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Volumn 191, Issue 5, 2009, Pages 1463-1471

Functional differences of two distinct catalases in Mesorhizobium loti MAFF303099 under free-living and symbiotic conditions

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; HYDROXIDE; KATE PROTEIN; KATG PROTEIN; PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; HYDROGEN PEROXIDE; PEROXIDASE;

EID: 62649149896     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01583-08     Document Type: Article
Times cited : (20)

References (46)
  • 1
    • 0242500443 scopus 로고    scopus 로고
    • Possible roles for a cysteine protease and hydrogen peroxide in soybean nodule development and senescence
    • Alesandrini, F., R. Mathis, G. Van de Sype, D. Hérouart, and A. Puppo. 2003. Possible roles for a cysteine protease and hydrogen peroxide in soybean nodule development and senescence. New Phytol. 158:131-138.
    • (2003) New Phytol , vol.158 , pp. 131-138
    • Alesandrini, F.1    Mathis, R.2    Van de Sype, G.3    Hérouart, D.4    Puppo, A.5
  • 2
    • 4744347907 scopus 로고    scopus 로고
    • Purification and physical-chemical characterization of the three hydroperoxidases from the symbiotic bacterium Sinorhizobium meliloti
    • Ardissone, S., P. Frendo, E. Laurenti, W. Jantschko, C. Obinger, A. Puppo, and R. P. Ferrari. 2004. Purification and physical-chemical characterization of the three hydroperoxidases from the symbiotic bacterium Sinorhizobium meliloti. Biochemistry 43:12692-12699.
    • (2004) Biochemistry , vol.43 , pp. 12692-12699
    • Ardissone, S.1    Frendo, P.2    Laurenti, E.3    Jantschko, W.4    Obinger, C.5    Puppo, A.6    Ferrari, R.P.7
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0015189585 scopus 로고
    • Control of leghemoglobin synthesis in snake beans
    • Broughton, W. J., and M. J. Dilworth. 1971. Control of leghemoglobin synthesis in snake beans. Biochem. J. 125:1075-1080.
    • (1971) Biochem. J , vol.125 , pp. 1075-1080
    • Broughton, W.J.1    Dilworth, M.J.2
  • 5
    • 0028889269 scopus 로고    scopus 로고
    • Brown, S. M., M, L. Howell, M. L. Vasil, A. J, Anderson, and D. J. Hassett. 1995. Cloning and characterization of the katB gene of Pseudomonas aeruginosa encoding a hydrogen peroxide-inducible catalase: purification of KatB, cellular localization, and demonstration that it is essential for optimal resistance to hydrogen peroxide. J. Bacteriol. 177:6536-6544.
    • Brown, S. M., M, L. Howell, M. L. Vasil, A. J, Anderson, and D. J. Hassett. 1995. Cloning and characterization of the katB gene of Pseudomonas aeruginosa encoding a hydrogen peroxide-inducible catalase: purification of KatB, cellular localization, and demonstration that it is essential for optimal resistance to hydrogen peroxide. J. Bacteriol. 177:6536-6544.
  • 6
    • 0842309140 scopus 로고    scopus 로고
    • Diversity of structures and properties among catalases
    • Chelikani, P., I. Fita, and P. C. Loewen. 2004. Diversity of structures and properties among catalases. Cell. Mol. Life Sci. 61:192-208.
    • (2004) Cell. Mol. Life Sci , vol.61 , pp. 192-208
    • Chelikani, P.1    Fita, I.2    Loewen, P.C.3
  • 7
    • 0021139249 scopus 로고
    • Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase
    • Clare, D. A., M. N. Duong, D. Darr, F. Archibald, and I. Fridovich. 1984. Effects of molecular oxygen on detection of superoxide radical with nitroblue tetrazolium and on activity stains for catalase. Anal. Biochem. 140:532-537.
