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Volumn 51, Issue 2, 2004, Pages 539-549

Molybdate transport and its effect on nitrogen utilization in the cyanobacterium Anabaena variabilis ATCC 29413

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; MOLYBDENUM; NITRATE REDUCTASE; NITROGEN; NITROGENASE;

EID: 0942301204     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03851.x     Document Type: Article
Times cited : (43)

References (63)
  • 1
    • 84984087585 scopus 로고
    • Simple conditions for the growth of unicellular blue-green algae on plates
    • Allen, M.M. (1968) Simple conditions for the growth of unicellular blue-green algae on plates. J Phycol 4: 1-4.
    • (1968) J Phycol , vol.4 , pp. 1-4
    • Allen, M.M.1
  • 2
    • 0000952381 scopus 로고
    • Studies on nitrogen-fixing blue-green algae. I. Growth and nitrogen fixation by Anabaena cylindrica Lemm
    • Allen, M.B., and Arnon, D.I. (1955) Studies on nitrogen-fixing blue-green algae. I. Growth and nitrogen fixation by Anabaena cylindrica Lemm. Plant Physiol (Bethesda) 30: 366-372.
    • (1955) Plant Physiol (Bethesda) , vol.30 , pp. 366-372
    • Allen, M.B.1    Arnon, D.I.2
  • 4
    • 0030917717 scopus 로고    scopus 로고
    • Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli
    • Anderson, L.A., Palmer, T., Price, N.C., Bornemann, S., Boxer, D.H., and Pau, R.N. (1997) Characterisation of the molybdenum-responsive ModE regulatory protein and its binding to the promoter region of the modABCD (molybdenum transport) operon of Escherichia coli. Eur J Biochem 246: 119-126.
    • (1997) Eur J Biochem , vol.246 , pp. 119-126
    • Anderson, L.A.1    Palmer, T.2    Price, N.C.3    Bornemann, S.4    Boxer, D.H.5    Pau, R.N.6
  • 5
    • 0034460301 scopus 로고    scopus 로고
    • ModE-dependent molybdate regulation of the molybdenum cofactor operon moa in Escherichia coli
    • Anderson, L.A., McNairn, E., Leubke, T., Pau, R.N., and Boxer, D.H. (2000) ModE-dependent molybdate regulation of the molybdenum cofactor operon moa in Escherichia coli. J Bacteriol 182: 7035-7043.
    • (2000) J Bacteriol , vol.182 , pp. 7035-7043
    • Anderson, L.A.1    McNairn, E.2    Leubke, T.3    Pau, R.N.4    Boxer, D.H.5
  • 6
    • 0002369684 scopus 로고
    • Alternative nitrogen fixation systems
    • Stacey, G., Burris, R.H., and Evans, H.J. (eds). New York: Chapman & Hall
    • Bishop, P.E., and Premakumar, R. (1992) Alternative nitrogen fixation systems. In Biological Nitrogen Fixation. Stacey, G., Burris, R.H., and Evans, H.J. (eds). New York: Chapman & Hall, pp. 736-762.
    • (1992) Biological Nitrogen Fixation , pp. 736-762
    • Bishop, P.E.1    Premakumar, R.2
  • 7
    • 0028179989 scopus 로고
    • - mutation in Anabaena sp. strain PCC 7120 implicates a secondary metabolite in the regulation of heterocyst spacing
    • - mutation in Anabaena sp. strain PCC 7120 implicates a secondary metabolite in the regulation of heterocyst spacing. J Bacteriol 176: 2282-2292.
    • (1994) J Bacteriol , vol.176 , pp. 2282-2292
    • Black, T.A.1    Wolk, C.P.2
  • 8
    • 0027210117 scopus 로고
    • Spatial expression and autoregulation of hetR, a gene involved in the control of heterocyst development in Anabaena
    • Black, T.A., Cai, Y., and Wolk, C.P. (1993) Spatial expression and autoregulation of hetR, a gene involved in the control of heterocyst development in Anabaena. Mol Microbiol 9: 873-880.
    • (1993) Mol Microbiol , vol.9 , pp. 873-880
    • Black, T.A.1    Cai, Y.2    Wolk, C.P.3
  • 9
    • 0024720297 scopus 로고
    • Excision of an 11-kilobase-pair DNA element from within the nifD gene in Anabaena variabilis heterocysts
    • Brusca, J.S., Hale, M.A., Carrasco, C.D., and Golden, J.W. (1989) Excision of an 11-kilobase-pair DNA element from within the nifD gene in Anabaena variabilis heterocysts. J Bacteriol 171: 4138-4145.
