszalek, J.2    Schilke, B.3    Craig, E.A.4    Lill, R.5    Muhlenhoff, U.6
  • 15
    • 57049133501 scopus 로고    scopus 로고
    • Bonomi, F., Iametti, S., Ta, D. T. and Vickery, L. E. (2005) The E. coli HscA/HscB chaperone/cochaperone system facilitates iron-sulfur cluster transfer from holo-IscU to apo-ferredoxin in an ATP-dependent manner, http://www.umich.edu/~icbic/Abstracts/370469-1.pdf.
    • Bonomi, F., Iametti, S., Ta, D. T. and Vickery, L. E. (2005) The E. coli HscA/HscB chaperone/cochaperone system facilitates iron-sulfur cluster transfer from holo-IscU to apo-ferredoxin in an ATP-dependent manner, http://www.umich.edu/~icbic/Abstracts/370469-1.pdf.
  • 16
    • 33748782301 scopus 로고    scopus 로고
    • HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction
    • Chandramouli, K., and Johnson, M. K. (2006) HscA and HscB stimulate [2Fe-2S] cluster transfer from IscU to apoferredoxin in an ATP-dependent reaction. Biochemistry 45, 11087-11095.
    • (2006) Biochemistry , vol.45 , pp. 11087-11095
    • Chandramouli, K.1    Johnson, M.K.2
  • 17
    • 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
    • Silberg, J. J., Tapley, T. L., Hoff, K. G., and Vickery, L. E. (2004) Regulation of the HscA ATPase reaction cycle by the co-chaperone HscB and the iron-sulfur cluster assembly protein IscU. J. Biol. Chem. 279, 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
  • 18
    • 0026704947 scopus 로고
    • Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from
    • Ta, D. T., and Vickery, L. E. (1992) Cloning, sequencing, and overexpression of a [2Fe-2S] ferredoxin gene from. Escherichia coli. J. Biol. Chem. 267, 11120-11125.
    • (1992) Escherichia coli. J. Biol. Chem , vol.267 , pp. 11120-11125
    • Ta, D.T.1    Vickery, L.E.2
  • 19
    • 0030903131 scopus 로고    scopus 로고
    • Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli
    • Vickery, L. E., Silberg, J. J., and Ta, D. T. (1997) Hsc66 and Hsc20, a new heat shock cognate molecular chaperone system from Escherichia coli. Protein Sci. 6, 1047-1056.
    • (1997) Protein Sci , vol.6 , pp. 1047-1056
    • Vickery, L.E.1    Silberg, J.J.2    Ta, D.T.3
  • 20
    • 0034636795 scopus 로고    scopus 로고
    • IscU as a scaffold for iron-sulfur cluster biosynthesis: Sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU
    • Agar, J. N., Krebs, C., Frazzon, J., Huynh, B. H., Dean, D. R., and Johnson, M. K. (2000) IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry 39, 7856-7862.
    • (2000) Biochemistry , vol.39 , pp. 7856-7862
    • Agar, J.N.1    Krebs, C.2    Frazzon, J.3    Huynh, B.H.4    Dean, D.R.5    Johnson, M.K.6
  • 21
    • 23844453358 scopus 로고    scopus 로고
    • Multiple turnover transfer of [2Fe2S] clusters by the iron-sulfur cluster assembly scaffold proteins IscU and IscA
    • Bonomi, F., Iametti, S., Ta, D. T., and Vickery, L. E. (2005) Multiple turnover transfer of [2Fe2S] clusters by the iron-sulfur cluster assembly scaffold proteins IscU and IscA. J. Biol. Chem. 280, 29513-29518.
    • (2005) J. Biol. Chem , vol.280 , pp. 29513-29518
    • Bonomi, F.1    Iametti, S.2    Ta, D.T.3    Vickery, L.E.4
  • 22
    • 0026076490 scopus 로고
    • DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity
    • McCarty, J. S., and Walker, G. C. (1991) DnaK as a thermometer: Threonine-199 is site of autophosphorylation and is critical for ATPase activity. Proc. Natl. Acad. Sci. U.S.A. 88, 9513-9517.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 9513-9517
    • McCarty, J.S.1    Walker, G.C.2
  • 23
    • 0034837025 scopus 로고    scopus 로고
    • ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release
    • Barthel, T. T., and Walker, G. C. (2001) ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release. J. Bacteriol. 183, 5482-5490.
    • (2001) J. Bacteriol , vol.183 , pp. 5482-5490
    • Barthel, T.T.1    Walker, G.C.2
  • 24
    • 0034678084 scopus 로고    scopus 로고
    • Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli
    • Silberg, J. J., and Vickery, L. E. (2000) Kinetic characterization of the ATPase cycle of the molecular chaperone Hsc66 from Escherichia coli. J. Biol. Chem. 275, 7779-7786.
    • (2000) J. Biol. Chem , vol.275 , pp. 7779-7786
    • Silberg, J.J.1    Vickery, L.E.2
  • 25
    • 0035910560 scopus 로고    scopus 로고
    • The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli
    • Silberg, J. J., Hoff, K. G., Tapley, T. L., and Vickery, L. E. (2001) The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli. J. Biol. Chem. 276, 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
  • 26
    • 0037117756 scopus 로고    scopus 로고
    • Characterization of an iron-sulfur cluster assembly protein (ISU1) from Schizosaccharomyces pombe
    • Wu, G., Mansy, S. S., Wu, S. P., Sureus, K. K., Foster, M. W., and Cowan, J. A. (2002) Characterization of an iron-sulfur cluster assembly protein (ISU1) from Schizosaccharomyces pombe. Biochemistry 41, 5024-5032.
    • (2002) Biochemistry , vol.41 , pp. 5024-5032
    • Wu, G.1    Mansy, S.S.2    Wu, S.P.3    Sureus, K.K.4    Foster, M.W.5    Cowan, J.A.6
  • 27
    • 51549120794 scopus 로고    scopus 로고
    • Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU
    • Füzéry, A. K., Tonelli, M., Ta, D. T., Cornilescu, G., Vickery, L. E., and Markley, J. L. (2008) Solution structure of the iron-sulfur cluster cochaperone HscB and its binding surface for the iron-sulfur assembly scaffold protein IscU. Biochemistry 47, 9394-9404.
    • (2008) Biochemistry , vol.47 , pp. 9394-9404
    • Füzéry, A.K.1    Tonelli, M.2    Ta, D.T.3    Cornilescu, G.4    Vickery, L.E.5    Markley, J.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.