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Volumn 187, Issue 20, 2005, Pages 7155-7160

YrxA is the transcriptional regulator that represses de novo NAD biosynthesis in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINIC ACID; PROTEIN YRXA; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 26444568675     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.187.20.7155-7160.2005     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 0035853296 scopus 로고    scopus 로고
    • Regulatory potential, phyletic distribution and evolution of ancient, intracellular, small-molecule-binding domains
    • Anantharaman, V., E. V. Koonin, and L. Aravind. 2001. Regulatory potential, phyletic distribution and evolution of ancient, intracellular, small-molecule-binding domains. J. Mol. Biol. 307:1271-1292.
    • (2001) J. Mol. Biol. , vol.307 , pp. 1271-1292
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 4
    • 0016429930 scopus 로고
    • Isolation of a metabolite capable of differentially supporting the growth of nicotinamide adenine dinucleotide auxotrophs of Escherichia coli
    • Chen, J. L., and G. J. Tritz. 1975. Isolation of a metabolite capable of differentially supporting the growth of nicotinamide adenine dinucleotide auxotrophs of Escherichia coli. J. Bacteriol. 121:212-218.
    • (1975) J. Bacteriol. , vol.121 , pp. 212-218
    • Chen, J.L.1    Tritz, G.J.2
  • 5
    • 0002802808 scopus 로고
    • Mutants of Escherichia coli requiring methionine or vitamin B12
    • Davis, B. D., and E. S. Mingioli. 1950. Mutants of Escherichia coli requiring methionine or vitamin B12. J. Bacteriol. 60:17-28.
    • (1950) J. Bacteriol. , vol.60 , pp. 17-28
    • Davis, B.D.1    Mingioli, E.S.2
  • 6
    • 0024058285 scopus 로고
    • Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB
    • Flachmann, R., N. Kunz, J. Seifert, M. Gutlich, F. J. Wientjes, A. Laufer, and H. G. Gassen. 1988. Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB. Eur. J. Biochem. 175:221-228.
    • (1988) Eur. J. Biochem. , vol.175 , pp. 221-228
    • Flachmann, R.1    Kunz, N.2    Seifert, J.3    Gutlich, M.4    Wientjes, F.J.5    Laufer, A.6    Gassen, H.G.7
  • 7
    • 0023355786 scopus 로고
    • Regulation of NAD metabolism in Salmonella typhimurium: Genetic analysis and cloning of the nadR repressor locus
    • Foster, J. W., E. A. Holley-Guthrie, and F. Warren. 1987. Regulation of NAD metabolism in Salmonella typhimurium: genetic analysis and cloning of the nadR repressor locus. Mol. Gen. Genet. 208:279-287.
    • (1987) Mol. Gen. Genet. , vol.208 , pp. 279-287
    • Foster, J.W.1    Holley-Guthrie, E.A.2    Warren, F.3
  • 8
    • 0042060978 scopus 로고    scopus 로고
    • Allosteric regulation of Bacillus subtilis NAD kinase by quinolinic acid
    • Garavaglia, S., A. Galizzi, and M. Rizzi. 2003. Allosteric regulation of Bacillus subtilis NAD kinase by quinolinic acid. J. Bacteriol. 185:4844-4850.
    • (2003) J. Bacteriol. , vol.185 , pp. 4844-4850
    • Garavaglia, S.1    Galizzi, A.2    Rizzi, M.3
  • 10
    • 0016739951 scopus 로고
    • Studies on the de novo biosynthesis of NAD in Escherichia coli. The separation of the nadB gene product from the nadA gene product and its purification
    • Griffith, G. R., J. L. Chandler, and R. K. Gholson. 1975. Studies on the de novo biosynthesis of NAD in Escherichia coli. The separation of the nadB gene product from the nadA gene product and its purification. Eur. J. Biochem. 54:239-245.
    • (1975) Eur. J. Biochem. , vol.54 , pp. 239-245
    • Griffith, G.R.1    Chandler, J.L.2    Gholson, R.K.3
  • 11
    • 16844384577 scopus 로고    scopus 로고
    • Regulation of NAD synthesis by the trifunctional NadR protein of Salmonella enterica
    • Grose, J. H., U. Bergthorsson, and J. R. Roth. 2005. Regulation of NAD synthesis by the trifunctional NadR protein of Salmonella enterica. J. Bacteriol. 187:2774-2782.
    • (2005) J. Bacteriol. , vol.187 , pp. 2774-2782
    • Grose, J.H.1    Bergthorsson, U.2    Roth, J.R.3
  • 12
    • 0022412901 scopus 로고
    • Regulation of NAD biosynthesis in Salmonella typhimurium: Expression of nad-lac gene fusions and identification of a nad regulatory locus
    • Holley, E. A., M. P. Spector, and J. W. Foster. 1985. Regulation of NAD biosynthesis in Salmonella typhimurium: expression of nad-lac gene fusions and identification of a nad regulatory locus. J. Gen. Microbiol. 131: 2759-2770.