    • (1989) J Bacteriol , vol.171 , pp. 4138-4145
    • Brusca, J.S.1    Hale, M.A.2    Carrasco, C.D.3    Golden, J.W.4
  • 10
    • 0026087496 scopus 로고
    • Isolation and complementation of nitrogen fixing mutants of cyanobacterium Anabaena sp. strain PCC 7120
    • Buikema, W., and Haselkorn, R. (1991) Isolation and complementation of nitrogen fixing mutants of cyanobacterium Anabaena sp. strain PCC 7120. J Bacteriol 173: 1879-1885.
    • (1991) J Bacteriol , vol.173 , pp. 1879-1885
    • Buikema, W.1    Haselkorn, R.2
  • 11
    • 0031038156 scopus 로고    scopus 로고
    • Nitrogen deprivation of Anabaena sp. strain PCC 7120 elicits rapid activation of a gene cluster that is essential for uptake and utilization of nitrate
    • Cai, Y., and Wolk, C.P. (1997) Nitrogen deprivation of Anabaena sp. strain PCC 7120 elicits rapid activation of a gene cluster that is essential for uptake and utilization of nitrate. J Bacteriol 179: 258-266.
    • (1997) J Bacteriol , vol.179 , pp. 258-266
    • Cai, Y.1    Wolk, C.P.2
  • 12
    • 0018367683 scopus 로고
    • Characteristics of Anabaena variabilis influencing plaque formation by cyanophage N-1
    • Currier, T.C., and Wolk, C.P. (1979) Characteristics of Anabaena variabilis influencing plaque formation by cyanophage N-1. J Bacteriol 139: 88-92.
    • (1979) J Bacteriol , vol.139 , pp. 88-92
    • Currier, T.C.1    Wolk, C.P.2
  • 13
    • 0035906703 scopus 로고    scopus 로고
    • Two crystal structures of the cytoplasmic molybdate-binding protein ModG suggest a novel cooperative binding mechanism and provide insights into ligand-binding specificity
    • Delarbre, L., Stevenson, C.E., White, D.J., Mitchenall, L.A., Pau, R.N., and Lawson, D.M. (2001) Two crystal structures of the cytoplasmic molybdate-binding protein ModG suggest a novel cooperative binding mechanism and provide insights into ligand-binding specificity. J Mol Biol 308: 1063-1079.
    • (2001) J Mol Biol , vol.308 , pp. 1063-1079
    • Delarbre, L.1    Stevenson, C.E.2    White, D.J.3    Mitchenall, L.A.4    Pau, R.N.5    Lawson, D.M.6
  • 14
    • 0023754017 scopus 로고
    • A versatile class of positive-selection vectors based on the nonviability of palindrome-containing plasmids that allows cloning into long polylinkers
    • Elhai, J., and Wolk, C.P. (1988) A versatile class of positive-selection vectors based on the nonviability of palindrome-containing plasmids that allows cloning into long polylinkers. Gene 68: 119-138.
    • (1988) Gene , vol.68 , pp. 119-138
    • Elhai, J.1    Wolk, C.P.2
  • 15
    • 0025091237 scopus 로고
    • Developmental regulation and spatial pattern of expression of the structural genes for nitrogenase in the cyanobacterium Anabaena
    • Elhai, J., and Wolk, C.P. (1990) Developmental regulation and spatial pattern of expression of the structural genes for nitrogenase In the cyanobacterium Anabaena. EMBO J 9: 3379-3388.
    • (1990) EMBO J , vol.9 , pp. 3379-3388
    • Elhai, J.1    Wolk, C.P.2
  • 16
    • 0026445180 scopus 로고
    • Landscape geochemistry: Retrospect and prospect 1990
    • Fortescue, J.A.C. (1992) Landscape geochemistry: retrospect and prospect 1990. Appl Geochem 7: 1-53.
