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Volumn 15, Issue 1, 2016, Pages

Using synthetic biology to increase nitrogenase activity

Author keywords

Electron transporter; Fe S cluster assembly; Nitrogenase; Paenibacillus

Indexed keywords

NITROGENASE; PROTEIN KINASE FER; IRON SULFUR PROTEIN;

EID: 84958280118     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/s12934-016-0442-6     Document Type: Article
Times cited : (60)

References (38)
  • 1
    • 50149115452 scopus 로고    scopus 로고
    • Biosynthesis of the iron-molybdenum cofactor of nitrogenase
    • Rubio LM, Ludden PW. Biosynthesis of the iron-molybdenum cofactor of nitrogenase. Annu Rev Microbiol. 2008;62:93-111.
    • (2008) Annu Rev Microbiol , vol.62 , pp. 93-111
    • Rubio, L.M.1    Ludden, P.W.2
  • 2
    • 79952746316 scopus 로고    scopus 로고
    • Biosynthesis of Nitrogenase FeMoco
    • Hu Y, Ribbe MW. Biosynthesis of Nitrogenase FeMoco. Coord Chem Rev. 2011;255:1218-24.
    • (2011) Coord Chem Rev , vol.255 , pp. 1218-1224
    • Hu, Y.1    Ribbe, M.W.2
  • 3
    • 0018167549 scopus 로고
    • Regulation and characterization of protein products coded by the nif (nitrogen fixation) genes of Klebsiella pneumoniae
    • Roberts GP, MacNeil T, MacNeil D, Brill WJ. Regulation and characterization of protein products coded by the nif (nitrogen fixation) genes of Klebsiella pneumoniae. J Bacteriol. 1979;136:267-79.
    • (1979) J Bacteriol , vol.136 , pp. 267-279
    • Roberts, G.P.1    MacNeil, T.2    MacNeil, D.3    Brill, W.J.4
  • 4
    • 0023701258 scopus 로고
    • Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire nitrogen fixation gene cluster of Klebsiella pneumoniae
    • Arnold W, Rump A, Klipp W, Priefer UB, Puhler A. Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire nitrogen fixation gene cluster of Klebsiella pneumoniae. J Mol Biol. 1988;203:715-38.
    • (1988) J Mol Biol , vol.203 , pp. 715-738
    • Arnold, W.1    Rump, A.2    Klipp, W.3    Priefer, U.B.4    Puhler, A.5
  • 6
    • 84860375761 scopus 로고    scopus 로고
    • Distribution of nitrogen fixation and nitrogenase-like sequences amongst microbial genomes
    • Dos SP, Fang Z, Mason SW, Setubal JC, Dixon R. Distribution of nitrogen fixation and nitrogenase-like sequences amongst microbial genomes. BMC Genom. 2012;13:162.
    • (2012) BMC Genom , vol.13 , pp. 162
    • Dos, S.P.1    Fang, Z.2    Mason, S.W.3    Setubal, J.C.4    Dixon, R.5
  • 7
    • 70349319658 scopus 로고    scopus 로고
    • Establishing nitrogen-fixing symbiosis with legumes: how many rhizobium recipes?
    • Masson-Boivin C, Giraud E, Perret X, Batut J. Establishing nitrogen-fixing symbiosis with legumes: how many rhizobium recipes? Trends Microbiol. 2009;17:458-66.
    • (2009) Trends Microbiol , vol.17 , pp. 458-466
    • Masson-Boivin, C.1    Giraud, E.2    Perret, X.3    Batut, J.4
  • 9
    • 84887277583 scopus 로고    scopus 로고
    • A minimal nitrogen fixation gene cluster from Paenibacillus sp. WLY78 enables expression of active nitrogenase in Escherichia coli
    • Wang L, Zhang L, Liu Z, Zhao D, Liu X, Zhang B, Xie J, Hong Y, Li P, Chen S, Dixon R, Li J. A minimal nitrogen fixation gene cluster from Paenibacillus sp. WLY78 enables expression of active nitrogenase in Escherichia coli. PLoS Genet. 2013;9:e1003865.
    • (2013) PLoS Genet , vol.9
    • Wang, L.1    Zhang, L.2    Liu, Z.3    Zhao, D.4    Liu, X.5    Zhang, B.6    Xie, J.7    Hong, Y.8    Li, P.9    Chen, S.10    Dixon, R.11    Li, J.12
  • 11
    • 0030694763 scopus 로고    scopus 로고
    • Nif gene transfer and expression in chloroplasts: prospects and problems.
