메뉴 건너뛰기




Volumn 28, Issue 12, 2015, Pages 1353-1363

Sinorhizobium meliloti controls nitric oxide-mediated post-Translational modification of a medicago truncatula nodule protein

Author keywords

[No Author keywords available]

Indexed keywords

NITRIC OXIDE; TYROSINE; VEGETABLE PROTEIN;

EID: 84951728538     PISSN: 08940282     EISSN: None     Source Type: Journal    
DOI: 10.1094/MPMI-05-15-0118-R     Document Type: Article
Times cited : (35)

References (58)
  • 1
    • 67650354415 scopus 로고    scopus 로고
    • Protein tyrosine nitration: Selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins
    • Abello, N., Kerstjens, H. A., Postma, D. S., and Bischoff, R. 2009. Protein tyrosine nitration: Selectivity, physicochemical and biological consequences, denitration, and proteomics methods for the identification of tyrosine-nitrated proteins. J. Proteome Res. 8:3222-3238.
    • (2009) J. Proteome Res , vol.8 , pp. 3222-3238
    • Abello, N.1    Kerstjens, H.A.2    Postma, D.S.3    Bischoff, R.4
  • 2
    • 84873550843 scopus 로고    scopus 로고
    • Transcriptome response to nitrosative stress in Rhodobacter sphaeroides 2.4.1
    • Arai, H., Roh, J. H., Eraso, J. M., and Kaplan, S. 2013. Transcriptome response to nitrosative stress in Rhodobacter sphaeroides 2.4.1. Biosci. Biotechnol. Biochem. 77:111-118.
    • (2013) Biosci. Biotechnol. Biochem , vol.77 , pp. 111-118
    • Arai, H.1    Roh, J.H.2    Eraso, J.M.3    Kaplan, S.4
  • 3
    • 84870721735 scopus 로고    scopus 로고
    • Nitric oxide-dependent posttranslational modification in plants: An update
    • Astier, J., and Lindermayr, C. 2012. Nitric oxide-dependent posttranslational modification in plants: An update. Int. J. Mol. Sci. 13:15193-15208.
    • (2012) Int. J. Mol. Sci , vol.13 , pp. 15193-15208
    • Astier, J.1    Lindermayr, C.2
  • 4
    • 0036128008 scopus 로고    scopus 로고
    • Characterization of a member of the NnrR regulon in Rhodobacter sphaeroides 2.4.3 encoding a haem-copper protein
    • Bartnikas, T. B., Wang, Y., Bobo, T., Veselov, A., Scholes, C. P., and Shapleigh, J. P. 2002. Characterization of a member of the NnrR regulon in Rhodobacter sphaeroides 2.4.3 encoding a haem-copper protein. Microbiology 148:825-833.
    • (2002) Microbiology , vol.148 , pp. 825-833
    • Bartnikas, T.B.1    Wang, Y.2    Bobo, T.3    Veselov, A.4    Scholes, C.P.5    Shapleigh, J.P.6
  • 5
    • 33747518685 scopus 로고    scopus 로고
    • Nitric oxide is formed in Medicago truncatula-Sinorhizobium meliloti functional nodules
    • Baudouin, E., Pieuchot, L., Engler, G., Pauly, N., and Puppo, A. 2006. Nitric oxide is formed in Medicago truncatula-Sinorhizobium meliloti functional nodules. Mol. Plant-Microbe Interact. 19:970-975.
    • (2006) Mol. Plant-Microbe Interact , vol.19 , pp. 970-975
    • Baudouin, E.1    Pieuchot, L.2    Engler, G.3    Pauly, N.4    Puppo, A.5
  • 8
    • 81855175401 scopus 로고    scopus 로고
    • The diversity of microbial responses to nitric oxide and agents of nitrosative stress close cousins but not identical twins
    • Bowman, L. A., McLean, S., Poole, R. K., and Fukuto, J. M. 2011. The diversity of microbial responses to nitric oxide and agents of nitrosative stress close cousins but not identical twins. Adv. Microb. Physiol. 59: 135-219.
