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Volumn 151, Issue 10, 2005, Pages 3427-3433

Dimeric Brucella abortus Irr protein controls its own expression and binds haem

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; DIMER; HEME; IRON RESPONSE REGULATOR; MUTANT PROTEIN; PROTEIN PRECURSOR; PROTOPORPHYRIN; RECOMBINANT PROTEIN; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 27144460913     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.28213-0     Document Type: Article
Times cited : (39)

References (30)
  • 1
    • 0034819639 scopus 로고    scopus 로고
    • Ferrochelatase is present in Brucella abortus and is critical for its intracellular survival and virulence
    • Almiron, M., Martinez, M., Sanjuan, N. & Ugalde, R. A. (2001). Ferrochelatase is present in Brucella abortus and is critical for its intracellular survival and virulence. Infect Immun 69, 6225-6230.
    • (2001) Infect. Immun. , vol.69 , pp. 6225-6230
    • Almiron, M.1    Martinez, M.2    Sanjuan, N.3    Ugalde, R.A.4
  • 3
    • 0029125099 scopus 로고
    • New gentamicin-resistance and lacZ promoter-probe cassettes suitable for insertion mutagenesis and generation of transcriptional fusions
    • Becker, A., Schmidt, M., Jager, W. & Puhler, A. (1995). New gentamicin-resistance and lacZ promoter-probe cassettes suitable for insertion mutagenesis and generation of transcriptional fusions. Gene 162, 37-39.
    • (1995) Gene , vol.162 , pp. 37-39
    • Becker, A.1    Schmidt, M.2    Jager, W.3    Puhler, A.4
  • 4
    • 0344405678 scopus 로고    scopus 로고
    • Genetic organization and iron-responsive regulation of the Brucella abortus 2,3-dihydroxybenzoic acid biosynthesis operon, a cluster of genes required for wild-type virulence in pregnant cattle
    • Bellaire, B. H., Elzer, P. H., Hagius, S., Walker, J., Baldwin, C. L. & Roop, R. M., 2nd (2003). Genetic organization and iron-responsive regulation of the Brucella abortus 2,3-dihydroxybenzoic acid biosynthesis operon, a cluster of genes required for wild-type virulence in pregnant cattle. Infect Immun 71, 1794-1803.
    • (2003) Infect. Immun. , vol.71 , pp. 1794-1803
    • Bellaire, B.H.1    Elzer, P.H.2    Hagius, S.3    Walker, J.4    Baldwin, C.L.5    Roop II, R.M.6
  • 5
    • 0015542618 scopus 로고
    • Porphyrin-accumulating mutants of Escherichia coli
    • Cox, R. & Charles, H. P. (1973). Porphyrin-accumulating mutants of Escherichia coli. J Bacteriol 113, 122-132.
    • (1973) J. Bacteriol. , vol.113 , pp. 122-132
    • Cox, R.1    Charles, H.P.2
  • 6
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: Transcriptional metalloregulation by the Fur protein
    • Escolar, L., Perez-Martin, J. & de Lorenzo, V. (1999). Opening the iron box: transcriptional metalloregulation by the Fur protein. J Bacteriol 181, 6223-6229.
    • (1999) J. Bacteriol. , vol.181 , pp. 6223-6229
    • Escolar, L.1    Perez-Martin, J.2    de Lorenzo, V.3
  • 7
    • 0026665634 scopus 로고
    • Characterization of a Bradyrhizobium japonicum ferrochelatase mutant and isolation of the hemH gene
    • Frustaci, J. M. & O'Brian, M. R. (1992). Characterization of a Bradyrhizobium japonicum ferrochelatase mutant and isolation of the hemH gene. J Bacteriol 174, 4223-4229.
