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Volumn 194, Issue 5, 2012, Pages 1145-1157

Transcriptional regulation of central carbon and energy metabolism in bacteria by redox-responsive repressor rex

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; REX PROTEIN;

EID: 84863285072     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.06412-11     Document Type: Article
Times cited : (112)

References (40)
  • 1
    • 3543068251 scopus 로고    scopus 로고
    • Regulog analysis: detection of conserved regulatory networks across bacteria: application to Staphylococcus aureus
    • Alkema WB, Lenhard B, Wasserman WW. 2004. Regulog analysis: detection of conserved regulatory networks across bacteria: application to Staphylococcus aureus. Genome Res. 14:1362-1373.
    • (2004) Genome Res. , vol.14 , pp. 1362-1373
    • Alkema, W.B.1    Lenhard, B.2    Wasserman, W.W.3
  • 2
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul SF, et al. 1997. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 3
    • 79958856251 scopus 로고    scopus 로고
    • Transcriptional repressor Rex is involved in regulation of oxidative stress response and biofilm formation by Streptococcus mutans
    • Bitoun JP, Nguyen AH, Fan Y, Burne RA, Wen ZT. 2011. Transcriptional repressor Rex is involved in regulation of oxidative stress response and biofilm formation by Streptococcus mutans. FEMS Microbiol. Lett. 320:110-117.
    • (2011) FEMS Microbiol. Lett. , vol.320 , pp. 110-117
    • Bitoun, J.P.1    Nguyen, A.H.2    Fan, Y.3    Burne, R.A.4    Wen, Z.T.5
  • 4
    • 0141737064 scopus 로고    scopus 로고
    • + redox poise in Streptomyces coelicolor A3(2)
    • + redox poise in Streptomyces coelicolor A3(2). EMBO J. 22:4856-4865.
    • (2003) EMBO J. , vol.22 , pp. 4856-4865
    • Brekasis, D.1    Paget, M.S.2
  • 5
    • 0028144995 scopus 로고
    • Purification, characterization and properties of an NADH oxidase from Desulfovibrio vulgaris (Hildenborough) and its coupling to adenylyl phosphosulfate reductase
    • Chen L, Le Gall J, Xavier AV. 1994. Purification, characterization and properties of an NADH oxidase from Desulfovibrio vulgaris (Hildenborough) and its coupling to adenylyl phosphosulfate reductase. Biochem. Biophys. Res. Commun. 203:839-844.
    • (1994) Biochem. Biophys. Res. Commun. , vol.203 , pp. 839-844
    • Chen, L.1    Le Gall, J.2    Xavier, A.V.3
  • 6
    • 33750041322 scopus 로고    scopus 로고
    • Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species
    • Conners SB, et al. 2006. Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species. FEMS Microbiol. Rev. 30:872-905.
    • (2006) FEMS Microbiol. Rev. , vol.30 , pp. 872-905
    • Conners, S.B.1
  • 8
    • 75549088819 scopus 로고    scopus 로고
    • MicrobesOnline: an integrated portal for comparative and functional genomics
    • Dehal PS, et al. 2010. MicrobesOnline: an integrated portal for comparative and functional genomics. Nucleic Acids Res. 38:D396-D400.
    • (2010) Nucleic Acids Res. , vol.38
    • Dehal, P.S.1
  • 9
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32:1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 10
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0
    • Guindon S, et al. 2010. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst. Biol. 59:307-321.
    • (2010) Syst. Biol. , vol.59 , pp. 307-321
    • Guindon, S.1
  • 11
    • 33749588803 scopus 로고    scopus 로고
    • Regulatory loop between redox sensing of the NADH/NAD(+) ratio by Rex (YdiH) and oxidation of NADH by NADH dehydrogenase Ndh in Bacillus subtilis
    • Gyan S, Shiohira Y, Sato I, Takeuchi M, Sato T. 2006. Regulatory loop between redox sensing of the NADH/NAD(+) ratio by Rex (YdiH) and oxidation of NADH by NADH dehydrogenase Ndh in Bacillus subtilis. J. Bacteriol. 188:7062-7071.
