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Volumn 14, Issue 2, 2011, Pages 218-223

Fe-S clusters, fragile sentinels of the cell

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; IRON SULFUR PROTEIN; MESSENGER RNA; MULTIPROTEIN COMPLEX; PROTEIN ISC; PROTEIN SUF; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 79954617423     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2011.01.004     Document Type: Review
Times cited : (64)

References (55)
  • 1
    • 33646368396 scopus 로고    scopus 로고
    • Iron-sulfur clusters: ever-expanding roles
    • Fontecave M. Iron-sulfur clusters: ever-expanding roles. Nat Chem Biol 2006, 2:171-174.
    • (2006) Nat Chem Biol , vol.2 , pp. 171-174
    • Fontecave, M.1
  • 2
    • 77952813340 scopus 로고    scopus 로고
    • Building Fe-S proteins: bacterial strategies
    • Py B., Barras F. Building Fe-S proteins: bacterial strategies. Nat Rev Microbiol 2010, 8:436-446.
    • (2010) Nat Rev Microbiol , vol.8 , pp. 436-446
    • Py, B.1    Barras, F.2
  • 3
    • 33645065589 scopus 로고    scopus 로고
    • Iron-sulphur clusters and the problem with oxygen
    • Imlay J.A. Iron-sulphur clusters and the problem with oxygen. Mol Microbiol 2006, 59:1073-1082.
    • (2006) Mol Microbiol , vol.59 , pp. 1073-1082
    • Imlay, J.A.1
  • 4
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defenses against superoxide and hydrogen peroxide
    • Imlay J.A. Cellular defenses against superoxide and hydrogen peroxide. Annu Rev Biochem 2008, 77:755-776.
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 5
    • 79954432514 scopus 로고    scopus 로고
    • Redox pioneer: professor Irwin Fridovich
    • Imlay J.A. Redox pioneer: professor Irwin Fridovich. Antioxid Redox Signal 2010, 14:335-340.
    • (2010) Antioxid Redox Signal , vol.14 , pp. 335-340
    • Imlay, J.A.1
  • 6
    • 78649983777 scopus 로고    scopus 로고
    • Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate
    • Jang S., Imlay J.A. Hydrogen peroxide inactivates the Escherichia coli Isc iron-sulphur assembly system, and OxyR induces the Suf system to compensate. Mol Microbiol 2010, 78:1448-1467.
    • (2010) Mol Microbiol , vol.78 , pp. 1448-1467
    • Jang, S.1    Imlay, J.A.2
  • 7
    • 33847753939 scopus 로고    scopus 로고
    • Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes
    • Jang S., Imlay J.A. Micromolar intracellular hydrogen peroxide disrupts metabolism by damaging iron-sulfur enzymes. J Biol Chem 2007, 282:929-937.
    • (2007) J Biol Chem , vol.282 , pp. 929-937
    • Jang, S.1    Imlay, J.A.2
  • 8
    • 0027491617 scopus 로고
    • The inactivation of Fe-S cluster containing hydro-lyases by superoxide
    • Flint D.H., Tuminello J.F., Emptage M.H. The inactivation of Fe-S cluster containing hydro-lyases by superoxide. J Biol Chem 1993, 268:22369-22376.
    • (1993) J Biol Chem , vol.268 , pp. 22369-22376
    • Flint, D.H.1    Tuminello, J.F.2    Emptage, M.H.3
  • 9
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free-iron levels
    • Keyer K., Imlay J.A. Superoxide accelerates DNA damage by elevating free-iron levels. PNAS USA 1996, 93:13635-13640.
    • (1996) PNAS USA , vol.93 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 10
    • 34548213103 scopus 로고    scopus 로고
    • A common mechanism of cellular death induced by bactericidal antibiotics
    • Kohanski M.A., Dwyer D.J., Hayete B., Lawrence C.A., Collins J.J. A common mechanism of cellular death induced by bactericidal antibiotics. Cell 2007, 130:797-810.
    • (2007) Cell , vol.130 , pp. 797-810
    • Kohanski, M.A.1    Dwyer, D.J.2    Hayete, B.3    Lawrence, C.A.4    Collins, J.J.5
  • 11
    • 77954609311 scopus 로고    scopus 로고
    • Iron homeostasis affects antibiotic-mediated cell death in Pseudomonas species
    • Yeom J., Imlay J.A., Park W. Iron homeostasis affects antibiotic-mediated cell death in Pseudomonas species. J Biol Chem 2010, 285:22689-22695.
