메뉴 건너뛰기




Volumn 46, Issue 17, 2007, Pages 5030-5037

NikA binds heme: A new role for an Escherichia coli periplasmic nickel-binding protein

Author keywords

[No Author keywords available]

Indexed keywords

HEME PROTEINS; NICKEL-BINDING SITES; PERIPLASMIC BINDING PROTEINS; PROTOPORPHYRIN; TETRAPYRROLES;

EID: 34247584487     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi700183u     Document Type: Article
Times cited : (38)

References (50)
  • 2
    • 0036667415 scopus 로고    scopus 로고
    • A whole genome view of prokaryotic haem biosynthesis
    • Panek, H., and O'Brian, M. R. (2002) A whole genome view of prokaryotic haem biosynthesis, Microbiology 148, 2273-2282.
    • (2002) Microbiology , vol.148 , pp. 2273-2282
    • Panek, H.1    O'Brian, M.R.2
  • 3
    • 0032555539 scopus 로고    scopus 로고
    • Prototype of a heme chaperone essential for cytochrome c maturation
    • Schulz, H., Hennecke, H., and Thony-Meyer, L. (1998) Prototype of a heme chaperone essential for cytochrome c maturation, Science 281, 1197-1200.
    • (1998) Science , vol.281 , pp. 1197-1200
    • Schulz, H.1    Hennecke, H.2    Thony-Meyer, L.3
  • 4
    • 33646585766 scopus 로고    scopus 로고
    • Dynamic ligation properties of the Escherichia coli heme chaperone CcmE to non-covalently bound heme
    • Stevens, J. M., Uchida, T., Daltrop, O., Kitagawa, T., and Ferguson, S. J. (2006) Dynamic ligation properties of the Escherichia coli heme chaperone CcmE to non-covalently bound heme, J. Biol. Chem. 281, 6144-6151.
    • (2006) J. Biol. Chem , vol.281 , pp. 6144-6151
    • Stevens, J.M.1    Uchida, T.2    Daltrop, O.3    Kitagawa, T.4    Ferguson, S.J.5
  • 7
    • 0022639247 scopus 로고
    • Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity
    • Wu, L. F., and Mandrand-Berthelot, M. A. (1986) Genetic and physiological characterization of new Escherichia coli mutants impaired in hydrogenase activity, Biochimie 68, 167-179.
    • (1986) Biochimie , vol.68 , pp. 167-179
    • Wu, L.F.1    Mandrand-Berthelot, M.A.2
  • 8
    • 0024836127 scopus 로고
    • Nickel deficiency gives rise to the defective hydrogenase phenotype of hydC and fnr mutants in Escherichia coli
    • Wu, L. F., Mandrand-Berthelot, M. A., Waugh, R., Edmonds, C. J., Holt, S. E., and Boxer, D. H. (1989) Nickel deficiency gives rise to the defective hydrogenase phenotype of hydC and fnr mutants in Escherichia coli, Mol. Microbiol. 3, 1709-1718.
    • (1989) Mol. Microbiol , vol.3 , pp. 1709-1718
    • Wu, L.F.1    Mandrand-Berthelot, M.A.2    Waugh, R.3    Edmonds, C.J.4    Holt, S.E.5    Boxer, D.H.6
  • 9
    • 0027482679 scopus 로고
    • The nik operon of Escherichia coli encodes a periplasmic binding-protein-dependent transport-system for nickel
    • Navarro, C., Wu, L. F., and Mandrand-Berthelot, M. A. (1993) The nik operon of Escherichia coli encodes a periplasmic binding-protein-dependent transport-system for nickel, Mol. Microbiol. 9, 1181-1191.
    • (1993) Mol. Microbiol , vol.9 , pp. 1181-1191
    • Navarro, C.1    Wu, L.F.2    Mandrand-Berthelot, M.A.3
  • 10
    • 0025984451 scopus 로고
    • The hydC region contains a multi-cistronic operon (Nik) involved in nickel transport in Escherichia coli
    • Wu, L. F., Navarro, C., and Mandrand-Berthelot, M. A. (1991) The hydC region contains a multi-cistronic operon (Nik) involved in nickel transport in Escherichia coli, Gene 107, 37-42.