    • (1984) Anal. Biochem , vol.140 , pp. 532-537
    • Clare, D.A.1    Duong, M.N.2    Darr, D.3    Archibald, F.4    Fridovich, I.5
  • 8
    • 1842349188 scopus 로고
    • Broad host range DNA cloning system for gram-negative bacteria: Construction of a gene bank of Rhizobium meliloti
    • Ditta, G., S. Stanfield, D. Corbin, and D. Helinski. 1980. Broad host range DNA cloning system for gram-negative bacteria: construction of a gene bank of Rhizobium meliloti. Proc. Natl. Acad. Sci. USA 77:7347-7351.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 7347-7351
    • Ditta, G.1    Stanfield, S.2    Corbin, D.3    Helinski, D.4
  • 9
    • 14544302196 scopus 로고    scopus 로고
    • Defence of Rhizobium etli bacteroids against oxidative stress involves a complexly regulated atypical 2-Cys perox-iredoxin
    • Dombrecht, B., C. Heusdens, S. Beullens, C. Verreth, E. Mulkers, P. Proost, J. Vanderleyden, and J. Michiels. 2005. Defence of Rhizobium etli bacteroids against oxidative stress involves a complexly regulated atypical 2-Cys perox-iredoxin. Mol. Microbiol. 55:1207-1221.
    • (2005) Mol. Microbiol , vol.55 , pp. 1207-1221
    • Dombrecht, B.1    Heusdens, C.2    Beullens, S.3    Verreth, C.4    Mulkers, E.5    Proost, P.6    Vanderleyden, J.7    Michiels, J.8
  • 10
    • 12244280198 scopus 로고    scopus 로고
    • Ordered cosmid library of the Mesorhizobium loti MAFF303099 genome for systematic gene disruption and complementation analysis
    • Hattori, Y., H. Omori, M. Hanyu, N. Kaseda, E, Mishima, T. Kaneko, S. Tabata, and K. Saeki. 2002. Ordered cosmid library of the Mesorhizobium loti MAFF303099 genome for systematic gene disruption and complementation analysis. Plant Cell Physiol. 43:1542-1557.
    • (2002) Plant Cell Physiol , vol.43 , pp. 1542-1557
    • Hattori, Y.1    Omori, H.2    Hanyu, M.3    Kaseda, N.4    Mishima, E.5    Kaneko, T.6    Tabata, S.7    Saeki, K.8
  • 11
    • 0029830431 scopus 로고    scopus 로고
    • Cloning and characterization of the katA gene of Rhizobium meliloti encoding a hydrogen peroxide-inducible catalase
    • Hérouart, D., S. Sigaud, S. Moreau, P. Frendo, D. Touati, and A. Puppo. 1996. Cloning and characterization of the katA gene of Rhizobium meliloti encoding a hydrogen peroxide-inducible catalase. J. Bacteriol. 178:6802-6809.
    • (1996) J. Bacteriol , vol.178 , pp. 6802-6809
    • Hérouart, D.1    Sigaud, S.2    Moreau, S.3    Frendo, P.4    Touati, D.5    Puppo, A.6
  • 12
    • 84987043534 scopus 로고
    • Developmental biology of legume nodulation
    • Hirsch, A. M. 1992. Developmental biology of legume nodulation. New Phytol. 122:211-237.
    • (1992) New Phytol , vol.122 , pp. 211-237
    • Hirsch, A.M.1
  • 13
    • 0242608621 scopus 로고    scopus 로고
    • Imlay, J., A. 2003. Pathways of oxidative damage. Annu. Rev. Microbiol. 57:395-418.
    • Imlay, J., A. 2003. Pathways of oxidative damage. Annu. Rev. Microbiol. 57:395-418.
  • 14
    • 11144308938 scopus 로고    scopus 로고
    • The katA catalase gene is regulated by OxyR in both free-living and symbiotic Sinorhizobium meliloti
    • Jamet, A., E. Kiss, J. Batut, A. Puppo, and D. Hérouart. 2005. The katA catalase gene is regulated by OxyR in both free-living and symbiotic Sinorhizobium meliloti. J. Bacteriol. 187:376-381.