    • (1992) Appl Geochem , vol.7 , pp. 1-53
    • Fortescue, J.A.C.1
  • 17
    • 0036366682 scopus 로고    scopus 로고
    • Biosynthesis of the nitrogenase iron-molybdenum-cofactor from Azotobacter vinelandii
    • Frazzon, J., and Dean, D.R. (2002) Biosynthesis of the nitrogenase iron-molybdenum-cofactor from Azotobacter vinelandii. Metal Ions Biol Syst 39: 163-186.
    • (2002) Metal Ions Biol Syst , vol.39 , pp. 163-186
    • Frazzon, J.1    Dean, D.R.2
  • 18
    • 0031014647 scopus 로고    scopus 로고
    • Nitrate assimilation gene cluster from the heterocyst-formlng cyanobacterium Anabaena sp. strain PCC 7120
    • Frias, J.E., Flores, E., and Herrero, A. (1997) Nitrate assimilation gene cluster from the heterocyst-formlng cyanobacterium Anabaena sp. strain PCC 7120. J Bacteriol 179: 477-486.
    • (1997) J Bacteriol , vol.179 , pp. 477-486
    • Frias, J.E.1    Flores, E.2    Herrero, A.3
  • 19
    • 0023957783 scopus 로고
    • Changes in sulfate transport characteristics and protein composition of Anacystis nidulans R2 during sulfur deprivation
    • Green, L.S., and Grossman, A.R. (1988) Changes in sulfate transport characteristics and protein composition of Anacystis nidulans R2 during sulfur deprivation. J Bacteriol 170: 583-587.
    • (1988) J Bacteriol , vol.170 , pp. 583-587
    • Green, L.S.1    Grossman, A.R.2
  • 20
    • 0030726129 scopus 로고    scopus 로고
    • Molybdate transport and regulation in bacteria
    • Grunden, A.M., and Shanmugam, K.T. (1997) Molybdate transport and regulation in bacteria. Arch Microbiol 168: 345-354.
    • (1997) Arch Microbiol , vol.168 , pp. 345-354
    • Grunden, A.M.1    Shanmugam, K.T.2
  • 21
    • 0030028140 scopus 로고    scopus 로고
    • Repression of the Escherichia coli modABCD (molybdate transport) operon by ModE
    • Grunden, A.M., Ray, R.M., Rosentel, J.K., Healy, F.G., and Shanmugam, K.T. (1996) Repression of the Escherichia coli modABCD (molybdate transport) operon by ModE. J Bacteriol 178: 735-744.
    • (1996) J Bacteriol , vol.178 , pp. 735-744
    • Grunden, A.M.1    Ray, R.M.2    Rosentel, J.K.3    Healy, F.G.4    Shanmugam, K.T.5
  • 22
    • 0033588028 scopus 로고    scopus 로고
    • An analysis of the binding of repressor protein ModE to modABCD (molybdate transport) operator/promoter DNA of Escherichia coli
    • Grunden, A.M., Self, W.T., Villain, M., Blalock, J.E., and Shanmugan, K.T. (1999) An analysis of the binding of repressor protein ModE to modABCD (molybdate transport) operator/promoter DNA of Escherichia coli. J Biol Chem 274: 24308-24315.
    • (1999) J Biol Chem , vol.274 , pp. 24308-24315
    • Grunden, A.M.1    Self, W.T.2    Villain, M.3    Blalock, J.E.4    Shanmugan, K.T.5
  • 23
    • 0001787027 scopus 로고    scopus 로고
    • Molecular modelling of proteins
    • Guex, N., and Peitsch, M.C. (1999) Molecular modelling of proteins. Immunol News 6: 132-134.
    • (1999) Immunol News , vol.6 , pp. 132-134
    • Guex, N.1    Peitsch, M.C.2
  • 24
    • 0000273676 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille, R. (1996) The mononuclear molybdenum enzymes. Chem Rev 96: 2757-2816.
    • (1996) Chem Rev , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 25
    • 0036629252 scopus 로고    scopus 로고
    • Molybdenum and tungsten in biology
    • Hille, R. (2002) Molybdenum and tungsten in biology. Trends Biochem Sci 27: 360-367.
    • (2002) Trends Biochem Sci , vol.27 , pp. 360-367
    • Hille, R.1
  • 26
    • 0031228463 scopus 로고    scopus 로고
    • Crystal structure of the molybdate binding protein ModA
    • Hu, Y., Rech, S., Gunsalus, R.P., and Rees, D.C. (1997) Crystal structure of the molybdate binding protein ModA. Nature Struct Biol 4: 703-707.