    • (2006) J. Bacteriol. , vol.188 , pp. 7062-7071
    • Gyan, S.1    Shiohira, Y.2    Sato, I.3    Takeuchi, M.4    Sato, T.5
  • 12
    • 80053902441 scopus 로고    scopus 로고
    • Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor
    • Hung YP, Albeck JG, Tantama M, Yellen G. 2011. Imaging cytosolic NADH-NAD(+) redox state with a genetically encoded fluorescent biosensor. Cell Metab. 14:545-554.
    • (2011) Cell Metab. , vol.14 , pp. 545-554
    • Hung, Y.P.1    Albeck, J.G.2    Tantama, M.3    Yellen, G.4
  • 13
    • 38649092410 scopus 로고    scopus 로고
    • Dendroscope: an interactive viewer for large phylogenetic trees
    • Huson DH, et al. 2007. Dendroscope: an interactive viewer for large phylogenetic trees. BMC Bioinform. 8:460.
    • (2007) BMC Bioinform. , vol.8 , pp. 460
    • Huson, D.H.1
  • 14
    • 0002226697 scopus 로고
    • Catabolism of malate and related dicarboxylic acids in various Desulfovibrio strains and the involvement of an oxygen-labile NADPH dehydrogenase
    • Kremer DR, Nienhuis-Kuiper HE, Timmer CJ, Hansen TA. 1989. Catabolism of malate and related dicarboxylic acids in various Desulfovibrio strains and the involvement of an oxygen-labile NADPH dehydrogenase. Arch. Microbiol. 151:34-39.
    • (1989) Arch. Microbiol. , vol.151 , pp. 34-39
    • Kremer, D.R.1    Nienhuis-Kuiper, H.E.2    Timmer, C.J.3    Hansen, T.A.4
  • 15
    • 27144540194 scopus 로고    scopus 로고
    • Coordinated patterns of cytochrome bd and lactate dehydrogenase expression in Bacillus subtilis
    • Larsson JT, Rogstam A, von Wachenfeldt C. 2005. Coordinated patterns of cytochrome bd and lactate dehydrogenase expression in Bacillus subtilis. Microbiology 151:3323-3335.
    • (2005) Microbiology , vol.151 , pp. 3323-3335
    • Larsson, J.T.1    Rogstam, A.2    von Wachenfeldt, C.3
  • 16
    • 80053915498 scopus 로고    scopus 로고
    • Control of proteobacterial central carbon metabolism by the HexR transcriptional regulator: a case study in Shewanella oneidensis
    • Leyn SA, et al. 2011. Control of proteobacterial central carbon metabolism by the HexR transcriptional regulator: a case study in Shewanella oneidensis. J. Biol. Chem. 286:35782-35794.
    • (2011) J. Biol. Chem. , vol.286 , pp. 35782-35794
    • Leyn, S.A.1
  • 17
    • 77952569775 scopus 로고    scopus 로고
    • Structural basis for NADH/NAD+ redox sensing by a Rex family repressor
    • McLaughlin KJ, et al. 2010. Structural basis for NADH/NAD+ redox sensing by a Rex family repressor. Mol. Cell 38:563-575.
    • (2010) Mol. Cell , vol.38 , pp. 563-575
    • McLaughlin, K.J.1
  • 19
    • 0033638223 scopus 로고    scopus 로고
    • Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
    • Mossessova E, Lima CD. 2000. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell 5:865-876.
    • (2000) Mol. Cell , vol.5 , pp. 865-876
    • Mossessova, E.1    Lima, C.D.2
  • 20
    • 33846202958 scopus 로고    scopus 로고
    • Crystal structure of TTHA1657 (AT-rich DNA-binding protein; p25) from Thermus thermophilus HB8 at 2.16 A resolution
    • Nakamura A, Sosa A, Komori H, Kita A, Miki K. 2007. Crystal structure of TTHA1657 (AT-rich DNA-binding protein; p25) from Thermus thermophilus HB8 at 2.16 A resolution. Proteins 66:755-759.
    • (2007) Proteins , vol.66 , pp. 755-759
    • Nakamura, A.1    Sosa, A.2    Komori, H.3    Kita, A.4    Miki, K.5
  • 21
    • 75549086541 scopus 로고    scopus 로고
    • RegPrecise: a database of curated genomic inferences of transcriptional regulatory interactions in prokaryotes
    • Novichkov PS, et al. 2010. RegPrecise: a database of curated genomic inferences of transcriptional regulatory interactions in prokaryotes. Nucleic Acids Res. 38:D111-D118.
