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Volumn 1647, Issue 1-2, 2003, Pages 303-309

Assembly of iron-sulfur clusters mediated by cysteine desulfurases, IscS, CsdB and CSD, from Escherichia coli

Author keywords

CSD; CsdB; Cysteine desulfurase; Iron sulfur cluster; IscS; IscU

Indexed keywords

CYSTATHIONINE GAMMA LYASE; CYSTEINE; FERREDOXIN; IRON SULFUR PROTEIN; PROTEIN; PROTEIN CSD; PROTEIN CSDB; PROTEIN ISCS; SULFUR; SULFUR DERIVATIVE; UNCLASSIFIED DRUG; DISULFIDE; ESCHERICHIA COLI PROTEIN; LYASE; SELENOCYSTEINE LYASE;

EID: 1242318521     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(03)00078-5     Document Type: Conference Paper
Times cited : (46)

References (24)
  • 1
    • 0028339794 scopus 로고
    • Catalytic formation of a nitrogenase iron-sulfur cluster
    • Zheng L., Dean D.R. Catalytic formation of a nitrogenase iron-sulfur cluster. J. Biol. Chem. 269:1994;18723-18726.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18723-18726
    • Zheng, L.1    Dean, D.R.2
  • 2
    • 0033554855 scopus 로고    scopus 로고
    • IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA
    • Kambampati R., Lauhon C.T. IscS is a sulfurtransferase for the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA. Biochemistry. 38:1999;16561-16568.
    • (1999) Biochemistry , vol.38 , pp. 16561-16568
    • Kambampati, R.1    Lauhon, C.T.2
  • 3
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • Kispal G., Csere P., Prohl C., Lill R. The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 18:1999;3981-3989.
    • (1999) EMBO J. , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 4
    • 0034255455 scopus 로고    scopus 로고
    • The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
    • Schwartz C.J., Djaman O., Imlay J.A., Kiley P.J. 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
  • 5
    • 0034733647 scopus 로고    scopus 로고
    • The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NAD
    • Lauhon C.T., Kambampati R. The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NAD. J. Biol. Chem. 275:2000;20096-20103.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20096-20103
    • Lauhon, C.T.1    Kambampati, R.2
  • 6
    • 0035933851 scopus 로고    scopus 로고
    • A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli
    • Leimkuhler S., Rajagopalan K.V. A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli. J. Biol. Chem. 276:2001;22024-22031.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22024-22031
    • Leimkuhler, S.1    Rajagopalan, K.V.2
  • 8
    • 0028265941 scopus 로고
    • Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product
    • Zheng L., White R.H., Cash V.L., Dean D.R. Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product. Biochemistry. 33:1994;4714-4720.
    • (1994) Biochemistry , vol.33 , pp. 4714-4720
    • Zheng, L.1    White, R.H.2    Cash, V.L.3    Dean, D.R.4
  • 9
    • 0034093325 scopus 로고    scopus 로고
    • Kinetic and mutational studies of three NifS homologs from Escherichia coli: Mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions
    • Mihara H., Kurihara T., Yoshimura T., Esaki N. Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions. J. Biochem. (Tokyo). 127:2000;559-567.
    • (2000) J. Biochem. (Tokyo) , vol.127 , pp. 559-567
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Esaki, N.4
  • 10
    • 0030018746 scopus 로고    scopus 로고
    • Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase
    • Flint D.H. Escherichia coli contains a protein that is homologous in function and N-terminal sequence to the protein encoded by the nifS gene of Azotobacter vinelandii and that can participate in the synthesis of the Fe-S cluster of dihydroxy-acid dehydratase. J. Biol. Chem. 271:1996;16068-16074.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16068-16074
    • Flint, D.H.1
  • 11
    • 0033591390 scopus 로고    scopus 로고
    • A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary X-ray crystallographic studies
    • Mihara H., Maeda M., Fujii T., Kurihara T., Hata Y., Esaki N. A nifS-like gene, csdB, encodes an Escherichia coli counterpart of mammalian selenocysteine lyase. Gene cloning, purification, characterization and preliminary X-ray crystallographic studies. J. Biol. Chem. 274:1999;14768-14772.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14768-14772