    • (1992) J. Bacteriol. , vol.174 , pp. 4223-4229
    • Frustaci, J.M.1    O'Brian, M.R.2
  • 8
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron-regulatory protein 2 by the proteasome
    • Guo, B., Phillips, J. D., Yu, Y. & Leibold, E. A. (1995). Iron regulates the intracellular degradation of iron-regulatory protein 2 by the proteasome. J Biol Chem 270, 21645-21651.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21645-21651
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 9
    • 0032555562 scopus 로고    scopus 로고
    • The bacterial Irr protein is required for coordination of heme biosynthesis with iron availability
    • Hamza, I., Chauhan, S., Hassett, R. & O'Brian, M. R. (1998). The bacterial Irr protein is required for coordination of heme biosynthesis with iron availability. J Biol Chem 273, 21669-21674.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21669-21674
    • Hamza, I.1    Chauhan, S.2    Hassett, R.3    O'Brian, M.R.4
  • 10
    • 0034062506 scopus 로고    scopus 로고
    • Fur-independent regulation of iron metabolism by Irr in Bradyrhizobium japonicum
    • Hamza, I., Qi, Z., King, N. D. & O'Brian, M. R. (2000). Fur-independent regulation of iron metabolism by Irr in Bradyrhizobium japonicum. Microbiology 146, 669-676.
    • (2000) Microbiology , vol.146 , pp. 669-676
    • Hamza, I.1    Qi, Z.2    King, N.D.3    O'Brian, M.R.4
  • 11
    • 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 & 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 II, R.M.6    Peterson, K.M.7
  • 12
    • 0033709980 scopus 로고    scopus 로고
    • Identification and characterization of in vivo attenuated mutants of Brucella melitensis
    • 7 other authors
    • Lestrate, P., Delrue, R. M., Danese, I. & 7 other authors (2000). Identification and characterization of in vivo attenuated mutants of Brucella melitensis. Mol Microbiol 38, 543-551.
    • (2000) Mol. Microbiol. , vol.38 , pp. 543-551
    • Lestrate, P.1    Delrue, R.M.2    Danese, I.3
  • 13
    • 0026492054 scopus 로고
    • Identification of 2,3-dihydroxybenzoic acid as a Brucella abortus siderophore
    • Lopez-Goñi, I., Moriyón, I. & Neilands, J. B. (1992). Identification of 2,3-dihydroxybenzoic acid as a Brucella abortus siderophore. Infect Immun 60, 4496-4503.
    • (1992) Infect. Immun. , vol.60 , pp. 4496-4503
    • Lopez-Goñi, I.1    Moriyón, I.2    Neilands, J.B.3
  • 15
    • 0035985617 scopus 로고    scopus 로고
    • Biochemistry, regulation and genomics of haem biosynthesis in prokaryotes
    • O'Brian, M. R. & Thony-Meyer, L. (2002). Biochemistry, regulation and genomics of haem biosynthesis in prokaryotes. Adv Microb Physiol 46, 257-318.
    • (2002) Adv. Microb. Physiol. , vol.46 , pp. 257-318
    • O'Brian, M.R.1    Thony-Meyer, L.2
  • 16
    • 17944372665 scopus 로고    scopus 로고
    • Heme mediates derepression of Maf recognition element through direct binding to transcription repressor Bach1
    • 8 other authors
    • Ogawa, K., Sun, J., Taketani, S. & 8 other authors (2001). Heme mediates derepression of Maf recognition element through direct binding to transcription repressor Bach1. EMBO J 20, 2835-2843.
    • (2001) EMBO J. , vol.20 , pp. 2835-2843
    • Ogawa, K.1    Sun, J.2    Taketani, S.3
  • 17
    • 0019469231 scopus 로고
    • Nucleotide sequence of the kanamycin resistance transposon Tn903
    • Oka, A., Sugisaki, H. & Takanami, M. (1981). Nucleotide sequence of the kanamycin resistance transposon Tn903. J Mol Biol 147, 217-226.