    • (2011) Adv. Microb. Physiol , vol.59 , pp. 135-219
    • Bowman, L.A.1    McLean, S.2    Poole, R.K.3    Fukuto, J.M.4
  • 9
    • 84866420464 scopus 로고    scopus 로고
    • Nitric oxide (NO): A key player in the senescence of Medicago truncatula root nodules
    • Cam, Y., Pierre, O., Boncompagni, E., Herouart, D., Meilhoc, E., and Bruand, C. 2012. Nitric oxide (NO): A key player in the senescence of Medicago truncatula root nodules. New Phytol. 196:548-560.
    • (2012) New Phytol , vol.196 , pp. 548-560
    • Cam, Y.1    Pierre, O.2    Boncompagni, E.3    Herouart, D.4    Meilhoc, E.5    Bruand, C.6
  • 10
    • 33645516750 scopus 로고    scopus 로고
    • Sinorhizobium meliloti differentiation during symbiosis with alfalfa: A transcriptomic dissection
    • Capela, D., Filipe, C., Bobik, C., Batut, J., and Bruand, C. 2006. Sinorhizobium meliloti differentiation during symbiosis with alfalfa: A transcriptomic dissection. Mol. Plant-Microbe Interact. 19:363-372.
    • (2006) Mol. Plant-Microbe Interact , vol.19 , pp. 363-372
    • Capela, D.1    Filipe, C.2    Bobik, C.3    Batut, J.4    Bruand, C.5
  • 11
    • 0034056054 scopus 로고    scopus 로고
    • Cellular expression and regulation of the Medicago truncatula cytosolic glutamine synthetase genes in root nodules
    • Carvalho, H., Lescure, N., de Billy, F., Chabaud, M., Lima, L., Salema, R., and Cullimore, J. 2000a. Cellular expression and regulation of the Medicago truncatula cytosolic glutamine synthetase genes in root nodules. Plant Mol. Biol. 42:741-756.
    • (2000) Plant Mol. Biol , vol.42 , pp. 741-756
    • Carvalho, H.1    Lescure, N.2    De Billy, F.3    Chabaud, M.4    Lima, L.5    Salema, R.6    Cullimore, J.7
  • 12
    • 0034613546 scopus 로고    scopus 로고
    • Differential expression of the two cytosolic glutamine synthetase genes in various organs of Medicago truncatula
    • Carvalho, H., Lima, L., Lescure, N., Camut, S., Salema, R., and Cullimore, J. 2000b. Differential expression of the two cytosolic glutamine synthetase genes in various organs of Medicago truncatula. Plant Sci. 159:301-312.
    • (2000) Plant Sci , vol.159 , pp. 301-312
    • Carvalho, H.1    Lima, L.2    Lescure, N.3    Camut, S.4    Salema, R.5    Cullimore, J.6
  • 14
    • 0006041876 scopus 로고
    • An association between photorespiration and protein catabolism: Studies with Chlamydomonas
    • Cullimore, J. V., and Sims, A. P. 1980. An association between photorespiration and protein catabolism: Studies with Chlamydomonas. Planta 150:392-396.
    • (1980) Planta , vol.150 , pp. 392-396
    • Cullimore, J.V.1    Sims, A.P.2
  • 15
    • 33745798389 scopus 로고    scopus 로고
    • A highly conserved Sinorhizobium meliloti operon is induced microaerobically via the FixLJ system and by nitric oxide (NO) via NnrR
    • de Bruijn, F. J., Rossbach, S., Bruand, C., and Parrish, J. R. 2006. A highly conserved Sinorhizobium meliloti operon is induced microaerobically via the FixLJ system and by nitric oxide (NO) via NnrR. Environ. Microbiol. 8:1371-1381.
    • (2006) Environ. Microbiol , vol.8 , pp. 1371-1381
    • De Bruijn, F.J.1    Rossbach, S.2    Bruand, C.3    Parrish, J.R.4
  • 17
    • 0000527903 scopus 로고
    • Replication of an origincontaining derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski, D. H., and Helinski, D. R. 1979. Replication of an origincontaining derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc. Natl. Acad. Sci. U.S.A. 76:1648-1652.