    • (2010) Nucleic Acids Res. , vol.38
    • Novichkov, P.S.1
  • 22
    • 77954254495 scopus 로고    scopus 로고
    • RegPredict: an integrated system for regulon inference in prokaryotes by comparative genomics approach
    • Novichkov PS, et al. 2010. RegPredict: an integrated system for regulon inference in prokaryotes by comparative genomics approach. Nucleic Acids Res. 38:W299-W307.
    • (2010) Nucleic Acids Res. , vol.38
    • Novichkov, P.S.1
  • 23
    • 0028853811 scopus 로고
    • Domain organization and a protease-sensitive loop in eukaryotic ornithine decarboxylase
    • Osterman AL, et al. 1995. Domain organization and a protease-sensitive loop in eukaryotic ornithine decarboxylase. Biochemistry 34:13431-13436.
    • (1995) Biochemistry , vol.34 , pp. 13431-13436
    • Osterman, A.L.1
  • 24
    • 25644458211 scopus 로고    scopus 로고
    • The subsystems approach to genome annotation and its use in the project to annotate 1,000 genomes
    • Overbeek R, et al. 2005. The subsystems approach to genome annotation and its use in the project to annotate 1,000 genomes. Nucleic Acids Res. 33:5691-5702.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5691-5702
    • Overbeek, R.1
  • 25
    • 77952821682 scopus 로고    scopus 로고
    • Redox sensing by a Rex-family repressor is involved in the regulation of anaerobic gene expression in Staphylococcus aureus
    • Pagels M, et al. 2010. Redox sensing by a Rex-family repressor is involved in the regulation of anaerobic gene expression in Staphylococcus aureus. Mol. Microbiol. 76:1142-1161.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1142-1161
    • Pagels, M.1
  • 26
    • 79952108090 scopus 로고    scopus 로고
    • The mechanism for regulating ethanol fermentation by redox levels in Thermoanaerobacter ethanolicus
    • Pei J, et al. 2011. The mechanism for regulating ethanol fermentation by redox levels in Thermoanaerobacter ethanolicus. Metab. Eng. 13:186-193.
    • (2011) Metab. Eng. , vol.13 , pp. 186-193
    • Pei, J.1
  • 27
    • 77956281182 scopus 로고    scopus 로고
    • Structural and operational complexity of the Geobacter sulfurreducens genome
    • Qiu Y, et al. 2010. Structural and operational complexity of the Geobacter sulfurreducens genome. Genome Res. 20:1304-1311.
    • (2010) Genome Res. , vol.20 , pp. 1304-1311
    • Qiu, Y.1
  • 28
    • 34548219522 scopus 로고    scopus 로고
    • Comparative genomic reconstruction of transcriptional regulatory networks in bacteria
    • Rodionov DA. 2007. Comparative genomic reconstruction of transcriptional regulatory networks in bacteria. Chem.Rev. 107:3467-3497.
    • (2007) Chem.Rev. , vol.107 , pp. 3467-3497
    • Rodionov, D.A.1
  • 29
    • 41849121949 scopus 로고    scopus 로고
    • Transcriptional regulation of NAD metabolism in bacteria: NrtR family of Nudix-related regulators
    • Rodionov DA, et al. 2008. Transcriptional regulation of NAD metabolism in bacteria: NrtR family of Nudix-related regulators. Nucleic Acids Res. 36:2047-2059.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2047-2059
    • Rodionov, D.A.1
  • 30
    • 41849131511 scopus 로고    scopus 로고
    • Transcriptional regulation of NAD metabolism in bacteria: genomic reconstruction of NiaR (YrxA) regulon
    • Rodionov DA, et al. 2008. Transcriptional regulation of NAD metabolism in bacteria: genomic reconstruction of NiaR (YrxA) regulon. Nucleic Acids Res. 36:2032-2046.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2032-2046
    • Rodionov, D.A.1
  • 31
    • 79958842141 scopus 로고    scopus 로고
    • Comparative genomic reconstruction of transcriptional networks controlling central metabolism in the Shewanella genus
    • Rodionov DA, et al. 2011. Comparative genomic reconstruction of transcriptional networks controlling central metabolism in the Shewanella genus. BMC Genomics 12(Suppl. 1):S3.