    • (1997) Nature Struct Biol , vol.4 , pp. 703-707
    • Hu, Y.1    Rech, S.2    Gunsalus, R.P.3    Rees, D.C.4
  • 27
    • 0025228504 scopus 로고
    • Molybdopterin guanine dinucleotide: A modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans
    • Johnson, J.L., Bastian, N.R., and Rajagopalan, K.V. (1990) Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans. Proc Natl Acad Sci USA 87: 3190-3194.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3190-3194
    • Johnson, J.L.1    Bastian, N.R.2    Rajagopalan, K.V.3
  • 28
    • 0030606607 scopus 로고    scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions
    • Kaneko, T., Sato, S., Kotani, H., Tanaka, A., Asamizu, E., Nakamura, Y., et al. (1996) Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions. DNA Res 3: 109-136.
    • (1996) DNA Res , vol.3 , pp. 109-136
    • Kaneko, T.1    Sato, S.2    Kotani, H.3    Tanaka, A.4    Asamizu, E.5    Nakamura, Y.6
  • 29
    • 0035980822 scopus 로고    scopus 로고
    • Complete genomic se-quence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120
    • Kaneko, T., Nakamura, Y., Wolk, C.P., Kuritz, T., Sasamoto, S., Watanabe, A., et al. (2001) Complete genomic se-quence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120. DNA Res 8: 205-213.
    • (2001) DNA Res , vol.8 , pp. 205-213
    • Kaneko, T.1    Nakamura, Y.2    Wolk, C.P.3    Kuritz, T.4    Sasamoto, S.5    Watanabe, A.6
  • 30
    • 0025793667 scopus 로고
    • Characterization and mutagenesis of sulfur-regulated genes in a cyanobacterium: Evidence for function in sulfate transport
    • Laudenbach, D.E., and Grossman, A.R. (1991) Characterization and mutagenesis of sulfur-regulated genes in a cyanobacterium: evidence for function in sulfate transport. J Bacteriol 173: 2739-2750.
    • (1991) J Bacteriol , vol.173 , pp. 2739-2750
    • Laudenbach, D.E.1    Grossman, A.R.2
  • 31
    • 0036364863 scopus 로고    scopus 로고
    • Molybdenum nitrogenases: A crystallographic and mechanistic view
    • Lawson, D.M., and Smith, B.E. (2002) Molybdenum nitrogenases: a crystallographic and mechanistic view. Metal Ions Biol Syst 39: 75-119.
    • (2002) Metal Ions Biol Syst , vol.39 , pp. 75-119
    • Lawson, D.M.1    Smith, B.E.2
  • 32
    • 0032534765 scopus 로고    scopus 로고
    • Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: The 1.2 A resolution crystal structure of Azotobacter vinelandii ModA
    • Lawson, D.M., Williams, C.E., Mitchenall, L.A., and Pau, R.N. (1998) Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA. Structure 6: 1529-1539.
    • (1998) Structure , vol.6 , pp. 1529-1539
    • Lawson, D.M.1    Williams, C.E.2    Mitchenall, L.A.3    Pau, R.N.4
  • 33
    • 0027467467 scopus 로고
    • Characterization of genes involved in molybdenum transport in Azotobacter vinelandii
    • Luque, F., Mitchenall, L.A., Chapman, M., Christine, R., and Pau, R.N. (1993) Characterization of genes involved in molybdenum transport in Azotobacter vinelandii. Mol Microbiol 7: 447-459.
    • (1993) Mol Microbiol , vol.7 , pp. 447-459
    • Luque, F.1    Mitchenall, L.A.2    Chapman, M.3    Christine, R.4    Pau, R.N.5
  • 34
    • 0028967177 scopus 로고
    • Characterization of nifB, nifS, and nifU genes in the cyanobacterium Anabaena variabilis - NifB is required for the vanadium-dependent nitrogenase
    • Lyons, E.M., and Thiel, T. (1995) Characterization of nifB, nifS, and nifU genes in the cyanobacterium Anabaena variabilis - NifB is required for the vanadium-dependent nitrogenase. J Bacteriol 177: 1570-1575.
    • (1995) J Bacteriol , vol.177 , pp. 1570-1575
    • Lyons, E.M.1    Thiel, T.2
  • 35
    • 0000411157 scopus 로고
    • Absorption of light by chlorophyll solutions
    • Mackinney, G. (1941) Absorption of light by chlorophyll solutions. J Biol Chem 140: 315-322.
