메뉴 건너뛰기




Volumn 28, Issue 1, 1998, Pages 179-192

The redox- and fixed nitrogen-responsive regulatory protein NIFL from Azotobacter vinelandii comprises discrete flavin and nucleotide-binding domains

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; FLAVOPROTEIN; REGULATOR PROTEIN; TRANSCRIPTION FACTOR;

EID: 0031921952     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00788.x     Document Type: Article
Times cited : (75)

References (35)
  • 1
    • 0028213705 scopus 로고
    • An adenosine nucleotide switch controlling the activity of a cell type-specific transcription factor in B.subtilis
    • Alper, S., Duncan, L., and Losick, R. (1994) An adenosine nucleotide switch controlling the activity of a cell type-specific transcription factor in B.subtilis. Cell 77: 195-205.
    • (1994) Cell , vol.77 , pp. 195-205
    • Alper, S.1    Duncan, L.2    Losick, R.3
  • 2
    • 0028264349 scopus 로고
    • Purification and in vitro activities of the native nitrogen fixation control proteins NIFA and NIFL
    • Austin, S., Buck, M., Cannon, W., Eydmann, T., and Dixon, R. (1994) Purification and in vitro activities of the native nitrogen fixation control proteins NIFA and NIFL. J Bacteriol 176: 3460-3465.
    • (1994) J Bacteriol , vol.176 , pp. 3460-3465
    • Austin, S.1    Buck, M.2    Cannon, W.3    Eydmann, T.4    Dixon, R.5
  • 3
    • 0030925238 scopus 로고    scopus 로고
    • A signal transducer for aerotaxis in Escherichia coli
    • Bibikov, S.I., Biran, R., Rudd, K., and Parkinson, J. (1997) A signal transducer for aerotaxis in Escherichia coli. J Bacteriol 179: 4075-4079.
    • (1997) J Bacteriol , vol.179 , pp. 4075-4079
    • Bibikov, S.I.1    Biran, R.2    Rudd, K.3    Parkinson, J.4
  • 4
    • 0027235767 scopus 로고
    • Sequence and molecular analysis of the nifL gene of Azotobacter vinelandii
    • Blanco, G., Drummond, M., Woodley, P., and Kennedy, C. (1993) Sequence and molecular analysis of the nifL gene of Azotobacter vinelandii. Mol Microbiol 9: 869-880.
    • (1993) Mol Microbiol , vol.9 , pp. 869-880
    • Blanco, G.1    Drummond, M.2    Woodley, P.3    Kennedy, C.4
  • 5
    • 0026316025 scopus 로고
    • The product of the nitrogen fixation regulatory gene nfrX of Azotobacter vinelandii is functionally and structurally homologous to the uridylyltransferase encoded by glnD in enteric bacteria
    • Contreras, A., Drummond, M., Bali, A., Blanco, G., Garcia, E., Bush, G., et al. (1991) The product of the nitrogen fixation regulatory gene nfrX of Azotobacter vinelandii is functionally and structurally homologous to the uridylyltransferase encoded by glnD in enteric bacteria. J Bacteriol 173: 7741-7749.
    • (1991) J Bacteriol , vol.173 , pp. 7741-7749
    • Contreras, A.1    Drummond, M.2    Bali, A.3    Blanco, G.4    Garcia, E.5    Bush, G.6
  • 6
    • 14444283340 scopus 로고
    • Role of interactions between SpollAA and SpollAB in regulating cell-type transcription factor σF in Bacillus subtilis
    • Diederich, D., Wilkinson, J.F., Magnin, T., Najafi, S.M.A., Errington, J., and Yudkin, M.D. (1994) Role of interactions between SpollAA and SpollAB in regulating cell-type transcription factor σF in Bacillus subtilis. Genes Dev. 3: 141-149.
    • (1994) Genes Dev. , vol.3 , pp. 141-149
    • Diederich, D.1    Wilkinson, J.F.2    Magnin, T.3    Najafi, S.M.A.4    Errington, J.5    Yudkin, M.D.6
  • 7
    • 0022668501 scopus 로고
    • Sequence and domain relationships of ntrC and nifA from Klebsiella pneumoniae: Homologies to other regulatory proteins
    • Drummond, M., Whitty, P., and Wootton, J. (1986) Sequence and domain relationships of ntrC and nifA from Klebsiella pneumoniae: homologies to other regulatory proteins. EMBO J 5: 441-447.