    • (1991) Gene , vol.107 , pp. 37-42
    • Wu, L.F.1    Navarro, C.2    Mandrand-Berthelot, M.A.3
  • 11
    • 0032932493 scopus 로고    scopus 로고
    • Isolation and characterization of the nikR gene encoding a nickel-responsive regulator in Escherichia coli
    • De Pina, K., Desjardin, V., Mandrand-Berthelot, M. A., Giordano, G., and Wu, L. F. (1999) Isolation and characterization of the nikR gene encoding a nickel-responsive regulator in Escherichia coli, J. Bacteriol. 181, 670-674.
    • (1999) J. Bacteriol , vol.181 , pp. 670-674
    • De Pina, K.1    Desjardin, V.2    Mandrand-Berthelot, M.A.3    Giordano, G.4    Wu, L.F.5
  • 12
    • 0028798434 scopus 로고
    • Oxidative mechanisms in the toxicity of metal ions
    • Stohs, S. J., and Bagchi, D. (1995) Oxidative mechanisms in the toxicity of metal ions, Free Radical Biol. Med. 18, 321-336.
    • (1995) Free Radical Biol. Med , vol.18 , pp. 321-336
    • Stohs, S.J.1    Bagchi, D.2
  • 14
    • 0036192820 scopus 로고    scopus 로고
    • A fluorescence-based sensing system for the environmental monitoring of nickel using the nickel binding protein from Escherichia coli
    • Salins, L. L. E., Goldsmith, E. S., Ensor, C. M., and Daunert, S. (2002) A fluorescence-based sensing system for the environmental monitoring of nickel using the nickel binding protein from Escherichia coli, Anal. Bioanal. Chem. 372, 174-180.
    • (2002) Anal. Bioanal. Chem , vol.372 , pp. 174-180
    • Salins, L.L.E.1    Goldsmith, E.S.2    Ensor, C.M.3    Daunert, S.4
  • 15
    • 0346118916 scopus 로고    scopus 로고
    • Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli
    • Heddle, J., Scott, D. J., Unzai, S., Park, S. Y., and Tame, J. R. H. (2003) Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli, J. Biol. Chem. 278, 50322-50329.
    • (2003) J. Biol. Chem , vol.278 , pp. 50322-50329
    • Heddle, J.1    Scott, D.J.2    Unzai, S.3    Park, S.Y.4    Tame, J.R.H.5
  • 16
    • 0037147266 scopus 로고    scopus 로고
    • Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly
    • Pittman, M. S., Corker, H., Wu, G. H., Binet, M. B., Moir, A. J. G., and Poole, R. K. (2002) Cysteine is exported from the Escherichia coli cytoplasm by CydDC, an ATP-binding cassette-type transporter required for cytochrome assembly, J. Biol. Chem. 277, 49841-49849.
    • (2002) J. Biol. Chem , vol.277 , pp. 49841-49849
    • Pittman, M.S.1    Corker, H.2    Wu, G.H.3    Binet, M.B.4    Moir, A.J.G.5    Poole, R.K.6
  • 17
    • 25444517605 scopus 로고    scopus 로고
    • A Bacterial Glutathione Transporter (Escherichia coli CydDC) Exports Reductant to the Periplasm
    • Pittman, M. S., Robinson, H. C., and Poole, R. K. (2005) A Bacterial Glutathione Transporter (Escherichia coli CydDC) Exports Reductant to the Periplasm, J. Biol. Chem. 280, 32254-32261.
    • (2005) J. Biol. Chem , vol.280 , pp. 32254-32261
    • Pittman, M.S.1    Robinson, H.C.2    Poole, R.K.3
  • 18
    • 0027489253 scopus 로고
    • Cytochrome bd biosynthesis in Escherichia coli: The sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter
    • Poole, R. K., Hatch, L., Cleeter, M. W. J., Gibson, F., Cox, G. B., and Wu, G. H. (1993) Cytochrome bd biosynthesis in Escherichia coli: The sequences of the cydC and cydD genes suggest that they encode the components of an ABC membrane transporter, Mol. Microbiol. 10, 421-430.