    • Netherlands: Springer
    • Dixon R, Cheng Q, Shen GF, Day A, Dowson-Day M. Nif gene transfer and expression in chloroplasts: prospects and problems. Netherlands: Springer; 1997. p. 193-203.
    • (1997) , pp. 193-203
    • Dixon, R.1    Cheng, Q.2    Shen, G.F.3    Day, A.4    Dowson-Day, M.5
  • 12
    • 0015503824 scopus 로고
    • Genetic transfer of nitrogen fixation from Klebsiella pneumoniae to Escherichia coli
    • Dixon RA, Postgate JR. Genetic transfer of nitrogen fixation from Klebsiella pneumoniae to Escherichia coli. Nature. 1972;237:102-3.
    • (1972) Nature , vol.237 , pp. 102-103
    • Dixon, R.A.1    Postgate, J.R.2
  • 13
    • 84860803588 scopus 로고    scopus 로고
    • Refactoring the nitrogen fixation gene cluster from Klebsiella oxytoca
    • Temme K, Zhao D, Voigt CA. Refactoring the nitrogen fixation gene cluster from Klebsiella oxytoca. Proc Natl Acad Sci. 2012;109:7085-90.
    • (2012) Proc Natl Acad Sci , vol.109 , pp. 7085-7090
    • Temme, K.1    Zhao, D.2    Voigt, C.A.3
  • 15
    • 84880795286 scopus 로고    scopus 로고
    • Using synthetic biology to distinguish and overcome regulatory and functional barriers related to nitrogen fixation
    • Wang X, Yang JG, Chen L, Wang JL, Cheng Q, Dixon R, Wang YP. Using synthetic biology to distinguish and overcome regulatory and functional barriers related to nitrogen fixation. PLoS One. 2013;8:e68677.
    • (2013) PLoS One , vol.8
    • Wang, X.1    Yang, J.G.2    Chen, L.3    Wang, J.L.4    Cheng, Q.5    Dixon, R.6    Wang, Y.P.7
  • 16
    • 84996335527 scopus 로고
    • New shuttle vectors for Escherichia coli and Bacillus subtilis. IV. The nucleotide sequence of pHY300PLK and some properties in relation to transformation
    • Ishiwa H, Shibahara H. New shuttle vectors for Escherichia coli and Bacillus subtilis. IV. The nucleotide sequence of pHY300PLK and some properties in relation to transformation. Jpn J Genet. 1986;61:515-28.
    • (1986) Jpn J Genet , vol.61 , pp. 515-528
    • Ishiwa, H.1    Shibahara, H.2
  • 17
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson DC, Dean DR, Smith AD, Johnson MK. Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem. 2005;74:247-81.
    • (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
  • 18
    • 4344704870 scopus 로고    scopus 로고
    • Genetic regulation of biological nitrogen fixation
    • Dixon R, Kahn D. Genetic regulation of biological nitrogen fixation. Nat Rev Microbiol. 2004;2:621-31.
    • (2004) Nat Rev Microbiol , vol.2 , pp. 621-631
    • Dixon, R.1    Kahn, D.2
  • 20
    • 0018849720 scopus 로고
    • Roles of nifF and nifJ gene products in electron transport to nitrogenase in Klebsiella pneumoniae
    • Hill S, Kavanagh EP. Roles of nifF and nifJ gene products in electron transport to nitrogenase in Klebsiella pneumoniae. J Bacteriol. 1980;141:470-5.
    • (1980) J Bacteriol , vol.141 , pp. 470-475
    • Hill, S.1    Kavanagh, E.P.2
  • 21
    • 0343509967 scopus 로고
    • Energetics and sources of energy for biological nitrogen fixation
    • Ludden PW. Energetics and sources of energy for biological nitrogen fixation. Curr Topics Bioenerg. 1991;16:369-90.
    • (1991) Curr Topics Bioenerg , vol.16 , pp. 369-390
    • Ludden, P.W.1
  • 22
    • 12644263291 scopus 로고
    • Electron-transport systems coupled to nitrogenase
    • New York: Wiley
    • Yoch DC. Electron-transport systems coupled to nitrogenase. A treatise on dinitrogen fixation. New York: Wiley; 1979. p. 605-52.
    • (1979) A treatise on dinitrogen fixation , pp. 605-652
    • Yoch, D.C.1
  • 23
    • 0022410283 scopus 로고