    • (1981) J. Mol. Biol. , vol.147 , pp. 217-226
    • Oka, A.1    Sugisaki, H.2    Takanami, M.3
  • 18
    • 0036791011 scopus 로고    scopus 로고
    • The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts
    • & 28 other authors
    • Paulsen, I. T., Seshadri, R., Nelson, K. E. & 28 other authors (2002). The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts. Proc Natl Acad Sci U S A 99, 13148-13153.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13148-13153
    • Paulsen, I.T.1    Seshadri, R.2    Nelson, K.E.3
  • 19
    • 0024979286 scopus 로고
    • Functional dissection and sequence of yeast HAP1 activator
    • Pfeifer, K., Kim, K. S., Kogan, S. & Guarente, L. (1989). Functional dissection and sequence of yeast HAP1 activator. Cell 56, 291-301.
    • (1989) Cell , vol.56 , pp. 291-301
    • Pfeifer, K.1    Kim, K.S.2    Kogan, S.3    Guarente, L.4
  • 20
    • 0344321893 scopus 로고    scopus 로고
    • Architecture of a protein central to iron homeostasis: Crystal structure and spectroscopic analysis of the ferric uptake regulator
    • Pohl, E., Haller, J. C., Mijovilovich, A., Meyer-Klaucke, W., Garman, E. & Vasil, M. L. (2003). Architecture of a protein central to iron homeostasis: crystal structure and spectroscopic analysis of the ferric uptake regulator. Mol Microbiol 47, 903-915.
    • (2003) Mol. Microbiol. , vol.47 , pp. 903-915
    • Pohl, E.1    Haller, J.C.2    Mijovilovich, A.3    Meyer-Klaucke, W.4    Garman, E.5    Vasil, M.L.6
  • 21
    • 0036161801 scopus 로고    scopus 로고
    • Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis
    • Qi, Z. & O'Brian, M. R. (2002). Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis. Mol Cell 9, 155-162.
    • (2002) Mol. Cell , vol.9 , pp. 155-162
    • Qi, Z.1    O'Brian, M.R.2
  • 22
    • 0033539642 scopus 로고    scopus 로고
    • Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein
    • Qi, Z., Hamza, I. & O'Brian, M. R. (1999). Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein. Proc Natl Acad Sci U S A 96, 13056-13061.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13056-13061
    • Qi, Z.1    Hamza, I.2    O'Brian, M.R.3
  • 25
    • 0028960213 scopus 로고
    • Functional domains of the Escherichia coli ferric uptake regulator protein (Fur)
    • Stojiljkovic, I. & Hantke, K. (1995). Functional domains of the Escherichia coli ferric uptake regulator protein (Fur). Mol Gen Genet 247, 199-205.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 199-205
    • Stojiljkovic, I.1    Hantke, K.2
  • 26
    • 0032762171 scopus 로고    scopus 로고
    • Intracellular lifestyle of Brucella spp. Common genes with other animal pathogens, plant pathogens, and endosymbionts
    • Ugalde, R. A. (1999). Intracellular lifestyle of Brucella spp. Common genes with other animal pathogens, plant pathogens, and endosymbionts. Microbes Infect 1, 1211-1219.
    • (1999) Microbes. Infect. , vol.1 , pp. 1211-1219
    • Ugalde, R.A.1
  • 29
    • 14844355242 scopus 로고    scopus 로고
    • Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein
    • Yang, J., Ishimori, K. & O'Brian, M. R. (2005). Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein. J Biol Chem 280, 7671-7676.
    • (2005) J. Biol. Chem. , vol.280 , pp. 7671-7676
    • Yang, J.1    Ishimori, K.2    O'Brian, M.R.3
  • 30
    • 0028821439 scopus 로고
    • Heme binds to a short sequence that serves a regulatory function in diverse proteins
    • Zhang, L. & Guarente, L. (1995). Heme binds to a short sequence that serves a regulatory function in diverse proteins. EMBO J 14, 313-320.
    • (1995) EMBO J. , vol.14 , pp. 313-320
    • Zhang, L.1    Guarente, L.2


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