메뉴 건너뛰기




Volumn 181, Issue 19, 1999, Pages 6092-6097

Characterization of a group of anaerobically induced, fnr-dependent genes of Salmonella typhimurium

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID; DNA; PROPIONIC ACID DERIVATIVE;

EID: 0032862459     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.181.19.6092-6097.1999     Document Type: Article
Times cited : (19)

References (49)
  • 1
    • 0025732327 scopus 로고
    • Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: Characterization of the dipeptide permease (Dpp) and the dipeptide-binding protein
    • Abouhamad, W. N., M. Manson, M. M. Gibson, and C. F. Higgins. 1991. Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: characterization of the dipeptide permease (Dpp) and the dipeptide-binding protein. Mol. Microbiol. 5:1035-1047.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1035-1047
    • Abouhamad, W.N.1    Manson, M.2    Gibson, M.M.3    Higgins, C.F.4
  • 2
    • 0024324714 scopus 로고
    • Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli
    • Alefounder, P. R., and R. N. Perham. 1989. Identification, molecular cloning and sequence analysis of a gene cluster encoding the class II fructose 1,6-bisphosphate aldolase, 3-phosphoglycerate kinase and a putative second glyceraldehyde 3-phosphate dehydrogenase of Escherichia coli. Mol. Microbiol. 3:723-732.
    • (1989) Mol. Microbiol. , vol.3 , pp. 723-732
    • Alefounder, P.R.1    Perham, R.N.2
  • 3
    • 0022532411 scopus 로고
    • Oxygen-regulated stimulons of Salmonella typhimurium identified by Mud(Ap lac) operon fusions
    • Aliabadi, Z., F. Warren, S. Mya, and J. W. Foster. 1986. Oxygen-regulated stimulons of Salmonella typhimurium identified by Mud(Ap lac) operon fusions. J. Bacteriol. 165:780-786.
    • (1986) J. Bacteriol. , vol.165 , pp. 780-786
    • Aliabadi, Z.1    Warren, F.2    Mya, S.3    Foster, J.W.4
  • 5
    • 0025881987 scopus 로고
    • Regulation of the chlA locus of Escherichia coli K12: Involvement of molybdenum cofactor
    • Baker, K. P., and D. H. Boxer. 1991. Regulation of the chlA locus of Escherichia coli K12: involvement of molybdenum cofactor. Mol. Microbiol. 5:901-907.
    • (1991) Mol. Microbiol. , vol.5 , pp. 901-907
    • Baker, K.P.1    Boxer, D.H.2
  • 6
    • 0024369036 scopus 로고
    • Nucleotide sequence of the FNR-regulated fumarase gene (fumB) of Escherichia coli K-12
    • Bell, P. J., S. C. Andrews, M. N. Sivak, and J. R. Guest. 1989. Nucleotide sequence of the FNR-regulated fumarase gene (fumB) of Escherichia coli K-12. J. Bacteriol. 171:3494-3503.
    • (1989) J. Bacteriol. , vol.171 , pp. 3494-3503
    • Bell, P.J.1    Andrews, S.C.2    Sivak, M.N.3    Guest, J.R.4
  • 7
    • 0024114971 scopus 로고
    • Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli
    • Bilous, P. T., S. T. Cole, W. F. Anderson, and J. H. Weiner. 1988. Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli. Mol. Microbiol. 2:785-795.
    • (1988) Mol. Microbiol. , vol.2 , pp. 785-795
    • Bilous, P.T.1    Cole, S.T.2    Anderson, W.F.3    Weiner, J.H.4
  • 8
    • 0029589284 scopus 로고
    • Five promoters integrate control of the cob/pdu regulon in Salmonella typhimurium
    • Chen, P., M. Ailion, T. Bobik, G. Storomo, and J. Roth. 1995. Five promoters integrate control of the cob/pdu regulon in Salmonella typhimurium. J. Bacteriol. 177:5401-5410.
    • (1995) J. Bacteriol. , vol.177 , pp. 5401-5410
    • Chen, P.1    Ailion, M.2    Bobik, T.3    Storomo, G.4    Roth, J.5
  • 9
    • 0026056114 scopus 로고
    • Anaerobically expressed Escherichia coli genes identified by operon fusion techniques
    • Choe, M., and W. S. Reznikoff. 1991. Anaerobically expressed Escherichia coli genes identified by operon fusion techniques. J. Bacteriol. 173:6139-6146.
    • (1991) J. Bacteriol. , vol.173 , pp. 6139-6146
    • Choe, M.1    Reznikoff, W.S.2
  • 10
    • 0027465165 scopus 로고
    • Identification of the regulatory sequence of anaerobically expressed locus aeg-46.5
    • Choe, M., and W. S. Reznikoff. 1993. Identification of the regulatory sequence of anaerobically expressed locus aeg-46.5. J. Bacteriol. 175:1165-1172.