    • Electron transfer to nitrogenase in Klebsiella pneumoniae. nifF gene cloned and the gene product, a flavodoxin, purified
    • Deistung J, Cannon FC, Cannon MC, Hill S, Thorneley RN. Electron transfer to nitrogenase in Klebsiella pneumoniae. nifF gene cloned and the gene product, a flavodoxin, purified. Biochem J. 1985;231:743-53.
    • (1985) Biochem J , vol.231 , pp. 743-753
    • Deistung, J.1    Cannon, F.C.2    Cannon, M.C.3    Hill, S.4    Thorneley, R.N.5
  • 24
    • 0018167549 scopus 로고
    • Regulation and characterization of protein products coded by the nif (nitrogen fixation) genes of Klebsiella pneumoniae
    • Roberts GP, MacNeil T, MacNeil D, Brill WJ. Regulation and characterization of protein products coded by the nif (nitrogen fixation) genes of Klebsiella pneumoniae. J Bacteriol. 1978;136:267-79.
    • (1978) J Bacteriol , vol.136 , pp. 267-279
    • Roberts, G.P.1    MacNeil, T.2    MacNeil, D.3    Brill, W.J.4
  • 25
    • 0018171975 scopus 로고
    • Fine-structure mapping and complementation analysis of nif (nitrogen fixation) genes in Klebsiella pneumoniae
    • MacNeil T, MacNeil D, Roberts GP, Supiano MA, Brill WJ. Fine-structure mapping and complementation analysis of nif (nitrogen fixation) genes in Klebsiella pneumoniae. J Bacteriol. 1978;136:253-66.
    • (1978) J Bacteriol , vol.136 , pp. 253-266
    • MacNeil, T.1    MacNeil, D.2    Roberts, G.P.3    Supiano, M.A.4    Brill, W.J.5
  • 26
    • 33748648580 scopus 로고    scopus 로고
    • Peptidyl-prolyl cis/trans isomerase-independent functional NifH mutant of Azotobacter vinelandii
    • Gavini N, Tungtur S, Pulakat L. Peptidyl-prolyl cis/trans isomerase-independent functional NifH mutant of Azotobacter vinelandii. J Bacteriol. 2006;188:6020-5.
    • (2006) J Bacteriol , vol.188 , pp. 6020-6025
    • Gavini, N.1    Tungtur, S.2    Pulakat, L.3
  • 27
    • 0030739401 scopus 로고    scopus 로고
    • Transcriptional regulation of a second flavodoxin gene from Klebsiella pneumoniae
    • Achenbach LA, Genova EG. Transcriptional regulation of a second flavodoxin gene from Klebsiella pneumoniae. Gene. 1997;194:235-40.
    • (1997) Gene , vol.194 , pp. 235-240
    • Achenbach, L.A.1    Genova, E.G.2
  • 28
    • 84937605477 scopus 로고    scopus 로고
    • Design and improvement of artificial redox modules by molecular fusion of flavodoxin and flavodoxin reductase from Escherichia coli
    • Bakkes PJ, Biemann S, Bokel A, Eickholt M, Girhard M, Urlacher VB. Design and improvement of artificial redox modules by molecular fusion of flavodoxin and flavodoxin reductase from Escherichia coli. Sci Rep. 2015;5:12158.
    • (2015) Sci Rep , vol.5 , pp. 12158
    • Bakkes, P.J.1    Biemann, S.2    Bokel, A.3    Eickholt, M.4    Girhard, M.5    Urlacher, V.B.6
  • 29
    • 0020064853 scopus 로고
    • Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate: flavodoxin and NADPH: flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase
    • Blaschkowski HP, Neuer G, Ludwig-Festl M, Knappe J. Routes of flavodoxin and ferredoxin reduction in Escherichia coli. CoA-acylating pyruvate: flavodoxin and NADPH: flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase. Eur J Biochem. 1982;123:563-9.
    • (1982) Eur J Biochem , vol.123 , pp. 563-569
    • Blaschkowski, H.P.1    Neuer, G.2    Ludwig-Festl, M.3    Knappe, J.4
  • 30
    • 0027453074 scopus 로고
    • Escherichia coli ferredoxin NADP + reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), and overexpression of the protein
