메뉴 건너뛰기




Volumn 195, Issue 18, 2013, Pages 4138-4145

The synechocystis PCC6803 MerA-like enzyme operates in the reduction of both mercury and uranium under the control of the glutaredoxin 1 enzyme

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GLUTAREDOXIN; GLUTAREDOXIN 1; MERCURY; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; UNCLASSIFIED DRUG; URANIUM;

EID: 84883280072     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00272-13     Document Type: Article
Times cited : (43)

References (39)
  • 1
    • 84871675776 scopus 로고    scopus 로고
    • Genomics of the pleiotropic glutathione system in cyanobacteria
    • Cassier-Chauvat C, Chauvat F (ed), Elsevier Academic Press, New York, NY
    • Narainsamy K, Marteyn B, Sakr S, Cassier-Chauvat C, Chauvat F. 2013. Genomics of the pleiotropic glutathione system in cyanobacteria, p. 157-188. In Cassier-Chauvat C, Chauvat F (ed), Genomics of cyanobacteria, vol 65. Elsevier Academic Press, New York, NY.
    • (2013) Genomics of cyanobacteria , vol.65 , pp. 157-188
    • Narainsamy, K.1    Marteyn, B.2    Sakr, S.3    Cassier-Chauvat, C.4    Chauvat, F.5
  • 3
    • 58149308104 scopus 로고    scopus 로고
    • The thioredoxin reductase-glutaredoxins-ferredoxin crossroad pathway for selenate tolerance in Synechocystis PCC6803
    • Marteyn B, Domain F, Legrain P, Chauvat F, Cassier-Chauvat C. 2009. The thioredoxin reductase-glutaredoxins-ferredoxin crossroad pathway for selenate tolerance in Synechocystis PCC6803. Mol. Microbiol. 71:520-532.
    • (2009) Mol. Microbiol. , vol.71 , pp. 520-532
    • Marteyn, B.1    Domain, F.2    Legrain, P.3    Chauvat, F.4    Cassier-Chauvat, C.5
  • 4
    • 1542320094 scopus 로고    scopus 로고
    • Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase
    • Johansson C, Lillig CH, Holmgren A. 2004. Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J. Biol. Chem. 279:7537-7543.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7537-7543
    • Johansson, C.1    Lillig, C.H.2    Holmgren, A.3
  • 5
    • 44049097906 scopus 로고    scopus 로고
    • Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii reveals the unique properties of a chloroplastic CGFS-type glutaredoxin
    • Zaffagnini M, Michelet L, Massot V, Trost P, Lemaire SD. 2008. Biochemical characterization of glutaredoxins from Chlamydomonas reinhardtii reveals the unique properties of a chloroplastic CGFS-type glutaredoxin. J. Biol. Chem. 283:8868-8876.
    • (2008) J. Biol. Chem. , vol.283 , pp. 8868-8876
    • Zaffagnini, M.1    Michelet, L.2    Massot, V.3    Trost, P.4    Lemaire, S.D.5
  • 6
    • 79951741634 scopus 로고    scopus 로고
    • Structural and functional diversity of glutaredoxins in yeast
    • Herrero E, Belli G, Casa C. 2010. Structural and functional diversity of glutaredoxins in yeast. Curr. Protein Pept. Sci. 11(8):659-668.
    • (2010) Curr. Protein Pept. Sci. , vol.11 , Issue.8 , pp. 659-668
    • Herrero, E.1    Belli, G.2    Casa, C.3
  • 9
    • 0038491193 scopus 로고    scopus 로고
    • Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin
    • Tamarit J, Belli G, Cabiscol E, Herrero E, Ros J. 2003. Biochemical characterization of yeast mitochondrial Grx5 monothiol glutaredoxin. J. Biol. Chem. 278:25745-25751.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25745-25751
    • Tamarit, J.1    Belli, G.2    Cabiscol, E.3    Herrero, E.4    Ros, J.5
  • 11
    • 37349036175 scopus 로고    scopus 로고
    • CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster
    • Picciocchi A, Saguez C, Boussac A, Cassier-Chauvat C, Chauvat F. 2007. CGFS-type monothiol glutaredoxins from the cyanobacterium Synechocystis PCC6803 and other evolutionary distant model organisms possess a glutathione-ligated [2Fe-2S] cluster. Biochemistry 46:15018-15026.
    • (2007) Biochemistry , vol.46 , pp. 15018-15026
    • Picciocchi, A.1    Saguez, C.2    Boussac, A.3    Cassier-Chauvat, C.4    Chauvat, F.5
  • 12
    • 66149092715 scopus 로고    scopus 로고
    • The glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803
    • Lopez-Maury L, Sanchez-Riego AM, Reyes JC, Florencio FJ. 2009. The glutathione/glutaredoxin system is essential for arsenate reduction in Synechocystis sp. strain PCC 6803. J. Bacteriol. 191:3534-3543.
    • (2009) J. Bacteriol. , vol.191 , pp. 3534-3543