    • (1986) EMBO J , vol.5 , pp. 441-447
    • Drummond, M.1    Whitty, P.2    Wootton, J.3
  • 9
    • 0028940319 scopus 로고
    • Transcriptional activation of the nitrogenase promoter in vitro: Adenosine nucleosides are required for inhibition of NIFA activity by NIFL
    • Eydmann, T., Söderbäck, E., Jones, T., Hill, S., Austin, S., and Dixon, R. (1995) Transcriptional activation of the nitrogenase promoter in vitro: adenosine nucleosides are required for inhibition of NIFA activity by NIFL. J Bacteriol 177: 1186-1195.
    • (1995) J Bacteriol , vol.177 , pp. 1186-1195
    • Eydmann, T.1    Söderbäck, E.2    Jones, T.3    Hill, S.4    Austin, S.5    Dixon, R.6
  • 10
    • 0021222463 scopus 로고
    • Nucleotide sequence of the sporulation locus spollA in Bacillus subtilis
    • Fort, P., and Piggot, P.J (1984) Nucleotide sequence of the sporulation locus spollA in Bacillus subtilis. J Gen Microbiol 130: 2147-2153.
    • (1984) J Gen Microbiol , vol.130 , pp. 2147-2153
    • Fort, P.1    Piggot, P.J.2
  • 11
    • 0025878267 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • Gilles-Gonzalez, A., Ditta, G.S., and Helinski, D.R. (1991) A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti. Nature 350: 170-172.
    • (1991) Nature , vol.350 , pp. 170-172
    • Gilles-Gonzalez, A.1    Ditta, G.S.2    Helinski, D.R.3
  • 12
    • 0028241788 scopus 로고
    • Heme-base sensors, exemplified by the kinase FixL are a new class of heme protein with distinctive binding and autoxidation
    • Gilles-Gonzales, M.A., Gonzales, G., Perutz, M.F., Kiger, L., Marden, M.C., and Poyart, C. (1994) Heme-base sensors, exemplified by the kinase FixL are a new class of heme protein with distinctive binding and autoxidation. Biochemistry 33: 8067-8073.
    • (1994) Biochemistry , vol.33 , pp. 8067-8073
    • Gilles-Gonzales, M.A.1    Gonzales, G.2    Perutz, M.F.3    Kiger, L.4    Marden, M.C.5    Poyart, C.6
  • 13
    • 0029829834 scopus 로고    scopus 로고
    • Mechanism of coordinated synthesis of the antagonistic regulatory proteins NifL and NifA of Klebsiella pneumoniae
    • Govantes, F., Molina-Lopez, J.A., and Santero, E. (1996) Mechanism of coordinated synthesis of the antagonistic regulatory proteins NifL and NifA of Klebsiella pneumoniae. J Bacteriol 178: 6817-6823.
    • (1996) J Bacteriol , vol.178 , pp. 6817-6823
    • Govantes, F.1    Molina-Lopez, J.A.2    Santero, E.3
  • 14
    • 0347190468 scopus 로고    scopus 로고
    • NtrC is required for control of Klebsiella pneumoniae NifL activity
    • Elmerich, C., Kondorosi, A., and Newton, W. (eds). Dordrecht: Kluwer Academic Publishers
    • He, L., Soupene, E., and Kustu, S. (1997) NtrC is required for control of Klebsiella pneumoniae NifL activity. In Biological Nitrogen Fixation for the 21st century. Elmerich, C., Kondorosi, A., and Newton, W. (eds). Dordrecht: Kluwer Academic Publishers, pp. 107-110.
    • (1997) Biological Nitrogen Fixation for the 21st Century , pp. 107-110
    • He, L.1    Soupene, E.2    Kustu, S.3
  • 15
    • 0029875231 scopus 로고    scopus 로고
    • Azotobacter vinelandii NIFL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch
    • Hill, S., Austin, S., Eydmann, T., Jones, T., and Dixon, R. (1996) Azotobacter vinelandii NIFL is a flavoprotein that modulates transcriptional activation of nitrogen-fixation genes via a redox-sensitive switch. Proc Natl Acad Sci USA 93: 2143-2148.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2143-2148
    • Hill, S.1    Austin, S.2    Eydmann, T.3    Jones, T.4    Dixon, R.5
  • 17
    • 0027184569 scopus 로고
    • PAS is a dimerisation domain common to Drosophila Period and several transcription factors
    • Huang, Z., Edery, I., and Rosbash, M. (1993) PAS is a dimerisation domain common to Drosophila Period and several transcription factors. Nature 364: 259-262.