    • (2010) J Biol Chem , vol.285 , pp. 22689-22695
    • Yeom, J.1    Imlay, J.A.2    Park, W.3
  • 12
    • 77952056332 scopus 로고    scopus 로고
    • Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis
    • Chillappagari S., Seubert A., Trip H., Kuipers O.P., Marahiel M.A., Miethke M. Copper stress affects iron homeostasis by destabilizing iron-sulfur cluster formation in Bacillus subtilis. J Bacteriol 2010, 192:2512-2524.
    • (2010) J Bacteriol , vol.192 , pp. 2512-2524
    • Chillappagari, S.1    Seubert, A.2    Trip, H.3    Kuipers, O.P.4    Marahiel, M.A.5    Miethke, M.6
  • 13
    • 77957320225 scopus 로고    scopus 로고
    • A genetic analysis of the response of Escherichia coli to cobalt stress
    • Fantino J.R., Py B., Fontecave M., Barras F. A genetic analysis of the response of Escherichia coli to cobalt stress. Environ Microbiol 2010, 12:2846-2857.
    • (2010) Environ Microbiol , vol.12 , pp. 2846-2857
    • Fantino, J.R.1    Py, B.2    Fontecave, M.3    Barras, F.4
  • 14
    • 66249112833 scopus 로고    scopus 로고
    • The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity
    • Macomber L., Imlay J.A. The iron-sulfur clusters of dehydratases are primary intracellular targets of copper toxicity. PNAS USA 2009, 106:8344-8349.
    • (2009) PNAS USA , vol.106 , pp. 8344-8349
    • Macomber, L.1    Imlay, J.A.2
  • 16
    • 35648957710 scopus 로고    scopus 로고
    • Cobalt targets multiple metabolic processes in Salmonella enterica
    • Thorgersen M.P., Downs D.M. Cobalt targets multiple metabolic processes in Salmonella enterica. J Bacteriol 2007, 189:7774-7781.
    • (2007) J Bacteriol , vol.189 , pp. 7774-7781
    • Thorgersen, M.P.1    Downs, D.M.2
  • 18
    • 48149092468 scopus 로고    scopus 로고
    • Cadmium toxicity in glutathione mutants of Escherichia coli
    • Helbig K., Grosse C., Nies D.H. Cadmium toxicity in glutathione mutants of Escherichia coli. J Bacteriol 2008, 190:5439-5454.
    • (2008) J Bacteriol , vol.190 , pp. 5439-5454
    • Helbig, K.1    Grosse, C.2    Nies, D.H.3
  • 20
    • 77957961907 scopus 로고    scopus 로고
    • Pseudomonas fluorescens orchestrates a fine metabolic-balancing act to counter aluminium toxicity
    • Lemire J., Mailloux R., Auger C., Whalen D., Appanna V.D. Pseudomonas fluorescens orchestrates a fine metabolic-balancing act to counter aluminium toxicity. Environ Microbiol 2010, 12:1384-1390.
    • (2010) Environ Microbiol , vol.12 , pp. 1384-1390
    • Lemire, J.1    Mailloux, R.2    Auger, C.3    Whalen, D.4    Appanna, V.D.5
  • 22
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R. Function and biogenesis of iron-sulphur proteins. Nature 2009, 460:831-838.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 23
    • 79954595431 scopus 로고    scopus 로고
    • Iron-sulfur clusters: biogenesis, molecular mechanisms and their functional significance
    • in press, doi:10.1089/ARS.2010.3259
    • Xu XM, Moller SG: Iron-sulfur clusters: biogenesis, molecular mechanisms and their functional significance. Antioxid Redox Signal 2011, in press. doi:10.1089/ARS.2010.3259.
    • (2011) Antioxid Redox Signal
    • Xu, X.M.1    Moller, S.G.2
  • 24
    • 0037415722 scopus 로고    scopus 로고
    • SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress
    • Nachin L., Loiseau L., Expert D., Barras F. SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress. EMBO J 2003, 22:427-437.