    • Lopez-Maury, L.1    Sanchez-Riego, A.M.2    Reyes, J.C.3    Florencio, F.J.4
  • 14
    • 0022408990 scopus 로고
    • Influence of leaching parameters on the biological removal of uranium from coal by a filamentous cyanobacterium
    • Lorenz MG, Krumbein WE. 1985. Influence of leaching parameters on the biological removal of uranium from coal by a filamentous cyanobacterium. Appl. Environ. Microbiol. 50:1296-1300.
    • (1985) Appl. Environ. Microbiol. , vol.50 , pp. 1296-1300
    • Lorenz, M.G.1    Krumbein, W.E.2
  • 16
    • 33745915895 scopus 로고    scopus 로고
    • The toxicology of mercury and its chemical compounds
    • Clarkson TW, Magos L. 2006. The toxicology of mercury and its chemical compounds. Crit. Rev. Toxicol. 36:609-662.
    • (2006) Crit. Rev. Toxicol. , vol.36 , pp. 609-662
    • Clarkson, T.W.1    Magos, L.2
  • 18
    • 82355190258 scopus 로고    scopus 로고
    • Exopolysaccharideproducing cyanobacteria in heavy metal removal from water: molecular basis and practical applicability of the biosorption process
    • De Philippis R, Colica G, Micheletti E. 2011. Exopolysaccharideproducing cyanobacteria in heavy metal removal from water: molecular basis and practical applicability of the biosorption process. Appl. Microbiol. Biotechnol. 92:697-708.
    • (2011) Appl. Microbiol. Biotechnol. , vol.92 , pp. 697-708
    • De Philippis, R.1    Colica, G.2    Micheletti, E.3
  • 22
    • 3142559798 scopus 로고    scopus 로고
    • Function and regulation of the cyanobacterial genes lexA, recA and ruvB: LexA is critical to the survival of cells facing inorganic carbon starvation
    • Domain F, Houot L, Chauvat F, Cassier-Chauvat C. 2004. Function and regulation of the cyanobacterial genes lexA, recA and ruvB: LexA is critical to the survival of cells facing inorganic carbon starvation. Mol. Microbiol. 53:65-80.
    • (2004) Mol. Microbiol. , vol.53 , pp. 65-80
    • Domain, F.1    Houot, L.2    Chauvat, F.3    Cassier-Chauvat, C.4
  • 23
    • 0030613795 scopus 로고    scopus 로고
    • Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli
    • Kanemori M, Nishihara K, Yanagi H, Yura T. 1997. Synergistic roles of HslVU and other ATP-dependent proteases in controlling in vivo turnover of sigma32 and abnormal proteins in Escherichia coli. J. Bacteriol. 179:7219-7225.
    • (1997) J. Bacteriol. , vol.179 , pp. 7219-7225
    • Kanemori, M.1    Nishihara, K.2    Yanagi, H.3    Yura, T.4
  • 24
    • 0032510783 scopus 로고    scopus 로고
    • A bacterial twohybrid system based on a reconstituted signal transduction pathway
    • Karimova G, Pidoux J, Ullmann A, Ladant D. 1998. A bacterial twohybrid system based on a reconstituted signal transduction pathway. Proc. Natl. Acad. Sci. U. S. A. 95:5752-5756.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5752-5756
    • Karimova, G.1    Pidoux, J.2    Ullmann, A.3    Ladant, D.4
  • 25
    • 0024399346 scopus 로고
    • Insertional mutagenesis by random cloning of antibiotic resistance genes into the genome of the cyanobacterium Synechocystis PCC6803
    • Labarre J, Chauvat F, Thuriaux P. 1989. Insertional mutagenesis by random cloning of antibiotic resistance genes into the genome of the cyanobacterium Synechocystis PCC6803. J. Bacteriol. 171:3449-3457.
    • (1989) J. Bacteriol. , vol.171 , pp. 3449-3457
    • Labarre, J.1    Chauvat, F.2    Thuriaux, P.3
  • 26
    • 0020478725 scopus 로고
    • Mercuric reductase Purification and characterization of a transposon-encoded flavoprotein containing an oxidationreduction-active disulfide
    • Fox B, Walsh CT. 1982. Mercuric reductase. Purification and characterization of a transposon-encoded flavoprotein containing an oxidationreduction-active disulfide. J. Biol. Chem. 257:2498-2503.
    • (1982) J. Biol. Chem. , vol.257 , pp. 2498-2503
    • Fox, B.1    Walsh, C.T.2
  • 27
    • 0038266370 scopus 로고    scopus 로고
    • Redox regulation of 3=-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins
    • Lillig CH, Potamitou A, Schwenn JD, Vlamis-Gardikas A, Holmgren A. 2003. Redox regulation of 3=-phosphoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins. J. Biol. Chem. 278: 22325-22330.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22325-22330
    • Lillig, C.H.1    Potamitou, A.2    Schwenn, J.D.3    Vlamis-Gardikas, A.4    Holmgren, A.5
  • 29
    • 70349909319 scopus 로고    scopus 로고