    • (1993) Nature , vol.364 , pp. 259-262
    • Huang, Z.1    Edery, I.2    Rosbash, M.3
  • 18
    • 0027497044 scopus 로고
    • In vitro activity of NifL a signal transduction protein for biological nitrogen fixation
    • Lee, H.-S., Narberhaus, F., and Kustu, S. (1993) In vitro activity of NifL a signal transduction protein for biological nitrogen fixation. J Bacteriol 175: 7683-7688.
    • (1993) J Bacteriol , vol.175 , pp. 7683-7688
    • Lee, H.-S.1    Narberhaus, F.2    Kustu, S.3
  • 19
    • 0030614462 scopus 로고    scopus 로고
    • The human Δ1261 mutation of the HERG potassium channel results in a truncated protein that contains a subunit interaction domain and decreases the channel expression
    • Li, X., Xu, J., and Li, M. (1997) The human Δ1261 mutation of the HERG potassium channel results in a truncated protein that contains a subunit interaction domain and decreases the channel expression. J Biol Chem 272: 705-708.
    • (1997) J Biol Chem , vol.272 , pp. 705-708
    • Li, X.1    Xu, J.2    Li, M.3
  • 22
    • 0030029525 scopus 로고    scopus 로고
    • F) alters its conformation and prevent formation of a SpollAA/SpollAB/ADP complex
    • F) alters its conformation and prevent formation of a SpollAA/SpollAB/ADP complex. Mol Microbiol 19: 901-907.
    • (1996) Mol Microbiol , vol.19 , pp. 901-907
    • Magnin, T.1    Lord, M.2    Eriington, J.3    Yudkin, M.D.4
  • 23
    • 0027328345 scopus 로고
    • F, the first compartment-specific transcription factor of B.subtilis, is regulated by an anti-sigma factor that is also a protein kinase
    • Min, K.T., Hilditch, C.M., Diederich, B., Errington, J., and Yudkin, M.D. (1993) F, the first compartment-specific transcription factor of B.subtilis, is regulated by an anti-sigma factor that is also a protein kinase. Cell 74: 735-742.
    • (1993) Cell , vol.74 , pp. 735-742
    • Min, K.T.1    Hilditch, C.M.2    Diederich, B.3    Errington, J.4    Yudkin, M.D.5
  • 24
    • 0029143019 scopus 로고
    • The C-terminal domain of NIFL is sufficient to inhibit NIFA activity
    • Narberhaus, F., Lee, H.-S., Schmitz, R.A., He, L., and Kustu, S. (1995) The C-terminal domain of NIFL is sufficient to inhibit NIFA activity. J Bacteriol 177: 5078-5087.
    • (1995) J Bacteriol , vol.177 , pp. 5078-5087
    • Narberhaus, F.1    Lee, H.-S.2    Schmitz, R.A.3    He, L.4    Kustu, S.5
  • 25
    • 0027056677 scopus 로고
    • Communication modules in bacterial signalling proteins
    • Parkinson, J.S., and Kofoid, E.C. (1992) Communication modules in bacterial signalling proteins. Annu Rev Genet 26: 71-112.
    • (1992) Annu Rev Genet , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 26
    • 0016667190 scopus 로고
    • Complications in the simplest cellular enzyme assay: Lysis of Escherichia coli for the assay of beta-galactosidase
    • Putnam, S.L., and Koch, A.L. (1975) Complications in the simplest cellular enzyme assay: lysis of Escherichia coli for the assay of beta-galactosidase. Anal Biochem 63: 350-360.