    • (2011) BMC Genomics , vol.12 , Issue.SUPPL. 1
    • Rodionov, D.A.1
  • 32
    • 3042857779 scopus 로고    scopus 로고
    • Bacillus subtilis YdiH is a direct negative regulator of the cydABCD operon
    • Schau M, Chen Y, Hulett FM. 2004. Bacillus subtilis YdiH is a direct negative regulator of the cydABCD operon. J. Bacteriol. 186:4585-4595.
    • (2004) J. Bacteriol. , vol.186 , pp. 4585-4595
    • Schau, M.1    Chen, Y.2    Hulett, F.M.3
  • 33
    • 11844285686 scopus 로고    scopus 로고
    • X-ray structure of a Rex-family repressor/NADH complex insights into the mechanism of redox sensing
    • Sickmier EA, et al. 2005. X-ray structure of a Rex-family repressor/NADH complex insights into the mechanism of redox sensing. Structure 13:43-45.
    • (2005) Structure , vol.13 , pp. 43-45
    • Sickmier, E.A.1
  • 34
    • 0037405823 scopus 로고    scopus 로고
    • Characterization of the minimalDNAbinding domain of the human papillomavirus e1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant protein
    • Titolo S, Brault K, Majewski J, White PW, Archambault J. 2003. Characterization of the minimalDNAbinding domain of the human papillomavirus e1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant protein. J. Virol. 77:5178-5191.
    • (2003) J. Virol. , vol.77 , pp. 5178-5191
    • Titolo, S.1    Brault, K.2    Majewski, J.3    White, P.W.4    Archambault, J.5
  • 35
    • 47249112605 scopus 로고    scopus 로고
    • Structure and functional properties of the Bacillus subtilis transcriptional repressor Rex
    • Wang E, et al. 2008. Structure and functional properties of the Bacillus subtilis transcriptional repressor Rex. Mol. Microbiol. 69:466-478.
    • (2008) Mol. Microbiol. , vol.69 , pp. 466-478
    • Wang, E.1
  • 36
    • 79955031175 scopus 로고    scopus 로고
    • Small-angle X-ray scattering study of a Rex family repressor: conformational response to NADH and NAD+ binding in solution
    • Wang E, et al. 2011. Small-angle X-ray scattering study of a Rex family repressor: conformational response to NADH and NAD+ binding in solution. J. Mol. Biol. 408:670-683.
    • (2011) J. Mol. Biol. , vol.408 , pp. 670-683
    • Wang, E.1
  • 37
    • 11844249971 scopus 로고    scopus 로고
    • Oxygen, metabolism, and gene expression: the T-Rex connection
    • Wood MJ, Storz G. 2005. Oxygen, metabolism, and gene expression: the T-Rex connection. Structure 13:2-4.
    • (2005) Structure , vol.13 , pp. 2-4
    • Wood, M.J.1    Storz, G.2
  • 38
    • 39749093113 scopus 로고    scopus 로고
    • Glycerate 2-kinase of Thermotoga maritima and genomic reconstruction of related metabolic pathways
    • Yang C, Rodionov DA, Rodionova IA, Li X, Osterman AL. 2008. Glycerate 2-kinase of Thermotoga maritima and genomic reconstruction of related metabolic pathways. J. Bacteriol. 190:1773-1782.
    • (2008) J. Bacteriol. , vol.190 , pp. 1773-1782
    • Yang, C.1    Rodionov, D.A.2    Rodionova, I.A.3    Li, X.4    Osterman, A.L.5
  • 39
    • 80053898694 scopus 로고    scopus 로고
    • Genetically encoded fluorescent sensors for intracellular NADH detection
    • Zhao Y, et al. 2011. Genetically encoded fluorescent sensors for intracellular NADH detection. Cell Metab. 14:555-566.
    • (2011) Cell Metab. , vol.14 , pp. 555-566
    • Zhao, Y.1
  • 40
    • 65249126970 scopus 로고    scopus 로고
    • On the chimeric nature, thermophilic origin, and phylogenetic placement of the Thermotogales
    • Zhaxybayeva O, et al. 2009. On the chimeric nature, thermophilic origin, and phylogenetic placement of the Thermotogales. Proc. Natl. Acad. Sci. U. S. A. 106:5865-5870.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 5865-5870
    • Zhaxybayeva, O.1


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