    • ZipN, a FtsA-like orchestrator of divisome assembly in the model cyanobacterium Synechocystis PCC6803
    • Marbouty M, Saguez C, Cassier-Chauvat C, Chauvat F. 2009. ZipN, a FtsA-like orchestrator of divisome assembly in the model cyanobacterium Synechocystis PCC6803. Mol. Microbiol. 74:409-420.
    • (2009) Mol. Microbiol. , vol.74 , pp. 409-420
    • Marbouty, M.1    Saguez, C.2    Cassier-Chauvat, C.3    Chauvat, F.4
  • 30
    • 0348230942 scopus 로고    scopus 로고
    • Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system
    • Fernandes AP, Holmgren A. 2004. Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Antioxid. Redox Signal. 6(1):63-74.
    • (2004) Antioxid. Redox Signal. , vol.6 , Issue.1 , pp. 63-74
    • Fernandes, A.P.1    Holmgren, A.2
  • 31
    • 28644437016 scopus 로고    scopus 로고
    • A bacterial view of the periodic table: genes and proteins for toxic inorganic ions
    • Silver S, Phung L. 2005. A bacterial view of the periodic table: genes and proteins for toxic inorganic ions. J. Ind. Microbiol. Biotechnol. 32:587-605.
    • (2005) J. Ind. Microbiol. Biotechnol. , vol.32 , pp. 587-605
    • Silver, S.1    Phung, L.2
  • 32
    • 0028348970 scopus 로고
    • A conditional expression vector for the cyanobacteria Synechocystis sp PCC6803 and PCC6714 or Synechococcus sp. PCC7942 and PCC6301
    • Mermet-Bouvier P, Chauvat F. 1994. A conditional expression vector for the cyanobacteria Synechocystis sp. PCC6803 and PCC6714 or Synechococcus sp. PCC7942 and PCC6301. Curr. Microbiol. 28:145-148.
    • (1994) Curr. Microbiol. , vol.28 , pp. 145-148
    • Mermet-Bouvier, P.1    Chauvat, F.2
  • 33
    • 0031803632 scopus 로고    scopus 로고
    • Targeted deletion and mutational analysis of the essential (2Fe-2S) plantlike ferredoxin in Synechocystis PCC6803 by plasmid shuffling
    • Poncelet M, Cassier-Chauvat C, Leschelle X, Bottin H, Chauvat F. 1998. Targeted deletion and mutational analysis of the essential (2Fe-2S) plantlike ferredoxin in Synechocystis PCC6803 by plasmid shuffling. Mol. Microbiol. 28:813-821.
    • (1998) Mol. Microbiol. , vol.28 , pp. 813-821
    • Poncelet, M.1    Cassier-Chauvat, C.2    Leschelle, X.3    Bottin, H.4    Chauvat, F.5
  • 34
    • 0027688535 scopus 로고
    • A conjugative plasmid vector for promoter analysis in several cyanobacteria of the genera Synechococcus and Synechocystis
    • Marraccini P, Bulteau S, Cassier-Chauvat C, Mermet-Bouvier P, Chauvat F. 1993. A conjugative plasmid vector for promoter analysis in several cyanobacteria of the genera Synechococcus and Synechocystis. Plant Mol. Biol. 23:905-909.
    • (1993) Plant Mol. Biol. , vol.23 , pp. 905-909
    • Marraccini, P.1    Bulteau, S.2    Cassier-Chauvat, C.3    Mermet-Bouvier, P.4    Chauvat, F.5
  • 35
    • 0344393487 scopus 로고    scopus 로고
    • An arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristics
    • Li R, Haile JD, Kennelly PJ. 2003. An arsenate reductase from Synechocystis sp. strain PCC 6803 exhibits a novel combination of catalytic characteristics. J. Bacteriol. 185:6780-6789.
    • (2003) J. Bacteriol. , vol.185 , pp. 6780-6789
    • Li, R.1    Haile, J.D.2    Kennelly, P.J.3
  • 36
    • 67650999518 scopus 로고    scopus 로고
    • Evolution and diversity of glutaredoxins in photosynthetic organisms
    • Couturier J, Jacquot JP, Rouhier N. 2009. Evolution and diversity of glutaredoxins in photosynthetic organisms. Cell. Mol. Life Sci. 66:2539-2557.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2539-2557
    • Couturier, J.1    Jacquot, J.P.2    Rouhier, N.3
  • 37
    • 34548163922 scopus 로고    scopus 로고
    • Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress
    • Gallogly MM, Mieyal JJ. 2007. Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr. Opin. Pharmacol. 7:381-391.
    • (2007) Curr. Opin. Pharmacol. , vol.7 , pp. 381-391
    • Gallogly, M.M.1    Mieyal, J.J.2
  • 39
    • 0025896072 scopus 로고
    • Plasmid vectors for selecting IS1-promoted deletions in cloned DNA: sequence analysis of the omega interposon
    • Prentki P, Binda A, Epstein A. 1991. Plasmid vectors for selecting IS1-promoted deletions in cloned DNA: sequence analysis of the omega interposon. Gene 103:17-23.
    • (1991) Gene , vol.103 , pp. 17-23
    • Prentki, P.1    Binda, A.2    Epstein, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.