    • (1979) Proc. Natl. Acad. Sci. U.S.A , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 18
    • 84865311277 scopus 로고    scopus 로고
    • NO loading: Efficiency assessment of five commonly used application methods of sodium nitroprusside in Medicago truncatula plants
    • Filippou, P., Antoniou, C., Yelamanchili, S., and Fotopoulos, V. 2012. NO loading: Efficiency assessment of five commonly used application methods of sodium nitroprusside in Medicago truncatula plants. Plant Physiol. Biochem. 60:115-118.
    • (2012) Plant Physiol. Biochem , vol.60 , pp. 115-118
    • Filippou, P.1    Antoniou, C.2    Yelamanchili, S.3    Fotopoulos, V.4
  • 21
    • 84884257971 scopus 로고    scopus 로고
    • Identification of genes involved in Neisseria meningitidis colonization
    • Jamet, A., Euphrasie, D., Martin, P., and Nassif, X. 2013. Identification of genes involved in Neisseria meningitidis colonization. Infect. Immun. 81:3375-3381.
    • (2013) Infect. Immun , vol.81 , pp. 3375-3381
    • Jamet, A.1    Euphrasie, D.2    Martin, P.3    Nassif, X.4
  • 23
    • 34249857689 scopus 로고    scopus 로고
    • Escherichia coli di-iron YtfE protein is necessary for the repair of stressdamaged iron-sulfur clusters
    • Justino, M. C., Almeida, C. C., Teixeira, M., and Saraiva, L. M. 2007. Escherichia coli di-iron YtfE protein is necessary for the repair of stressdamaged iron-sulfur clusters. J. Biol. Chem. 282:10352-10359.
    • (2007) J. Biol. Chem , vol.282 , pp. 10352-10359
    • Justino, M.C.1    Almeida, C.C.2    Teixeira, M.3    Saraiva, L.M.4
  • 24
    • 59449083567 scopus 로고    scopus 로고
    • Di-iron proteins of the Ric family are involved in iron-sulfur cluster repair
    • Justino, M. C., Baptista, J. M., and Saraiva, L. M. 2009. Di-iron proteins of the Ric family are involved in iron-sulfur cluster repair. Biometals 22: 99-108.
    • (2009) Biometals , vol.22 , pp. 99-108
    • Justino, M.C.1    Baptista, J.M.2    Saraiva, L.M.3
  • 25
    • 72049132368 scopus 로고    scopus 로고
    • Involvement of nitric oxide in the inhibition of nitrogenase activity by nitrate in Lotus root nodules
    • Kato, K., Kanahama, K., and Kanayama, Y. 2010. Involvement of nitric oxide in the inhibition of nitrogenase activity by nitrate in Lotus root nodules. J. Plant Physiol. 167:238-241.
    • (2011) J. Plant Physiol , vol.167 , pp. 238-241
    • Kato, K.1    Kanahama, K.2    Kanayama, Y.3
  • 26
    • 0028793123 scopus 로고
    • Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes
    • Kovach, M. E., Elzer, P. H., Hill, D. S., Robertson, G. T., Farris, M. A., Roop, R. M., 2nd, and Peterson, K. M. 1995. Four new derivatives of the broad-host-range cloning vector pBBR1MCS, carrying different antibiotic-resistance cassettes. Gene 166:175-176.
    • (1995) Gene , vol.166 , pp. 175-176
    • Kovach, M.E.1    Elzer, P.H.2    Hill, D.S.3    Robertson, G.T.4    Farris, M.A.5    Roop, I.I.R.M.6    Peterson, K.M.7
  • 27
    • 0005093093 scopus 로고
    • Plant gene expression in effective and ineffective root nodules of alfalfa (Medicago sativa
    • Lullien, V., Barker, D. G., de Lajudie, P., and Huguet, T. 1987. Plant gene expression in effective and ineffective root nodules of alfalfa (Medicago sativa). Plant Mol. Biol. 9:469-478.