    • Mihara, H.1    Maeda, M.2    Fujii, T.3    Kurihara, T.4    Hata, Y.5    Esaki, N.6
  • 12
    • 0030963659 scopus 로고    scopus 로고
    • Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme
    • Mihara H., Kurihara T., Yoshimura T., Soda K., Esaki N. Cysteine sulfinate desulfinase, a NIFS-like protein of Escherichia coli with selenocysteine lyase and cysteine desulfurase activities. Gene cloning, purification, and characterization of a novel pyridoxal enzyme. J. Biol. Chem. 272:1997;22417-22424.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22417-22424
    • Mihara, H.1    Kurihara, T.2    Yoshimura, T.3    Soda, K.4    Esaki, N.5
  • 13
    • 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., Johnson M.K. IscU as a scaffold for iron-sulfur cluster biosynthesis: sequential assembly of [2Fe-2S] and [4Fe-4S] clusters in IscU. Biochemistry. 39:2000;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
  • 15
    • 0035977015 scopus 로고    scopus 로고
    • Transfer of sulfur from IscS to IscU during Fe/S cluster assembly
    • Urbina H.D., Silberg J.J., Hoff K.G., Vickery L.E. 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
  • 16
    • 0032557666 scopus 로고    scopus 로고
    • Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii
    • Zheng L., Cash V.L., Flint D.H., Dean D.R. Assembly of iron-sulfur clusters. Identification of an iscSUA-hscBA-fdx gene cluster from Azotobacter vinelandii. J. Biol. Chem. 273:1998;13264-13272.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13264-13272
    • Zheng, L.1    Cash, V.L.2    Flint, D.H.3    Dean, D.R.4
  • 17
    • 0023669069 scopus 로고
    • The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara Y., Akiyama K., Isono K. The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell. 50:1987;495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 18
    • 0023070121 scopus 로고
    • Sulfane sulfur
    • Wood J.L. Sulfane sulfur. Methods Enzymol. 143:1987;25-29.
    • (1987) Methods Enzymol. , vol.143 , pp. 25-29
    • Wood, J.L.1
  • 19
    • 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
    • Kato S., Mihara H., Kurihara T., Takahashi Y., Tokumoto U., Yoshimura T., Esaki N. 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. U. S. A. 99:2002;5948-5952.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , 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
  • 20
    • 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., Vickery L.E. Hsc66 substrate specificity is directed toward a discrete region of the iron-sulfur cluster template protein IscU. J. Biol. Chem. 277:2002;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
  • 22
    • 0034673177 scopus 로고    scopus 로고
    • Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase
    • Fujii T., Maeda M., Mihara H., Kurihara T., Esaki N., Hata Y. Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase. Biochemistry. 39:2000;1263-1273.
    • (2000) Biochemistry , vol.39 , pp. 1263-1273
    • Fujii, T.1    Maeda, M.2    Mihara, H.3    Kurihara, T.4    Esaki, N.5    Hata, Y.6
  • 23
    • 0034708346 scopus 로고    scopus 로고
    • Crystal structure of a NifS-like protein from Thermotoga maritima: Implications for iron sulphur cluster assembly
    • Kaiser J.T., Clausen T., Bourenkow G.P., Bartunik H.D., Steinbacher S., Huber R. Crystal structure of a NifS-like protein from Thermotoga maritima: implications for iron sulphur cluster assembly. J. Mol. Biol. 297:2000;451-464.
    • (2000) J. Mol. Biol. , vol.297 , pp. 451-464
    • Kaiser, J.T.1    Clausen, T.2    Bourenkow, G.P.3    Bartunik, H.D.4    Steinbacher, S.5    Huber, R.6
  • 24
    • 0037047411 scopus 로고    scopus 로고
    • A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids
    • Takahashi Y., Tokumoto U. A third bacterial system for the assembly of iron-sulfur clusters with homologs in archaea and plastids. J. Biol. Chem. 277:2002;28380-28383.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28380-28383
    • Takahashi, Y.1    Tokumoto, U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.