    • (1975) Anal Biochem , vol.63 , pp. 350-360
    • Putnam, S.L.1    Koch, A.L.2
  • 27
    • 0030883388 scopus 로고    scopus 로고
    • The Aer protein and the serine chemoreceptor sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behaviour
    • Rebbapragada, A., Johnson, M.S., Harding, G.P., Zuccarelli, A.J., Fletcher, H.M., Zhulin, I.B., and Taylor, B.L. (1997) The Aer protein and the serine chemoreceptor sense intracellular energy levels and transduce oxygen, redox, and energy signals for Escherichia coli behaviour. Proc Natl Acad Sci USA 94: 10541-10546.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10541-10546
    • Rebbapragada, A.1    Johnson, M.S.2    Harding, G.P.3    Zuccarelli, A.J.4    Fletcher, H.M.5    Zhulin, I.B.6    Taylor, B.L.7
  • 28
    • 0000073508 scopus 로고    scopus 로고
    • Molecular analysis of the glnB, AmtB, glnD and glnA genes in Azotobacter vinelandii
    • Elmerich, C., Kondorosi, A., and Newton, W. (eds). Dordrecht: Kluwer Academic Publishers
    • Rudnick, P., Colnaghi, R., Green, A., and Kennedy, C (1998) Molecular analysis of the glnB, AmtB, glnD and glnA genes in Azotobacter vinelandii. In Biological Nitrogen Fixation for the 21st Century. Elmerich, C., Kondorosi, A., and Newton, W. (eds). Dordrecht: Kluwer Academic Publishers, pp. 123-124.
    • (1998) Biological Nitrogen Fixation for the 21st Century , pp. 123-124
    • Rudnick, P.1    Colnaghi, R.2    Green, A.3    Kennedy, C.4
  • 29
    • 9344269892 scopus 로고    scopus 로고
    • Iron is required to relieve inhibitory effects of NifL on transcriptional activation by NifA in Klebsiella pneumoniae
    • Schmitz, R., He, L., and Kustu, S. (1996) Iron is required to relieve inhibitory effects of NifL on transcriptional activation by NifA in Klebsiella pneumoniae. J Bacteriol 178: 4679-4687.
    • (1996) J Bacteriol , vol.178 , pp. 4679-4687
    • Schmitz, R.1    He, L.2    Kustu, S.3
  • 30
    • 0027997677 scopus 로고
    • Oxygen sensitivity and metal ion-dependent transcriptional activation by NIFA protein from Rhizobium leguminosarum biovar trifolii
    • Screen, S., Watson, J., and Dixon, R. (1994) Oxygen sensitivity and metal ion-dependent transcriptional activation by NIFA protein from Rhizobium leguminosarum biovar trifolii. Mol Gen Genet 245: 313-22.
    • (1994) Mol Gen Genet , vol.245 , pp. 313-322
    • Screen, S.1    Watson, J.2    Dixon, R.3
  • 31
    • 0027478839 scopus 로고
    • Characterisation of mutations in the Klebsiella pneumoniae nitrogen fixation regulatory gene nifL which impair oxygen regulation
    • Sidoti, C., Harwood, G., Ackerman, R., Coppard, J., and Merrick, M. (1993) Characterisation of mutations in the Klebsiella pneumoniae nitrogen fixation regulatory gene nifL which impair oxygen regulation. Arch Microbiol 159: 276-81.
    • (1993) Arch Microbiol , vol.159 , pp. 276-281
    • Sidoti, C.1    Harwood, G.2    Ackerman, R.3    Coppard, J.4    Merrick, M.5
  • 34
    • 0028111188 scopus 로고
    • Redundancy of the conserved His residue in Azotobacter vinelandii NifL, a histidine protein kinase homologue which regulates transcription of nitrogen fixation genes
    • Woodley, P., and Drummond, M. (1994) Redundancy of the conserved His residue in Azotobacter vinelandii NifL, a histidine protein kinase homologue which regulates transcription of nitrogen fixation genes. Mol Microbiol 13: 619-626.
    • (1994) Mol Microbiol , vol.13 , pp. 619-626
    • Woodley, P.1    Drummond, M.2
  • 35
    • 0030884102 scopus 로고    scopus 로고
    • PAS domain S-boxes in Archea, Bacteria and sensors for oxygen and redox
    • Zhulin, I.B., Taylor, B.L., and Dixon, R. (1997) PAS domain S-boxes in Archea, Bacteria and sensors for oxygen and redox. Trends Biochem Sci 22: 331-333.
    • (1997) Trends Biochem Sci , vol.22 , pp. 331-333
    • Zhulin, I.B.1    Taylor, B.L.2    Dixon, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.