    • (2005) J. Bacteriol , vol.187 , pp. 376-381
    • Jamet, A.1    Kiss, E.2    Batut, J.3    Puppo, A.4    Hérouart, D.5
  • 15
    • 0037370853 scopus 로고    scopus 로고
    • Expression of the bacterial catalase genes during Sinorhizobium meliloti-Medicago sativa symbiosis and their crucial role during the infection process
    • Jamet, A., S. Sigaud, G. Van de Sype, A. Puppo, and D. Hérouart. 2003. Expression of the bacterial catalase genes during Sinorhizobium meliloti-Medicago sativa symbiosis and their crucial role during the infection process. Mol. Plant-Microbe Interact. 16:217-225.
    • (2003) Mol. Plant-Microbe Interact , vol.16 , pp. 217-225
    • Jamet, A.1    Sigaud, S.2    Van de Sype, G.3    Puppo, A.4    Hérouart, D.5
  • 16
    • 0020352836 scopus 로고
    • Intracellular catalase function: Analysis of the catalytic activity by product formation in isolated liver cells
    • Jones, D. P. 1982. Intracellular catalase function: analysis of the catalytic activity by product formation in isolated liver cells. Arch. Biochem. Biophys. 214:806-814.
    • (1982) Arch. Biochem. Biophys , vol.214 , pp. 806-814
    • Jones, D.P.1
  • 18
    • 0036062728 scopus 로고    scopus 로고
    • Molecular characterization of long direct repeat (LDR) sequences expressing a stable mRNA encoding for a 35-amino-acid cell-killing peptide and a cis-encoded small antisense RNA in Escherichia coli
    • Kawano, M., T. Oshima, H. Kasai, and H. Mori. 2002. Molecular characterization of long direct repeat (LDR) sequences expressing a stable mRNA encoding for a 35-amino-acid cell-killing peptide and a cis-encoded small antisense RNA in Escherichia coli. Mol. Microbiol. 45:333-349.
    • (2002) Mol. Microbiol , vol.45 , pp. 333-349
    • Kawano, M.1    Oshima, T.2    Kasai, H.3    Mori, H.4
  • 19
    • 0041821981 scopus 로고    scopus 로고
    • Host sanctions and the legume-rhizobium mutualism
    • Kiers, E. T., R. A. Rousseau, S. A. West, and R. F. Denison. 2003. Host sanctions and the legume-rhizobium mutualism. Nature 425:78-81.
    • (2003) Nature , vol.425 , pp. 78-81
    • Kiers, E.T.1    Rousseau, R.A.2    West, S.A.3    Denison, R.F.4
  • 20
    • 0033118515 scopus 로고    scopus 로고
    • Rice ENOD40: Isolation, expression analvsis in rice, transgenic soybean root nodules
    • Kouchi, H., K. Takane, R. B. So, J. K. Ladha, and P. M. Reddy. 1999. Rice ENOD40: isolation, expression analvsis in rice, transgenic soybean root nodules. Plant J. 18:121-129.
    • (1999) Plant J , vol.18 , pp. 121-129
    • Kouchi, H.1    Takane, K.2    So, R.B.3    Ladha, J.K.4    Reddy, P.M.5
  • 22
    • 0026020230 scopus 로고
    • Identification of a central regulator of stationary-phase gene expression in Escherichia coli
    • Lange, R., and R. Hengge-Aronis. 1991. Identification of a central regulator of stationary-phase gene expression in Escherichia coli. Mol. Microbiol. 5:49-59.
    • (1991) Mol. Microbiol , vol.5 , pp. 49-59
    • Lange, R.1    Hengge-Aronis, R.2
  • 24
    • 0021719208 scopus 로고
    • Genetic mapping of katF, a locus that with katE affects the synthesis of a second catalase species in Escherichia coli
    • Loewen, P. C, and B. L. Triggs. 1984. Genetic mapping of katF, a locus that with katE affects the synthesis of a second catalase species in Escherichia coli. J. Bacteriol. 160:668-675.
    • (1984) J. Bacteriol , vol.160 , pp. 668-675
    • Loewen, P.C.1    Triggs, B.L.2
  • 25
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor. NY
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor. NY.