    • (1993) Mol. Microbiol , vol.10 , pp. 421-430
    • Poole, R.K.1    Hatch, L.2    Cleeter, M.W.J.3    Gibson, F.4    Cox, G.B.5    Wu, G.H.6
  • 19
    • 0028177039 scopus 로고
    • The cydD gene-product, component of a heterodimeric ABC transporter, is required for assembly of periplasmic cytochrome c and of cytochrome bd in Escherichia coli
    • Poole, R. K., Gibson, F., and Wu, G. H. (1994) The cydD gene-product, component of a heterodimeric ABC transporter, is required for assembly of periplasmic cytochrome c and of cytochrome bd in Escherichia coli, FEMS Microbiol. Lett. 117, 217-224.
    • (1994) FEMS Microbiol. Lett , vol.117 , pp. 217-224
    • Poole, R.K.1    Gibson, F.2    Wu, G.H.3
  • 20
    • 0029858253 scopus 로고    scopus 로고
    • Use of heme reporters for studies of cytochrome biosynthesis and heme transport
    • Goldman, B. S., Gabbert, K. K., and Kranz, R. G. (1996) Use of heme reporters for studies of cytochrome biosynthesis and heme transport, J. Bacteriol. 178, 6338-6347.
    • (1996) J. Bacteriol , vol.178 , pp. 6338-6347
    • Goldman, B.S.1    Gabbert, K.K.2    Kranz, R.G.3
  • 21
    • 0036400868 scopus 로고    scopus 로고
    • A novel haem compound accumulated in Escherichia coli overexpressing the cydDC operon, encoding an ABC-type transporter required for cytochrome assembly
    • Cook, G. M., Cruz-Ramos, H., Moir, A. J. G., and Poole, R. K. (2002) A novel haem compound accumulated in Escherichia coli overexpressing the cydDC operon, encoding an ABC-type transporter required for cytochrome assembly, Arch. Microbiol. 178, 358-369.
    • (2002) Arch. Microbiol , vol.178 , pp. 358-369
    • Cook, G.M.1    Cruz-Ramos, H.2    Moir, A.J.G.3    Poole, R.K.4
  • 24
    • 0017615828 scopus 로고
    • 0 portion of the magnesium ion-stimulated adenosine-triphosphatase of Escherichia coli K12: The uncC424 allele
    • 0 portion of the magnesium ion-stimulated adenosine-triphosphatase of Escherichia coli K12: The uncC424 allele, Biochem. J. 164, 193-198.
    • (1977) Biochem. J , vol.164 , pp. 193-198
    • Gibson, F.1    Cox, G.B.2    Downie, J.A.3    Radik, J.4
  • 25
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier, F. W. (1991) Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system, J. Mol. Biol. 219, 37-44.
    • (1991) J. Mol. Biol , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 26
    • 0029742635 scopus 로고    scopus 로고
    • Proteome of Salmonella typhimurium SL1344: Identification of novel abundant cell envelope proteins and assignment to a two-dimensional reference map
    • Qi, S. Y., Moir, A. J. G., and O'Connor, D. (1996) Proteome of Salmonella typhimurium SL1344: Identification of novel abundant cell envelope proteins and assignment to a two-dimensional reference map, J. Bacteriol. 178, 5032-5038.
    • (1996) J. Bacteriol , vol.178 , pp. 5032-5038
    • Qi, S.Y.1    Moir, A.J.G.2    O'Connor, D.3
  • 27
    • 0344734168 scopus 로고    scopus 로고
    • Time-resolved and steady-state fluorescence quenching of N-acetyl-L-tryptophanamide by acrylamide and iodide
    • Zelent, B., Kusba, J., Gryczynski, L, Johnson, M. L., and Lakowicz, J. R. (1998) Time-resolved and steady-state fluorescence quenching of N-acetyl-L-tryptophanamide by acrylamide and iodide, Biophys. Chem. 73, 53-75.
    • (1998) Biophys. Chem , vol.73 , pp. 53-75
    • Zelent, B.1    Kusba, J.2    Gryczynski, L.3    Johnson, M.L.4    Lakowicz, J.R.5
  • 28
    • 0037093643 scopus 로고    scopus 로고
    • Docking unbound proteins using shape complementarity, desolvation, and electrostatics
    • Chen, R., and Weng, Z. (2002) Docking unbound proteins using shape complementarity, desolvation, and electrostatics, Proteins 47, 281-294.