    • (2003) EMBO J , vol.22 , pp. 427-437
    • Nachin, L.1    Loiseau, L.2    Expert, D.3    Barras, F.4
  • 25
    • 2442567822 scopus 로고    scopus 로고
    • A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli
    • Outten F.W., Djaman O., Storz G. A suf operon requirement for Fe-S cluster assembly during iron starvation in Escherichia coli. Mol Microbiol 2004, 52:861-872.
    • (2004) Mol Microbiol , vol.52 , pp. 861-872
    • Outten, F.W.1    Djaman, O.2    Storz, G.3
  • 26
    • 39849096561 scopus 로고    scopus 로고
    • Biogenesis of Fe/S proteins and pathogenicity: IscR plays a key role in allowing Erwinia chrysanthemi to adapt to hostile conditions
    • Rincon-Enriquez G., Crete P., Barras F., Py B. Biogenesis of Fe/S proteins and pathogenicity: IscR plays a key role in allowing Erwinia chrysanthemi to adapt to hostile conditions. Mol Microbiol 2008, 67:1257-1273.
    • (2008) Mol Microbiol , vol.67 , pp. 1257-1273
    • Rincon-Enriquez, G.1    Crete, P.2    Barras, F.3    Py, B.4
  • 27
    • 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 2000, 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
  • 28
    • 38849198557 scopus 로고    scopus 로고
    • Characterization and crystallization of an IscU-type scaffold protein with bound [2Fe-2S] cluster from the hyperthermophile, Aquifex aeolicus
    • Shimomura Y., Kamikubo H., Nishi Y., Masako T., Kataoka M., Kobayashi Y., Fukuyama K., Takahashi Y. Characterization and crystallization of an IscU-type scaffold protein with bound [2Fe-2S] cluster from the hyperthermophile, Aquifex aeolicus. J Biochem 2007, 142:577-586.
    • (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
  • 29
    • 78049288246 scopus 로고    scopus 로고
    • SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB
    • Saini A., Mapolelo D.T., Chahal H.K., Johnson M.K., Outten F.W. SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB. Biochemistry 2010, 49:9402-9412.
    • (2010) Biochemistry , vol.49 , pp. 9402-9412
    • Saini, A.1    Mapolelo, D.T.2    Chahal, H.K.3    Johnson, M.K.4    Outten, F.W.5
  • 32
    • 57049159293 scopus 로고    scopus 로고
    • Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones
    • Bonomi F., Iametti S., Morleo A., Ta D., Vickery L.E. Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones. Biochemistry 2008, 47:12795-12801.
    • (2008) Biochemistry , vol.47 , pp. 12795-12801
    • Bonomi, F.1    Iametti, S.2    Morleo, A.3    Ta, D.4    Vickery, L.E.5
  • 33
    • 57349087129 scopus 로고    scopus 로고
    • Oxidant-responsive induction of the suf operon, encoding a Fe-S assembly system, through Fur and IscR in Escherichia coli
    • Lee K.C., Yeo W.S., Roe J.H. Oxidant-responsive induction of the suf operon, encoding a Fe-S assembly system, through Fur and IscR in Escherichia coli. J Bacteriol 2008, 190:8244-8247.
    • (2008) J Bacteriol , vol.190 , pp. 8244-8247
    • Lee, K.C.1    Yeo, W.S.2    Roe, J.H.3
  • 34
    • 61349134073 scopus 로고    scopus 로고
    • Sequence-specific binding to a subset of IscR-regulated promoters does not require IscR Fe-S cluster ligation
    • Nesbit A.D., Giel J.L., Rose J.C., Kiley P.J. Sequence-specific binding to a subset of IscR-regulated promoters does not require IscR Fe-S cluster ligation. J Mol Biol 2009, 387:28-41.
    • (2009) J Mol Biol , vol.387 , pp. 28-41
    • Nesbit, A.D.1    Giel, J.L.2    Rose, J.C.3    Kiley, P.J.4
  • 35
    • 67349095027 scopus 로고    scopus 로고
    • Small RNA-induced differential degradation of the polycistronic mRNA iscRSUA
    • Desnoyers G., Morissette A., Prevost K., Masse E. Small RNA-induced differential degradation of the polycistronic mRNA iscRSUA. EMBO J 2009, 28:1551-1561.