    • (1972) Experiments in molecular genetics
    • Miller, J.H.1
  • 26
  • 27
    • 9244247620 scopus 로고    scopus 로고
    • KatG is the primary detoxifier of hydrogen peroxide produced by aerobic metabolism in Bradyrhizobium japonicum
    • Panek, H. R., and M. R, O'Brian. 2004. KatG is the primary detoxifier of hydrogen peroxide produced by aerobic metabolism in Bradyrhizobium japonicum. J. Bacteriol. 186:7874-7880.
    • (2004) J. Bacteriol , vol.186 , pp. 7874-7880
    • Panek, H.R.1    O'Brian, M.R.2
  • 28
    • 1842471990 scopus 로고    scopus 로고
    • The role of a bifunctional catalase-peroxidase KatA in protection of Agrobacterium tume-faciens from menadione toxicity
    • Prapagdee, B., P. Yattanaviboon, and S. Mongkolsuk. 2004. The role of a bifunctional catalase-peroxidase KatA in protection of Agrobacterium tume-faciens from menadione toxicity. FEMS Microbiol. Lett. 232:217-223.
    • (2004) FEMS Microbiol. Lett , vol.232 , pp. 217-223
    • Prapagdee, B.1    Yattanaviboon, P.2    Mongkolsuk, S.3
  • 29
    • 0021592032 scopus 로고
    • In vitro insertional mutagenesis with a selectable DNA fragment
    • Prentki, P., and H. M. Krisch. 1984. In vitro insertional mutagenesis with a selectable DNA fragment. Gene 29:303-313.
    • (1984) Gene , vol.29 , pp. 303-313
    • Prentki, P.1    Krisch, H.M.2
  • 31
    • 0027565051 scopus 로고    scopus 로고
    • Saeki, K., K. Tokuda, T. Fujiwara, and H. Matsubara. 1993. Nucleotide sequence and genetic analysis of the region essential for functional expression of the gene for ferredoxin I, fdxN, in Rhodobacter capsulatum: sharing of one upstream activator sequence in opposite directions by two operons related to nitrogen fixation. Plant Cell Physiol. 34:185-199.
    • Saeki, K., K. Tokuda, T. Fujiwara, and H. Matsubara. 1993. Nucleotide sequence and genetic analysis of the region essential for functional expression of the gene for ferredoxin I, fdxN, in Rhodobacter capsulatum: sharing of one upstream activator sequence in opposite directions by two operons related to nitrogen fixation. Plant Cell Physiol. 34:185-199.
  • 32
    • 0024603522 scopus 로고
    • Exonuclease III and the catalase hydroperoxidase II in Escherichia coli are both regulated by the katF gene product
    • Sak, B. D., A. Eisenstark, and D. Touati. 1989. Exonuclease III and the catalase hydroperoxidase II in Escherichia coli are both regulated by the katF gene product. Proc. Natl. Acad. Sci. USA 86:3271-3275.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3271-3275
    • Sak, B.D.1    Eisenstark, A.2    Touati, D.3
  • 35
    • 34249796382 scopus 로고    scopus 로고
    • An extracytoplasmic function sigma factor acts as a general stress response regulator in Sinorhi-zobium meliloti
    • Sauviac, L., H. Philippe, K. Phok, and C. Bruand. 2007. An extracytoplasmic function sigma factor acts as a general stress response regulator in Sinorhi-zobium 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
  • 36
    • 0028289983 scopus 로고
    • Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: Selection of defined deletions in the chromosome of Corynebacterium glutamicum
    • Schäfer, A., A. Tauch, W. Jäger, J. Kalirnowski, G. Thierbach, and A. Pühler. 1994. Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined deletions in the chromosome of Corynebacterium glutamicum. Gene 145:69-73.
    • (1994) Gene , vol.145 , pp. 69-73
    • Schäfer, A.1    Tauch, A.2    Jäger, W.3    Kalirnowski, J.4    Thierbach, G.5    Pühler, A.6
  • 37
    • 0035209075 scopus 로고    scopus 로고
    • Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli
    • Seaver, L. C., and J. A. Imlay. 2001. Alkyl hydroperoxide reductase is the primary scavenger of endogenous hydrogen peroxide in Escherichia coli. J. Bacteriol. 183:7173-7181.