    • (2002) Proteins , vol.47 , pp. 281-294
    • Chen, R.1    Weng, Z.2
  • 30
    • 0038072139 scopus 로고    scopus 로고
    • Haem-polypeptide interactions during cytochrome c maturation
    • Thony-Meyer, L. (2000) Haem-polypeptide interactions during cytochrome c maturation, Biochim. Biophys. Acta 1459, 316-324.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 316-324
    • Thony-Meyer, L.1
  • 31
    • 0034115404 scopus 로고    scopus 로고
    • Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli
    • Fabianek, R. A., Hennecke, H., and Thony-Meyer, L. (2000) Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli, FEMS Microbiol. Rev. 24, 303-316.
    • (2000) FEMS Microbiol. Rev , vol.24 , pp. 303-316
    • Fabianek, R.A.1    Hennecke, H.2    Thony-Meyer, L.3
  • 32
    • 0031875674 scopus 로고    scopus 로고
    • Molecular mechanisms of cytochrome c biogenesis: Three distinct systems
    • Kranz, R., Lill, R., Goldman, B., Bonnard, G., and Merchant, S. (1998) Molecular mechanisms of cytochrome c biogenesis: Three distinct systems, Mol. Microbiol. 29, 383-396.
    • (1998) Mol. Microbiol , vol.29 , pp. 383-396
    • Kranz, R.1    Lill, R.2    Goldman, B.3    Bonnard, G.4    Merchant, S.5
  • 33
    • 0032031987 scopus 로고    scopus 로고
    • Contrasting routes of c-type cytochrome assembly in mitochondria, chloroplasts and bacteria
    • Page, M. D., Sambongi, Y., and Ferguson, S. J. (1998) Contrasting routes of c-type cytochrome assembly in mitochondria, chloroplasts and bacteria, Trends Biochem. Sci. 23, 103-108.
    • (1998) Trends Biochem. Sci , vol.23 , pp. 103-108
    • Page, M.D.1    Sambongi, Y.2    Ferguson, S.J.3
  • 36
    • 32644489127 scopus 로고    scopus 로고
    • Characterization of the reaction products of cytochrome c with glutathione by mass spectrometry
    • Deng, H. T. (2006) Characterization of the reaction products of cytochrome c with glutathione by mass spectrometry, Biochem. Biophys. Res. Commun. 342, 73-80.
    • (2006) Biochem. Biophys. Res. Commun , vol.342 , pp. 73-80
    • Deng, H.T.1
  • 39
    • 0028072561 scopus 로고
    • The dipeptide permease of Escherichia coli closely resembles other bacterial transport-systems and shows growth-phase-dependent expression
    • Abouhamad, W. N., and Manson, M. D. (1994) The dipeptide permease of Escherichia coli closely resembles other bacterial transport-systems and shows growth-phase-dependent expression, Mol. Microbiol. 14, 1077-1092.
    • (1994) Mol. Microbiol , vol.14 , pp. 1077-1092
    • Abouhamad, W.N.1    Manson, M.D.2
  • 40
    • 0029175995 scopus 로고
    • Modeling of the structure of the Haemophilus influenzae heme-binding protein suggests a mode of heme interaction
    • Dunten, P., and Mowbray, S. L. (1995) Modeling of the structure of the Haemophilus influenzae heme-binding protein suggests a mode of heme interaction, Protein Sci. 4, 2335-2340.
    • (1995) Protein Sci , vol.4 , pp. 2335-2340
    • Dunten, P.1    Mowbray, S.L.2
  • 42
    • 33748053969 scopus 로고    scopus 로고
    • The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins
    • Letoffe, S., Delepelaire, P., and Wandersman, C. (2006) The housekeeping dipeptide permease is the Escherichia coli heme transporter and functions with two optional peptide binding proteins, Proc. Natl. Acad. Sci. U.S.A. 103, 12891-12896.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 12891-12896
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 43
    • 0025366313 scopus 로고
    • Cloning and sequencing of a putative Escherichia coli [NiFe] Hydrogenase-1 operon containing 6 open reading frames
    • Menon, N. K., Robbins, J., Peck, H. D., Chatelus, C. Y., Choi, E. S., and Przybyla, A. E. (1990) Cloning and sequencing of a putative Escherichia coli [NiFe] Hydrogenase-1 operon containing 6 open reading frames, J. Bacteriol. 172, 1969-1977.