    • (1985) J. Gen. Microbiol. , vol.131 , pp. 2759-2770
    • Holley, E.A.1    Spector, M.P.2    Foster, J.W.3
  • 13
    • 0023945746 scopus 로고
    • Structural gene for NAD synthetase in Salmonella typhimurium
    • Hughes, K. T., B. M. Olivera, and J. R. Roth. 1988. Structural gene for NAD synthetase in Salmonella typhimurium. J. Bacteriol. 170:2113-2120.
    • (1988) J. Bacteriol. , vol.170 , pp. 2113-2120
    • Hughes, K.T.1    Olivera, B.M.2    Roth, J.R.3
  • 14
    • 0025814841 scopus 로고
    • A genetic characterization of the nadC gene of Salmonella typhimurium
    • Hughes, K. T., J. R. Roth, and B. M. Olivera. 1991. A genetic characterization of the nadC gene of Salmonella typhimurium. Genetics 127:657-670.
    • (1991) Genetics , vol.127 , pp. 657-670
    • Hughes, K.T.1    Roth, J.R.2    Olivera, B.M.3
  • 18
    • 0001406338 scopus 로고    scopus 로고
    • Structure of L-aspartate oxidase: Implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family
    • Mattevi, A., G. Tedeschi, L. Bacchella, A. Coda, A. Negri, and S. Ronchi. 1999. Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family. Struct. Fold. Des. 7:745-756.
    • (1999) Struct. Fold. Des. , vol.7 , pp. 745-756
    • Mattevi, A.1    Tedeschi, G.2    Bacchella, L.3    Coda, A.4    Negri, A.5    Ronchi, S.6
  • 19
    • 0020080252 scopus 로고
    • L-Aspartate oxidase, a newly discovered enzyme in Escherichia coli, is the B protein of quinolinate synthetase
    • Nasu, S., F. D. Wicks, and R. K. Gholson. 1982. L-Aspartate oxidase, a newly discovered enzyme in Escherichia coli, is the B protein of quinolinate synthetase. J. Biol. Chem. 257:626-632.
    • (1982) J. Biol. Chem. , vol.257 , pp. 626-632
    • Nasu, S.1    Wicks, F.D.2    Gholson, R.K.3
  • 20
  • 22
    • 0000397680 scopus 로고    scopus 로고
    • Biosynthesis and recycling of NAD
    • F. C. Neidhart, R. Curtiss, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter and H. E. Umarger (ed.). American Society for Microbiology, Washington, D.C.
    • Penfound, T., and J. W. Foster. 1996. Biosynthesis and recycling of NAD. p. 721-730. In F. C. Neidhart, R. Curtiss, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter and H. E. Umarger (ed.), Escherichia coli and Salmonella. Cellular and molecular biology, 2nd ed. vol. 1 American Society for Microbiology, Washington, D.C.
    • (1996) Escherichia coli and Salmonella. Cellular and Molecular Biology, 2nd Ed. , vol.1 , pp. 721-730
    • Penfound, T.1    Foster, J.W.2
  • 23
    • 0032925513 scopus 로고    scopus 로고
    • NAD-dependent DNA-binding activity of the bifunctional NadR regulator of Salmonella typhimurium
    • Penfound, T., and J. W. Foster. 1999. NAD-dependent DNA-binding activity of the bifunctional NadR regulator of Salmonella typhimurium. J. Bacteriol. 181:648-655.
    • (1999) J. Bacteriol. , vol.181 , pp. 648-655
    • Penfound, T.1    Foster, J.W.2
  • 24
    • 0002151089 scopus 로고
    • Integrational vectors for genetic manipulation in Bacillus subtilis
    • A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.). American Society for Microbiology, Washington D.C.
    • Perego, M. 1993. Integrational vectors for genetic manipulation in Bacillus subtilis, p. 615-624. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and other gram-positive bacteria: biochemistry, physiology, and molecular genetics. American Society for Microbiology, Washington D.C.
    • (1993) Bacillus Subtilis and Other Gram-Positive Bacteria: Biochemistry, Physiology, and Molecular Genetics , pp. 615-624
    • Perego, M.1
  • 25
    • 0032857728 scopus 로고    scopus 로고
    • The Echerichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltransferase activity
    • Raffaelli, N., T. Lorenzi, P. L. Mariani, M. Emanuelli, A. Amici, S. Ruggieri, and G. Magni. 1999. The Echerichia coli NadR regulator is endowed with nicotinamide mononucleotide adenylyltransferase activity. J. Bacteriol. 181: 5509-5511.