    • (1987) Plant Mol. Biol , vol.9 , pp. 469-478
    • Lullien, V.1    Barker, D.G.2    De Lajudie, P.3    Huguet, T.4
  • 28
    • 0032078780 scopus 로고    scopus 로고
    • Direct detection of radicals in intact soybean nodules: Presence of nitric oxide-leghemoglobin complexes
    • Mathieu, C., Moreau, S., Frendo, P., Puppo, A., and Davies, M. J. 1998. Direct detection of radicals in intact soybean nodules: Presence of nitric oxide-leghemoglobin complexes. Free Radic. Biol. Med. 24:1242-1249.
    • (1998) Free Radic. Biol. Med , vol.24 , pp. 1242-1249
    • Mathieu, C.1    Moreau, S.2    Frendo, P.3    Puppo, A.4    Davies, M.J.5
  • 29
    • 0020058862 scopus 로고
    • Physical and genetic characterization of symbiotic and auxotrophic mutants of Rhizobium meliloti induced by transposon Tn5 mutagenesis
    • Meade, H. M., Long, S. R., Ruvkun, G. B., Brown, S. E., and Ausubel, F. M. 1982. Physical and genetic characterization of symbiotic and auxotrophic mutants of Rhizobium meliloti induced by transposon Tn5 mutagenesis. J. Bacteriol. 149:114-122.
    • (1982) J. Bacteriol , vol.149 , pp. 114-122
    • Meade, H.M.1    Long, S.R.2    Ruvkun, G.B.3    Brown, S.E.4    Ausubel, F.M.5
  • 30
    • 84885198183 scopus 로고    scopus 로고
    • Control of NO level in rhizobium-legume root nodules: Not only a plant globin story
    • Meilhoc E., Blanquet P., Cam Y. and Bruand C. 2013. Control of NO level in rhizobium-legume root nodules: Not only a plant globin story. Plant Signal. Behav. 8:10.
    • (2013) Plant Signal. Behav , vol.8 , pp. 10
    • Meilhoc, E.1    Blanquet, P.2    Cam, Y.3    Bruand, C.4
  • 32
    • 77952689236 scopus 로고    scopus 로고
    • The response to nitric oxide of the nitrogen-fixing symbiont Sinorhizobium meliloti
    • Meilhoc, E., Cam, Y., Skapski, A., and Bruand, C. 2010. The response to nitric oxide of the nitrogen-fixing symbiont Sinorhizobium meliloti. Mol. Plant-Microbe Interact. 23:748-759.
    • (2011) Mol. Plant-Microbe Interact , vol.23 , pp. 748-759
    • Meilhoc, E.1    Cam, Y.2    Skapski, A.3    Bruand, C.4
  • 33
    • 80455173502 scopus 로고    scopus 로고
    • Glutamine synthetase is a molecular target of nitric oxide in root nodules of Medicago truncatula and is regulated by tyrosine nitration
    • Melo, P. M., Silva, L. S., Ribeiro, I., Seabra, A. R., and Carvalho, H. G. 2011. Glutamine synthetase is a molecular target of nitric oxide in root nodules of Medicago truncatula and is regulated by tyrosine nitration. Plant Physiol. 157:1505-1517.
    • (2011) Plant Physiol , vol.157 , pp. 1505-1517
    • Melo, P.M.1    Silva, L.S.2    Ribeiro, I.3    Seabra, A.R.4    Carvalho, H.G.5
  • 34
    • 31544432566 scopus 로고    scopus 로고
    • NO way to live: The various roles of nitric oxide in plant-pathogen interactions
    • Mur, L. A., Carver, T. L., and Prats, E. 2006. NO way to live: The various roles of nitric oxide in plant-pathogen interactions. J. Exp. Bot. 57: 489-505.
    • (2006) J. Exp. Bot , vol.57 , pp. 489-505
    • Mur, L.A.1    Carver, T.L.2    Prats, E.3
  • 37
  • 38
    • 80455174952 scopus 로고    scopus 로고
    • The rules of engagement in the legume-rhizobial symbiosis
    • Oldroyd, G. E., Murray, J. D., Poole, P. S., and Downie, J. A. 2011. The rules of engagement in the legume-rhizobial symbiosis. Annu. Rev. Genet. 45:119-144.