    • (2009) EMBO J , vol.28 , pp. 1551-1561
    • Desnoyers, G.1    Morissette, A.2    Prevost, K.3    Masse, E.4
  • 36
    • 70449455583 scopus 로고    scopus 로고
    • The SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster transfer
    • Chahal H.K., Dai Y., Saini A., Ayala-Castro C., Outten F.W. The SufBCD Fe-S scaffold complex interacts with SufA for Fe-S cluster transfer. Biochemistry 2009, 48:10644-10653.
    • (2009) Biochemistry , vol.48 , pp. 10644-10653
    • Chahal, H.K.1    Dai, Y.2    Saini, A.3    Ayala-Castro, C.4    Outten, F.W.5
  • 37
    • 69949162828 scopus 로고    scopus 로고
    • Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes
    • Gupta V., Sendra M., Naik S.G., Chahal H.K., Huynh B.H., Outten F.W., Fontecave M., Ollagnier de Choudens S. Native Escherichia coli SufA, coexpressed with SufBCDSE, purifies as a [2Fe-2S] protein and acts as an Fe-S transporter to Fe-S target enzymes. JACS 2009, 131:6149-6153.
    • (2009) JACS , vol.131 , pp. 6149-6153
    • Gupta, V.1    Sendra, M.2    Naik, S.G.3    Chahal, H.K.4    Huynh, B.H.5    Outten, F.W.6    Fontecave, M.7    Ollagnier de Choudens, S.8
  • 38
    • 67149111967 scopus 로고    scopus 로고
    • Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers
    • Vinella D., Brochier-Armanet C., Loiseau L., Talla E., Barras F. Iron-sulfur (Fe/S) protein biogenesis: phylogenomic and genetic studies of A-type carriers. PLoS Genet 2009, 5:e1000497.
    • (2009) PLoS Genet , vol.5
    • Vinella, D.1    Brochier-Armanet, C.2    Loiseau, L.3    Talla, E.4    Barras, F.5
  • 39
    • 38749100215 scopus 로고    scopus 로고
    • Complementary roles of SufA and IscA in the biogenesis of iron-sulfur clusters in Escherichia coli
    • Lu J., Yang J., Tan G., Ding H. Complementary roles of SufA and IscA in the biogenesis of iron-sulfur clusters in Escherichia coli. Biochem J 2008, 409:535-543.
    • (2008) Biochem J , vol.409 , pp. 535-543
    • Lu, J.1    Yang, J.2    Tan, G.3    Ding, H.4
  • 40
    • 7244239273 scopus 로고    scopus 로고
    • Repair of oxidized iron-sulfur clusters in Escherichia coli
    • Djaman O., Outten F.W., Imlay J.A. Repair of oxidized iron-sulfur clusters in Escherichia coli. J Biol Chem 2004, 279:44590-44599.
    • (2004) J Biol Chem , vol.279 , pp. 44590-44599
    • Djaman, O.1    Outten, F.W.2    Imlay, J.A.3
  • 41
    • 56249090364 scopus 로고    scopus 로고
    • The impact of O2 on the Fe-S cluster biogenesis requirements of Escherichia coli FNR
    • Mettert E.L., Outten F.W., Wanta B., Kiley P.J. The impact of O2 on the Fe-S cluster biogenesis requirements of Escherichia coli FNR. J Mol Biol 2008, 384:798-811.
    • (2008) J Mol Biol , vol.384 , pp. 798-811
    • Mettert, E.L.1    Outten, F.W.2    Wanta, B.3    Kiley, P.J.4
  • 43
    • 72049124821 scopus 로고    scopus 로고
    • The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein
    • Trotter V., Vinella D., Loiseau L., Ollagnier de Choudens S., Fontecave M., Barras F. The CsdA cysteine desulphurase promotes Fe/S biogenesis by recruiting Suf components and participates to a new sulphur transfer pathway by recruiting CsdL (ex-YgdL), a ubiquitin-modifying-like protein. Mol Microbiol 2009, 74:1527-1542.