    • (1999) J. Bacteriol. , vol.181 , pp. 5509-5511
    • Raffaelli, N.1    Lorenzi, T.2    Mariani, P.L.3    Emanuelli, M.4    Amici, A.5    Ruggieri, S.6    Magni, G.7
  • 30
    • 0031721044 scopus 로고    scopus 로고
    • Salmonella typhimurium nit is nadE: Defective nitrogen utilization and ammonia-dependent NAD synthetase
    • Schneider, B. L., and L. J. Reitzer. 1998. Salmonella typhimurium nit is nadE: defective nitrogen utilization and ammonia-dependent NAD synthetase. J. Bacteriol. 180:4739-4741.
    • (1998) J. Bacteriol. , vol.180 , pp. 4739-4741
    • Schneider, B.L.1    Reitzer, L.J.2
  • 31
    • 0025364212 scopus 로고
    • Expression of the E. coli nadB gene and characterization of the gene product aspartate oxidase
    • Seifert, J., N. Kunz, R. Flachmann, A. Laufer, K. D. Jany, and H. G. Gassen. 1990. Expression of the E. coli nadB gene and characterization of the gene product aspartate oxidase. Biol. Chem. Hoppe Seyler 371:239-248.
    • (1990) Biol. Chem. Hoppe Seyler , vol.371 , pp. 239-248
    • Seifert, J.1    Kunz, N.2    Flachmann, R.3    Laufer, A.4    Jany, K.D.5    Gassen, H.G.6
  • 32
    • 0027401768 scopus 로고
    • Cloning, nuclcotide sequence, and regulation of the Bacillus subtilis nadB gene and a nifS-like gene, both of which are essential for NAD biosynthesis
    • Sun, D., and P. Setlow. 1993. Cloning, nuclcotide sequence, and regulation of the Bacillus subtilis nadB gene and a nifS-like gene, both of which are essential for NAD biosynthesis. J. Bacteriol. 175:1423-1432.
    • (1993) J. Bacteriol. , vol.175 , pp. 1423-1432
    • Sun, D.1    Setlow, P.2
  • 33
    • 0037446304 scopus 로고    scopus 로고
    • New antibiotics for anthrax?
    • Sutherland, S. 2003. New antibiotics for anthrax? Drug Discov. Today 8: 335-336.
    • (2003) Drug Discov. Today , vol.8 , pp. 335-336
    • Sutherland, S.1
  • 34
    • 0015938087 scopus 로고
    • Studies on the de novo biosynthesis of NAD in Eschericha coli. V. Properties of the quinolinic acid synthetase system
    • Suzuki, N., J. Carlson, G. Griffith, and R. K. Gholson. 1973. Studies on the de novo biosynthesis of NAD in Eschericha coli. V. Properties of the quinolinic acid synthetase system. Biochim. Biophys. Acta 304:309-315.
    • (1973) Biochim. Biophys. Acta , vol.304 , pp. 309-315
    • Suzuki, N.1    Carlson, J.2    Griffith, G.3    Gholson, R.K.4
  • 35
    • 0002275682 scopus 로고    scopus 로고
    • Purine, pyrimidine, and pyridine nuclcotide metabolism
    • A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.). American Society for Microbiology, Washington, D.C.
    • Switzer, R. L., H. Zalkin, and H. H. Saxild. 2002. Purine, pyrimidine, and pyridine nuclcotide metabolism, p. 265-269. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and its closest relatives: from genes to cells. American Society for Microbiology, Washington, D.C.
    • (2002) Bacillus Subtilis and Its Closest Relatives: From Genes to Cells , pp. 265-269
    • Switzer, R.L.1    Zalkin, H.2    Saxild, H.H.3
  • 37
    • 0031737309 scopus 로고    scopus 로고
    • A vector for systematic gene inactivation in Bacillus subtilis
    • Vagner, V., E. Dervyn, and S. D. Ehrlich. 1998. A vector for systematic gene inactivation in Bacillus subtilis. Microbiology 144:3097-3104.
    • (1998) Microbiology , vol.144 , pp. 3097-3104
    • Vagner, V.1    Dervyn, E.2    Ehrlich, S.D.3
  • 38
    • 0026085518 scopus 로고
    • Activity of the nicotinamide mononuclcotide transport system is regulated in Salmonella typhimurium
    • Zhu, N., B. M. Olivera, and J. R. Roth. 1991. Activity of the nicotinamide mononuclcotide transport system is regulated in Salmonella typhimurium. J. Bacteriol. 173:1311-1320.
    • (1991) J. Bacteriol. , vol.173 , pp. 1311-1320
    • Zhu, N.1    Olivera, B.M.2    Roth, J.R.3


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