    • (2011) Annu. Rev. Genet , vol.45 , pp. 119-144
    • Oldroyd, G.E.1    Murray, J.D.2    Poole, P.S.3    Downie, J.A.4
  • 39
    • 84906852609 scopus 로고    scopus 로고
    • Conserved evolutionary units in the heme-copper oxidase superfamily revealed by novel homologous protein families
    • Pei, J., Li, W., Kinch, L. N., and Grishin, N. V. 2014. Conserved evolutionary units in the heme-copper oxidase superfamily revealed by novel homologous protein families. Protein Sci. 23:1220-1234.
    • (2014) Protein Sci , vol.23 , pp. 1220-1234
    • Pei, J.1    Li, W.2    Kinch, L.N.3    Grishin, N.V.4
  • 41
    • 33745122953 scopus 로고    scopus 로고
    • Construction of a large signature-Tagged mini-Tn5 transposon library and its application to mutagenesis of Sinorhizobium meliloti
    • Pobigaylo, N., Wetter, D., Szymczak, S., Schiller, U., Kurtz, S., Meyer, F., Nattkemper, T. W., and Becker, A. 2006. Construction of a large signature-Tagged mini-Tn5 transposon library and its application to mutagenesis of Sinorhizobium meliloti. Appl. Environ. Microbiol. 72: 4329-37.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 4329-4337
    • Pobigaylo, N.1    Wetter, D.2    Szymczak, S.3    Schiller, U.4    Kurtz, S.5    Meyer, F.6    Nattkemper, T.W.7    Becker, A.8
  • 42
    • 79951677750 scopus 로고    scopus 로고
    • Nitric oxide, reactive nitrogen species and associated enzymes during plant senescence
    • Prochazkova, D., and Wilhelmova, N. 2011. Nitric oxide, reactive nitrogen species and associated enzymes during plant senescence. Nitric Oxide 24:61-65.
    • (2011) Nitric Oxide , vol.24 , pp. 61-65
    • Prochazkova, D.1    Wilhelmova, N.2
  • 44
    • 84878215218 scopus 로고    scopus 로고
    • Hydrogen peroxide and nitric oxide: Key regulators of the Legume-Rhizobium and mycorrhizal symbioses
    • Puppo, A., Pauly, N., Boscari, A., Mandon, K., and Brouquisse, R. 2013. Hydrogen peroxide and nitric oxide: Key regulators of the Legume-Rhizobium and mycorrhizal symbioses. Antioxid. Redox Signal. 18: 2202-2219.
    • (2013) Antioxid. Redox Signal , vol.18 , pp. 2202-2219
    • Puppo, A.1    Pauly, N.2    Boscari, A.3    Mandon, K.4    Brouquisse, R.5
  • 46
    • 84923508152 scopus 로고    scopus 로고
    • Leghemoglobin is nitrated in functional legume nodules in a tyrosine residue within the heme cavity by a nitrite/peroxide-dependent mechanism
    • Sainz, M., Calvo-Begueria, L., Perez-Rontome, C., Wienkoop, S., Abían, J., Staudinger, C., Bartesaghi, S., Radi, R., and Becana, M. 2015. Leghemoglobin is nitrated in functional legume nodules in a tyrosine residue within the heme cavity by a nitrite/peroxide-dependent mechanism. Plant J. 81:723-735.
    • (2015) Plant J , vol.81 , pp. 723-735
    • Sainz, M.1    Calvo-Begueria, L.2    Perez-Rontome, C.3    Wienkoop, S.4    Abían, J.5    Staudinger, C.6    Bartesaghi, S.7    Radi, R.8    Becana, M.9
  • 48
    • 34249796382 scopus 로고    scopus 로고
    • An extracytoplasmic function sigma factor acts as a general stress response regulator in Sinorhizobium meliloti
    • Sauviac, L., Philippe, H., Phok, K., and Bruand, C. 2007. An extracytoplasmic function sigma factor acts as a general stress response regulator in Sinorhizobium meliloti. J. Bacteriol. 189:4204-4216.