    • (1941) J Biol Chem , vol.140 , pp. 315-322
    • Mackinney, G.1
  • 37
    • 0029116786 scopus 로고
    • Mutational analysis of genes of the mod locus involved in molybdenum transport, homeostasis, and processing in Azotobacter vinelandii
    • Mouncey, N.J., Mitchenall, L.A., and Pau, R.N. (1995) Mutational analysis of genes of the mod locus involved in molybdenum transport, homeostasis, and processing in Azotobacter vinelandii. J Bacteriol 177: 5294-5302.
    • (1995) J Bacteriol , vol.177 , pp. 5294-5302
    • Mouncey, N.J.1    Mitchenall, L.A.2    Pau, R.N.3
  • 38
    • 0029824740 scopus 로고    scopus 로고
    • The modE gene product mediates molybdenum-dependent expression of genes for the high-affinity molybdate transporter and modG in Azotobacter vinelandii
    • Mouncey, N.J., Mitchenall, L.A., and Pau, R.N. (1996) The modE gene product mediates molybdenum-dependent expression of genes for the high-affinity molybdate transporter and modG in Azotobacter vinelandii. Microbiology 142: 1997-2004.
    • (1996) Microbiology , vol.142 , pp. 1997-2004
    • Mouncey, N.J.1    Mitchenall, L.A.2    Pau, R.N.3
  • 39
    • 0036363905 scopus 로고    scopus 로고
    • Transport, homeostasis, regulation, and binding of molybdate and tungstate to proteins
    • Pau, R.N., and Lawson, D.M. (2002) Transport, homeostasis, regulation, and binding of molybdate and tungstate to proteins. Metal Ions Biol Syst 39: 31-74.
    • (2002) Metal Ions Biol Syst , vol.39 , pp. 31-74
    • Pau, R.N.1    Lawson, D.M.2
  • 40
    • 0002625517 scopus 로고    scopus 로고
    • Molybdenum transport, processing and gene regulation
    • Winkelmann, G., and Carrano, C.J. (eds). Newark, NJ: Harwood Academic Publishers
    • Pau, R.N., Klipp, W., and Leimkuhler, S. (1997) Molybdenum transport, processing and gene regulation. In Transition Metals in Microbial Metabolism. Winkelmann, G., and Carrano, C.J. (eds). Newark, NJ: Harwood Academic Publishers, pp. 217-234.
    • (1997) Transition Metals in Microbial Metabolism , pp. 217-234
    • Pau, R.N.1    Klipp, W.2    Leimkuhler, S.3
  • 41
    • 0030066554 scopus 로고    scopus 로고
    • Phenotypic characterization of a tungsten-tolerant mutant of Azotobacter vinelandii
    • Premakumar, R., Jacobitz, S., Ricke, S.C., and Bishop, P.E. (1996) Phenotypic characterization of a tungsten-tolerant mutant of Azotobacter vinelandii. J Bacteriol 178: 691-696.
    • (1996) J Bacteriol , vol.178 , pp. 691-696
    • Premakumar, R.1    Jacobitz, S.2    Ricke, S.C.3    Bishop, P.E.4
  • 42
    • 0030868420 scopus 로고    scopus 로고
    • Biosynthesis and processing of the molybdenum cofactors
    • Rajagopalan, K.V. (1997) Biosynthesis and processing of the molybdenum cofactors. Biochem Soc Trans 25: 757-761.
    • (1997) Biochem Soc Trans , vol.25 , pp. 757-761
    • Rajagopalan, K.V.1
  • 43
    • 0029884299 scopus 로고    scopus 로고
    • Nitrate reductase activity and heterocyst suppression on nitrate in Anabaena sp. strain PCC 7120 require moeA
    • Ramaswamy, K.S., Endley, S., and Golden, J.W. (1996) Nitrate reductase activity and heterocyst suppression on nitrate in Anabaena sp. strain PCC 7120 require moeA. J Bacteriol 178: 3893-3898.