    • (2009) Mol Microbiol , vol.74 , pp. 1527-1542
    • Trotter, V.1    Vinella, D.2    Loiseau, L.3    Ollagnier de Choudens, S.4    Fontecave, M.5    Barras, F.6
  • 44
    • 46049084588 scopus 로고    scopus 로고
    • Salmonella enterica requires ApbC function for growth on tricarballylate: evidence of functional redundancy between ApbC and IscU
    • Boyd J.M., Lewis J.A., Escalante-Semerena J.C., Downs D.M. Salmonella enterica requires ApbC function for growth on tricarballylate: evidence of functional redundancy between ApbC and IscU. J Bacteriol 2008, 190:4596-4602.
    • (2008) J Bacteriol , vol.190 , pp. 4596-4602
    • Boyd, J.M.1    Lewis, J.A.2    Escalante-Semerena, J.C.3    Downs, D.M.4
  • 45
    • 46649115965 scopus 로고    scopus 로고
    • NfuA, a new factor required for maturing Fe/S proteins in Escherichia coli under oxidative stress and iron starvation conditions
    • Angelini S., Gerez C., Ollagnier-de Choudens S., Sanakis Y., Fontecave M., Barras F., Py B. NfuA, a new factor required for maturing Fe/S proteins in Escherichia coli under oxidative stress and iron starvation conditions. J Biol Chem 2008, 283:14084-14091.
    • (2008) J Biol Chem , vol.283 , pp. 14084-14091
    • Angelini, S.1    Gerez, C.2    Ollagnier-de Choudens, S.3    Sanakis, Y.4    Fontecave, M.5    Barras, F.6    Py, B.7
  • 47
    • 59449083567 scopus 로고    scopus 로고
    • Di-iron proteins of the Ric family are involved in iron-sulfur cluster repair
    • Justino M.C., Baptista J.M., Saraiva L.M. Di-iron proteins of the Ric family are involved in iron-sulfur cluster repair. Biometals 2009, 22:99-108.
    • (2009) Biometals , vol.22 , pp. 99-108
    • Justino, M.C.1    Baptista, J.M.2    Saraiva, L.M.3
  • 48
    • 61449135987 scopus 로고    scopus 로고
    • Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica
    • Thorgersen M.P., Downs D.M. Oxidative stress and disruption of labile iron generate specific auxotrophic requirements in Salmonella enterica. Microbiology 2009, 155:295-304.
    • (2009) Microbiology , vol.155 , pp. 295-304
    • Thorgersen, M.P.1    Downs, D.M.2
  • 50
    • 36148932962 scopus 로고    scopus 로고
    • SufR coordinates two [4Fe-4S]2+, 1+ clusters and functions as a transcriptional repressor of the sufBCDS operon and an autoregulator of sufR in cyanobacteria
    • Shen G., Balasubramanian R., Wang T., Wu Y., Hoffart L.M., Krebs C., Bryant D.A., Golbeck J.H. SufR coordinates two [4Fe-4S]2+, 1+ clusters and functions as a transcriptional repressor of the sufBCDS operon and an autoregulator of sufR in cyanobacteria. J Biol Chem 2007, 282:31909-31919.
    • (2007) J Biol Chem , vol.282 , pp. 31909-31919
    • Shen, G.1    Balasubramanian, R.2    Wang, T.3    Wu, Y.4    Hoffart, L.M.5    Krebs, C.6    Bryant, D.A.7    Golbeck, J.H.8
  • 52
    • 60649117402 scopus 로고    scopus 로고
    • Structural studies of the Enterococcus faecalis SufU [Fe-S] cluster protein
    • Riboldi G.P., Verli H., Frazzon J. Structural studies of the Enterococcus faecalis SufU [Fe-S] cluster protein. BMC Biochem 2009, 10:3.
    • (2009) BMC Biochem , vol.10 , pp. 3
    • Riboldi, G.P.1    Verli, H.2    Frazzon, J.3
  • 55
    • 70350144292 scopus 로고    scopus 로고
    • NsrR targets in the Escherichia coli genome: new insights into DNA sequence requirements for binding and a role for NsrR in the regulation of motility
    • Partridge J.D., Bodenmiller D.M., Humphrys M.S., Spiro S. NsrR targets in the Escherichia coli genome: new insights into DNA sequence requirements for binding and a role for NsrR in the regulation of motility. Mol Microbiol 2009, 73:680-694.
    • (2009) Mol Microbiol , vol.73 , pp. 680-694
    • Partridge, J.D.1    Bodenmiller, D.M.2    Humphrys, M.S.3    Spiro, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.