    • (2007) J. Bacteriol , vol.189 , pp. 4204-4216
    • Sauviac, L.1    Philippe, H.2    Phok, K.3    Bruand, C.4
  • 49
    • 84900855382 scopus 로고    scopus 로고
    • Possible role of glutamine synthetase in the NO signaling response in root nodules by contributing to the antioxidant defenses
    • Silva, L., and Carvalho, H. 2013. Possible role of glutamine synthetase in the NO signaling response in root nodules by contributing to the antioxidant defenses. Front. Plant Sci. 4:372-380.
    • (2013) Front. Plant Sci , vol.4 , pp. 372-380
    • Silva, L.1    Carvalho, H.2
  • 51
    • 84860506227 scopus 로고    scopus 로고
    • The NorR regulon is critical for Vibrio cholerae resistance to nitric oxide and sustained colonization of the intestines
    • Stern, A. M., Hay, A. J., Liu, Z., Desland, F. A., Zhang, J., Zhong, Z., and Zhu, J. 2012. The NorR regulon is critical for Vibrio cholerae resistance to nitric oxide and sustained colonization of the intestines. MBio 3: e00013-12.
    • (2012) MBio , vol.3 , pp. e00013-e00112
    • Stern, A.M.1    Hay, A.J.2    Liu, Z.3    Desland, F.A.4    Zhang, J.5    Zhong, Z.6    Zhu, J.7
  • 52
    • 84885445591 scopus 로고    scopus 로고
    • A novel protein protects bacterial iron-dependent metabolism from nitric oxide
    • Stern, A. M., Liu, B., Bakken, L. R., Shapleigh, J. P., and Zhu, J. 2013. A novel protein protects bacterial iron-dependent metabolism from nitric oxide. J. Bacteriol. 195:4702-4708.
    • (2013) J. Bacteriol , vol.195 , pp. 4702-4708
    • Stern, A.M.1    Liu, B.2    Bakken, L.R.3    Shapleigh, J.P.4    Zhu, J.5
  • 53
    • 84894470782 scopus 로고    scopus 로고
    • An introduction to nitric oxide sensing and response in bacteria
    • Stern, A. M., and Zhu, J. 2014. An introduction to nitric oxide sensing and response in bacteria. Adv. Appl. Microbiol. 87:187-220.
    • (2014) Adv. Appl. Microbiol , vol.87 , pp. 187-220
    • Stern, A.M.1    Zhu, J.2
  • 54
    • 84861438378 scopus 로고    scopus 로고
    • What determines the efficiency of N2-fixing Rhizobium-legume symbioses?
    • Terpolilli, J. J., Hood, G. A., and Poole, P. S. 2012. What determines the efficiency of N2-fixing Rhizobium-legume symbioses? Adv. Microb. Physiol. 60:325-389.
    • (2012) Adv. Microb. Physiol , vol.60 , pp. 325-389
    • Terpolilli, J.J.1    Hood, G.A.2    Poole, P.S.3
  • 56
    • 0020366896 scopus 로고
    • Nitrite and nitric oxide as inhibitors of nitrogenase from soybean bacteroids
    • Trinchant, J. C., and Rigaud, J. 1982. Nitrite and nitric oxide as inhibitors of nitrogenase from soybean bacteroids. Appl. Environ. Microbiol. 44: 1385-1388.
    • (1982) Appl. Environ. Microbiol , vol.44 , pp. 1385-1388
    • Trinchant, J.C.1    Rigaud, J.2
  • 57
    • 79952639196 scopus 로고    scopus 로고
    • The roles of NO in microbial symbioses
    • Wang, Y., and Ruby, E. G. 2011. The roles of NO in microbial symbioses. Cell. Microbiol. 13:518-526.
    • (2011) Cell. Microbiol , vol.13 , pp. 518-526
    • Wang, Y.1    Ruby, E.G.2
  • 58
    • 84899962359 scopus 로고    scopus 로고
    • Nitric oxide function in plant biology: A redox cue in deconvolution
    • Yu, M., Lamattina, L., Spoel, S. H., and Loake, G. J. 2014. Nitric oxide function in plant biology: A redox cue in deconvolution. New Phytol. 202:1142-1156.
    • (2014) New Phytol , vol.202 , pp. 1142-1156
    • Yu, M.1    Lamattina, L.2    Spoel, S.H.3    Loake, G.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.