    • Bianchi V, Reichard P, Eliasson R, Pontis E, Krook M, Jornvall H, Haggard-Ljungquist E. Escherichia coli ferredoxin NADP + reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), and overexpression of the protein. J Bacteriol. 1993;175:1590-5.
    • (1993) J Bacteriol , vol.175 , pp. 1590-1595
    • Bianchi, V.1    Reichard, P.2    Eliasson, R.3    Pontis, E.4    Krook, M.5    Jornvall, H.6    Haggard-Ljungquist, E.7
  • 31
    • 0032211496 scopus 로고    scopus 로고
    • Characterisation of flavodoxin NADP + oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli
    • McIver L, Leadbeater C, Campopiano DJ, Baxter RL, Daff SN, Chapman SK, Munro AW. Characterisation of flavodoxin NADP + oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli. Eur J Biochem. 1998;257:577-85.
    • (1998) Eur J Biochem , vol.257 , pp. 577-585
    • McIver, L.1    Leadbeater, C.2    Campopiano, D.J.3    Baxter, R.L.4    Daff, S.N.5    Chapman, S.K.6    Munro, A.W.7
  • 32
    • 31144457521 scopus 로고    scopus 로고
    • Molecular evolution of the nif gene cluster carrying nifI1 and nifI2 genes in the Gram-positive phototrophic bacterium Heliobacterium chlorum
    • Enkh-Amgalan J, Kawasaki H, Seki T. Molecular evolution of the nif gene cluster carrying nifI1 and nifI2 genes in the Gram-positive phototrophic bacterium Heliobacterium chlorum. Int J Syst Evol Microbiol. 2006;56:65-74.
    • (2006) Int J Syst Evol Microbiol , vol.56 , pp. 65-74
    • Enkh-Amgalan, J.1    Kawasaki, H.2    Seki, T.3
  • 33
    • 0022607892 scopus 로고
    • Klebsiella pneumoniae nifM gene product is required for stabilization and activation of nitrogenase iron protein in Escherichia coli
    • Howard KS, McLean PA, Hansen FB, Lemley PV, Koblan KS, Orme-Johnson WH. Klebsiella pneumoniae nifM gene product is required for stabilization and activation of nitrogenase iron protein in Escherichia coli. J Biol Chem. 1986;261:772-8.
    • (1986) J Biol Chem , vol.261 , pp. 772-778
    • Howard, K.S.1    McLean, P.A.2    Hansen, F.B.3    Lemley, P.V.4    Koblan, K.S.5    Orme-Johnson, W.H.6
  • 34
    • 0021183145 scopus 로고
    • Role of the nifQ gene product in the incorporation of molybdenum into nitrogenase in Klebsiella pneumoniae
    • Imperial J, Ugalde RA, Shah VK, Brill WJ. Role of the nifQ gene product in the incorporation of molybdenum into nitrogenase in Klebsiella pneumoniae. J Bacteriol. 1984;158:187-94.
    • (1984) J Bacteriol , vol.158 , pp. 187-194
    • Imperial, J.1    Ugalde, R.A.2    Shah, V.K.3    Brill, W.J.4
  • 35
    • 84857063536 scopus 로고    scopus 로고
    • Organization of nif gene cluster in Frankia sp. EuIK1 strain, a symbiont of Elaeagnus umbellata
    • Oh CJ, Kim HB, Kim J, Kim WJ, Lee H, An CS. Organization of nif gene cluster in Frankia sp. EuIK1 strain, a symbiont of Elaeagnus umbellata. Arch Microbiol. 2012;194:29-34.
    • (2012) Arch Microbiol , vol.194 , pp. 29-34
    • Oh, C.J.1    Kim, H.B.2    Kim, J.3    Kim, W.J.4    Lee, H.5    An, C.S.6
  • 37
    • 0035891318 scopus 로고    scopus 로고
    • Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
    • Lake MW, Wuebbens MM, Rajagopalan KV, Schindelin H. Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature. 2001;414:325-9.
    • (2001) Nature , vol.414 , pp. 325-329
    • Lake, M.W.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 38
    • 30144434909 scopus 로고    scopus 로고
    • Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis
    • Lehmann C, Begley TP, Ealick SE. Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis. Biochemistry. 2006;45:11-9.
    • (2006) Biochemistry , vol.45 , pp. 11-19
    • Lehmann, C.1    Begley, T.P.2    Ealick, S.E.3


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