    • (1996) J Bacteriol , vol.178 , pp. 3893-3898
    • Ramaswamy, K.S.1    Endley, S.2    Golden, J.W.3
  • 44
    • 0035844146 scopus 로고    scopus 로고
    • 55Fe-labeled precursors of the iron-molybdenum cofactor of nitrogenase on NifH and NifX of Azotobacter vinelandii
    • 55Fe-labeled precursors of the iron-molybdenum cofactor of nitrogenase on NifH and NifX of Azotobacter vinelandii. J Biol Chem 276: 15968-15974.
    • (2001) J Biol Chem , vol.276 , pp. 15968-15974
    • Rangaraj, P.1    Rüttimann-Johnson, C.2    Shah, V.K.3    Ludden, P.W.4
  • 45
    • 0028851284 scopus 로고
    • Regulation of the molybdate transport operon, modABCD, of Escherichia coli in response to molybdate availability
    • Rech, S., Deppenmeier, U., and Gunsalus, R.P. (1995) Regulation of the molybdate transport operon, modABCD, of Escherichia coli in response to molybdate availability. J Bacteriol 177: 1023-1029.
    • (1995) J Bacteriol , vol.177 , pp. 1023-1029
    • Rech, S.1    Deppenmeier, U.2    Gunsalus, R.P.3
  • 46
    • 0030023719 scopus 로고    scopus 로고
    • Properties of the periplasmic ModA molybdate-binding protein of Escherichia coli
    • Rech, S., Wolin, C., and Gunsalus, R.P. (1996) Properties of the periplasmic ModA molybdate-binding protein of Escherichia coli. J Biol Chem 271: 2557-2562.
    • (1996) J Biol Chem , vol.271 , pp. 2557-2562
    • Rech, S.1    Wolin, C.2    Gunsalus, R.P.3
  • 47
    • 0029117622 scopus 로고
    • Molybdate and regulation of mod (molybdate transport), fdhF, and hyc (formate hydrogenlyase) operons in Escherichia coli
    • Rosentel, J.K., Healy, F., Maupin-Furlow, J.A., Lee, J.H., and Shanmugam, K.T. (1995) Molybdate and regulation of mod (molybdate transport), fdhF, and hyc (formate hydrogenlyase) operons in Escherichia coli. J Bacteriol 177: 4857-4864.
    • (1995) J Bacteriol , vol.177 , pp. 4857-4864
    • Rosentel, J.K.1    Healy, F.2    Maupin-Furlow, J.A.3    Lee, J.H.4    Shanmugam, K.T.5
  • 48
    • 0031910877 scopus 로고    scopus 로고
    • The narA Locus of Synechococcus sp. strain PCC 7942 consists of a cluster of molybdopterin biosynthesis genes
    • Rubio, L.M., Flores, E., and Herrero, A. (1998) The narA Locus of Synechococcus sp. strain PCC 7942 consists of a cluster of molybdopterin biosynthesis genes. J Bacteriol 180: 1200-1206.
    • (1998) J Bacteriol , vol.180 , pp. 1200-1206
    • Rubio, L.M.1    Flores, E.2    Herrero, A.3
  • 51
    • 0042622380 scopus 로고    scopus 로고
    • Swiss-model: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M.C. (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31: 3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 53
    • 0032947995 scopus 로고    scopus 로고
    • Requirement of NifX and other nif proteins for in vitro biosynthesis of the iron-molybdenum cofactor of nitrogenase
    • Shah, V.K., Rangaraj, P., Chatterjee, R., Allen, J.R., Roll, J.T., Roberts, G.P., and Ludden, P.W. (1999) Requirement of NifX and other nif proteins for in vitro biosynthesis of the iron-molybdenum cofactor of nitrogenase. J Bacteriol 181: 2797-2801.
    • (1999) J Bacteriol , vol.181 , pp. 2797-2801
    • Shah, V.K.1    Rangaraj, P.2    Chatterjee, R.3    Allen, J.R.4    Roll, J.T.5    Roberts, G.P.6    Ludden, P.W.7
  • 54
    • 0027495919 scopus 로고
    • Characterization of genes for an alternative nitrogenase in the cyanobacterium Anabaena variabilis
    • Thiel, T. (1993) Characterization of genes for an alternative nitrogenase in the cyanobacterium Anabaena variabilis. J Bacteriol 175: 6276-6286.
    • (1993) J Bacteriol , vol.175 , pp. 6276-6286
    • Thiel, T.1
  • 55
    • 0024742399 scopus 로고
    • Optimum conditions for growth of cyanobacteria on solid media
    • Thiel, T., Bramble, J., and Roger, S. (1989) Optimum conditions for growth of cyanobacteria on solid media. FEMS Microbiol Lett 61: 27-32.