    • (2001) J. Bacteriol , vol.183 , pp. 7173-7181
    • Seaver, L.C.1    Imlay, J.A.2
  • 38
    • 0042510530 scopus 로고    scopus 로고
    • Nod factor inhibition of reactive oxygen efflux in a host legume
    • Shaw, S. L., and S. R. Long. 2003. Nod factor inhibition of reactive oxygen efflux in a host legume. Plant Physiol. 132:2196-2204.
    • (2003) Plant Physiol , vol.132 , pp. 2196-2204
    • Shaw, S.L.1    Long, S.R.2
  • 39
    • 0032929263 scopus 로고    scopus 로고
    • Differential regulation of two divergent Sinorhizobium meliloti genes for HPII-like catalases during free-living growth and protective role of both catalases during symbiosis
    • Sigaud, S., V. Becquet, P. Frendo, A. Puppo, and D. Hérouart. 1999. Differential regulation of two divergent Sinorhizobium meliloti genes for HPII-like catalases during free-living growth and protective role of both catalases during symbiosis. J. Bacteriol. 181:2634-2639.
    • (1999) J. Bacteriol , vol.181 , pp. 2634-2639
    • Sigaud, S.1    Becquet, V.2    Frendo, P.3    Puppo, A.4    Hérouart, D.5
  • 40
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative s tress-inducible genes: Direct activation by oxidation
    • Storz, G., L. A. Tartaglia, and B. N. Ames. 1990. Transcriptional regulator of oxidative s tress-inducible genes: direct activation by oxidation. Science 248: 189-194.
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.N.3
  • 41
    • 0037560407 scopus 로고    scopus 로고
    • The Lotus japonicus Senl gene controls rhizobial differentiation into nitrogen-fixing bacteroids in nodules
    • Suganuma, N., Y. Nakamura, M. Yamamoto, T. Ohta, H. Koiwa, S. Akao, and M. Kawaguchi. 2003. The Lotus japonicus Senl gene controls rhizobial differentiation into nitrogen-fixing bacteroids in nodules. Mol. Genet. Genomics 269:312-320.
    • (2003) Mol. Genet. Genomics , vol.269 , pp. 312-320
    • Suganuma, N.1    Nakamura, Y.2    Yamamoto, M.3    Ohta, T.4    Koiwa, H.5    Akao, S.6    Kawaguchi, M.7
  • 42
  • 44
    • 0037854380 scopus 로고    scopus 로고
    • Only one catalase, KatG, is detectable in Rhizobium etli, and is encoded along with the regulator OxyR on a plasmid replicon
    • Vargas, M. C, S. Encarnacion, A. Davalos, A. Reyes-Perez, Y. Mora, A. Garcia-de los Santos, S. Brom, and J. Mora. 2003. Only one catalase, KatG, is detectable in Rhizobium etli, and is encoded along with the regulator OxyR on a plasmid replicon. Microbiology 149:1165-1176.
    • (2003) Microbiology , vol.149 , pp. 1165-1176
    • Vargas, M.C.1    Encarnacion, S.2    Davalos, A.3    Reyes-Perez, A.4    Mora, Y.5    Garcia-de los Santos, A.6    Brom, S.7    Mora, J.8
  • 45
    • 0026074553 scopus 로고
    • Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII
    • von Ossowski, I., M. R. Mulvey, P. A. Leco, A. Borys, and P. C. Loewen. 1991. Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII. J. Bacteriol. 173:514-520.
    • (1991) J. Bacteriol , vol.173 , pp. 514-520
    • von Ossowski, I.1    Mulvey, M.R.2    Leco, P.A.3    Borys, A.4    Loewen, P.C.5
  • 46
    • 0023050076 scopus 로고
    • A double staining method for differentiating between two classes of mycobacterial catalase in Polyacrylamide electrophoresis gels
    • Wayne, L. G., and G. A. Diaz. 1986. A double staining method for differentiating between two classes of mycobacterial catalase in Polyacrylamide electrophoresis gels. Anal. Biochem. 157:89-92.
    • (1986) Anal. Biochem , vol.157 , pp. 89-92
    • Wayne, L.G.1    Diaz, G.A.2


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