    • (1990) J. Bacteriol , vol.172 , pp. 1969-1977
    • Menon, N.K.1    Robbins, J.2    Peck, H.D.3    Chatelus, C.Y.4    Choi, E.S.5    Przybyla, A.E.6
  • 44
    • 0032146314 scopus 로고    scopus 로고
    • Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit: Identification of a soluble precursor of the small subunit in a hypB mutant
    • Sargent, F., Ballantine, S. P., Rugman, P. A., Palmer, T., and Boxer, D. H. (1998) Reassignment of the gene encoding the Escherichia coli hydrogenase 2 small subunit: Identification of a soluble precursor of the small subunit in a hypB mutant, Eur. J. Biochem. 255, 746-754.
    • (1998) Eur. J. Biochem , vol.255 , pp. 746-754
    • Sargent, F.1    Ballantine, S.P.2    Rugman, P.A.3    Palmer, T.4    Boxer, D.H.5
  • 46
    • 0023049475 scopus 로고
    • Purification and properties of membrane-bound hydrogenase isoenzyme-1 from anaerobically grown Escherichia coli-K12
    • Sawers, R. G., and Boxer, D. H. (1986) Purification and properties of membrane-bound hydrogenase isoenzyme-1 from anaerobically grown Escherichia coli-K12, Eur. J. Biochem. 156, 265-275.
    • (1986) Eur. J. Biochem , vol.156 , pp. 265-275
    • Sawers, R.G.1    Boxer, D.H.2
  • 47
    • 0036836358 scopus 로고    scopus 로고
    • How bacteria get energy from hydrogen: A genetic analysis of periplasmic hydrogen oxidation in Escherichia coli
    • Dubini, A., Pye, R. L., Jack, R. L., Palmer, T., and Sargent, F. (2002) How bacteria get energy from hydrogen: A genetic analysis of periplasmic hydrogen oxidation in Escherichia coli, Int. J. Hydrogen Energy 27, 1413-1420.
    • (2002) Int. J. Hydrogen Energy , vol.27 , pp. 1413-1420
    • Dubini, A.1    Pye, R.L.2    Jack, R.L.3    Palmer, T.4    Sargent, F.5
  • 48
    • 0031756314 scopus 로고    scopus 로고
    • Electron transfer between hydrogenases and mono- and multiheme cytochromes in Desulfovibrio ssp
    • Pereira, I. A. C., Romao, C. V., Xavier, A. V., LeGall, J., and Teixeira, M. (1998) Electron transfer between hydrogenases and mono- and multiheme cytochromes in Desulfovibrio ssp., J. Biol. Inorg. Chem. 3, 494-498.
    • (1998) J. Biol. Inorg. Chem , vol.3 , pp. 494-498
    • Pereira, I.A.C.1    Romao, C.V.2    Xavier, A.V.3    LeGall, J.4    Teixeira, M.5
  • 49
    • 0033851906 scopus 로고    scopus 로고
    • Deletion of the hmc operon of Desulfovibrio vulgaris subsp vulgaris Hildenborough hampers hydrogen metabolism and low-redox-potential niche establishment
    • Dolla, A., Pohorelic, B. K. J., Voordouw, J. K., and Voordouw, G. (2000) Deletion of the hmc operon of Desulfovibrio vulgaris subsp vulgaris Hildenborough hampers hydrogen metabolism and low-redox-potential niche establishment, Arch. Microbiol. 174, 143-151.
    • (2000) Arch. Microbiol , vol.174 , pp. 143-151
    • Dolla, A.1    Pohorelic, B.K.J.2    Voordouw, J.K.3    Voordouw, G.4
  • 50
    • 17944386101 scopus 로고
    • Mutations affecting the cytochrome-d-containing oxidase complex of Escherichia coli K12: Identification and mapping of a 4th locus, cydD
    • Poole, R. K., Williams, H. D., Downie, J. A., and Gibson, F. (1989) Mutations affecting the cytochrome-d-containing oxidase complex of Escherichia coli K12: Identification and mapping of a 4th locus, cydD, J. Gen. Microbiol. 135, 1865-1874.
    • (1989) J. Gen. Microbiol , vol.135 , pp. 1865-1874
    • Poole, R.K.1    Williams, H.D.2    Downie, J.A.3    Gibson, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.