    • (1989) FEMS Microbiol Lett , vol.61 , pp. 27-32
    • Thiel, T.1    Bramble, J.2    Roger, S.3
  • 56
    • 0029049235 scopus 로고
    • A second nitrogenase in vegetative cells of a heterocyst-forming cyanobacterium
    • Thiel, T., Lyons, E.M., Erker, J.C., and Ernst, A. (1995) A second nitrogenase in vegetative cells of a heterocyst-forming cyanobacterium. Proc Natl Acad Sci USA 92: 9358-9362.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 9358-9362
    • Thiel, T.1    Lyons, E.M.2    Erker, J.C.3    Ernst, A.4
  • 57
    • 0030746391 scopus 로고    scopus 로고
    • Characterization of genes for a second molybdate dependent nitrogenase in the cyanobacterium Anabaena variabilis
    • Thiel, T., Lyons, E.M., and Erker, J.C. (1997) Characterization of genes for a second molybdate dependent nitrogenase in the cyanobacterium Anabaena variabilis. J Bacteriol 179: 5222-5225.
    • (1997) J Bacteriol , vol.179 , pp. 5222-5225
    • Thiel, T.1    Lyons, E.M.2    Erker, J.C.3
  • 58
    • 0037213708 scopus 로고    scopus 로고
    • Transport of molybdate in the cyanobacterium Anabaena variabilis ATCC 29413
    • Thiel, T., Pratte, B., and Zahalak, M. (2002) Transport of molybdate in the cyanobacterium Anabaena variabilis ATCC 29413. Arch Microbiol 179: 50-56.
    • (2002) Arch Microbiol , vol.179 , pp. 50-56
    • Thiel, T.1    Pratte, B.2    Zahalak, M.3
  • 59
    • 0027053219 scopus 로고
    • Analysis of the gene encoding the RNA subunit of ribonuclease P from cyanobacteria
    • Vioque, A. (1992) Analysis of the gene encoding the RNA subunit of ribonuclease P from cyanobacteria. Nucleic Acids Res 20: 6331-6337.
    • (1992) Nucleic Acids Res , vol.20 , pp. 6331-6337
    • Vioque, A.1
  • 60
    • 0034435588 scopus 로고    scopus 로고
    • Structure of the molybdate/tungstate binding protein mop from Sporomusa ovata
    • Wagner, U.G., Stupperich, E., and Kratky, C. (2000) Structure of the molybdate/tungstate binding protein mop from Sporomusa ovata. Structure Fold Des 8: 1127-1136.
    • (2000) Structure Fold des , vol.8 , pp. 1127-1136
    • Wagner, U.G.1    Stupperich, E.2    Kratky, C.3
  • 61
    • 0027175827 scopus 로고
    • Characterization of Rhodobacter capsulatus genes encoding a molybdenum transport system and putative molybdenumpterin-binding proteins
    • Wang, G., Angermüller, S., and Klipp, W. (1993) Characterization of Rhodobacter capsulatus genes encoding a molybdenum transport system and putative molybdenumpterin-binding proteins. J Bacteriol 175: 3031-3042.
    • (1993) J Bacteriol , vol.175 , pp. 3031-3042
    • Wang, G.1    Angermüller, S.2    Klipp, W.3
  • 62
    • 0030458712 scopus 로고    scopus 로고
    • Heterocyst formation
    • Wolk, C.P. (1996) Heterocyst formation. Annu Rev Genet 30: 59-78.
    • (1996) Annu Rev Genet , vol.30 , pp. 59-78
    • Wolk, C.P.1
  • 63
    • 0000368322 scopus 로고
    • Heterocyst metabolism and development
    • Bryant, D. (ed.). Dordrecht, The Netherlands: Kluwer Academic Publishers
    • Wolk, C.P., Ernst, A., and Elhai, J. (1994) Heterocyst metabolism and development. In Molecular Genetics of Cyanobacteria. Bryant, D. (ed.). Dordrecht, The Netherlands: Kluwer Academic Publishers, pp. 769-823.
    • (1994) Molecular Genetics of Cyanobacteria , pp. 769-823
    • Wolk, C.P.1    Ernst, A.2    Elhai, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.