    • (1993) J. Bacteriol. , vol.175 , pp. 1165-1172
    • Choe, M.1    Reznikoff, W.S.2
  • 11
    • 0024397725 scopus 로고
    • Oxygen, nitrate, and molybdenum regulation of dmsABC gene expression in Escherichia coli
    • Cotter, P. A., and R P. Gunsalus. 1989. Oxygen, nitrate, and molybdenum regulation of dmsABC gene expression in Escherichia coli. J. Bacteriol. 171: 3817-3823.
    • (1989) J. Bacteriol. , vol.171 , pp. 3817-3823
    • Cotter, P.A.1    Gunsalus, R.P.2
  • 12
    • 0027446537 scopus 로고
    • Transport of 5-aminolevulinic acid by the dipeptide permease in Salmonella typhimurium
    • Elliott, T. 1993. Transport of 5-aminolevulinic acid by the dipeptide permease in Salmonella typhimurium. J. Bacteriol. 175:325-331.
    • (1993) J. Bacteriol. , vol.175 , pp. 325-331
    • Elliott, T.1
  • 13
    • 0026802544 scopus 로고
    • Anaerobic fumarate transport in Escherichia coli by an fnr-dependent dicarboxylate uptake system which is different from the aerobic dicarboxylate uptake system
    • Engel, P., R. Kramer, and G. Unden. 1992. Anaerobic fumarate transport in Escherichia coli by an fnr-dependent dicarboxylate uptake system which is different from the aerobic dicarboxylate uptake system. J. Bacteriol. 174: 5533-5539.
    • (1992) J. Bacteriol. , vol.174 , pp. 5533-5539
    • Engel, P.1    Kramer, R.2    Unden, G.3
  • 14
    • 0021193852 scopus 로고
    • Genetic characterization and molecular cloning of the tripeptide permease (tpp) genes of Salmonella typhimurium
    • Gibson, M. M., M. Price, and C. F. Higgins. 1984. Genetic characterization and molecular cloning of the tripeptide permease (tpp) genes of Salmonella typhimurium. J. Bacteriol. 160:122-130.
    • (1984) J. Bacteriol. , vol.160 , pp. 122-130
    • Gibson, M.M.1    Price, M.2    Higgins, C.F.3
  • 15
    • 0030033752 scopus 로고    scopus 로고
    • Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm
    • Grove, J., S. Tanapongpipat, G. Thomas, L. Griffiths, H. Crooke, and J. Cole. 1996. Escherichia coli K-12 genes essential for the synthesis of c-type cytochromes and a third nitrate reductase located in the periplasm. Mol. Microbiol. 19:467-481.
    • (1996) Mol. Microbiol. , vol.19 , pp. 467-481
    • Grove, J.1    Tanapongpipat, S.2    Thomas, G.3    Griffiths, L.4    Crooke, H.5    Cole, J.6
  • 16
  • 17
    • 0014589126 scopus 로고
    • Compounds which serve as sole source of carbon or nitrogen for Salmonella typhimurium LT2
    • Gutnick, D., J. M. Calvo, T. Klopotowski, and B. N. Ames. 1969. Compounds which serve as sole source of carbon or nitrogen for Salmonella typhimurium LT2. J. Bacteriol. 100:215-219.
    • (1969) J. Bacteriol. , vol.100 , pp. 215-219
    • Gutnick, D.1    Calvo, J.M.2    Klopotowski, T.3    Ames, B.N.4
  • 18
    • 0021074501 scopus 로고
    • Periplasmic protein associated with the oligopeptide permeases of Salmonella typhimurium and Escherichia coli
    • Higgins, C. F., and M. M. Hardie. 1983. Periplasmic protein associated with the oligopeptide permeases of Salmonella typhimurium and Escherichia coli. J. Bacteriol. 155:1434-1438.
    • (1983) J. Bacteriol. , vol.155 , pp. 1434-1438
    • Higgins, C.F.1    Hardie, M.M.2
  • 19
    • 0025761156 scopus 로고
    • ERIC sequences: A novel family of repetitive elements in the genomes of Escherichia coli, Salmonella typhimurium and other enterobacteria
    • Hulton, C. S., C. F. Higgins, and P. M. Sharp. 1991. ERIC sequences: a novel family of repetitive elements in the genomes of Escherichia coli, Salmonella typhimurium and other enterobacteria. Mol. Microbiol. 5:825-834.
    • (1991) Mol. Microbiol. , vol.5 , pp. 825-834
    • Hulton, C.S.1    Higgins, C.F.2    Sharp, P.M.3
  • 22
    • 0030695304 scopus 로고    scopus 로고
    • FNR is a direct oxygen sensor having a biphasic response curve
    • Jordan, P. A., A. J. Thomson, E. T. Ralph, J. R. Guest, and J. Green. 1997. FNR is a direct oxygen sensor having a biphasic response curve. FEBS Lett. 416:349-352.
    • (1997) FEBS Lett. , vol.416 , pp. 349-352
    • Jordan, P.A.1    Thomson, A.J.2    Ralph, E.T.3    Guest, J.R.4    Green, J.5
  • 23
    • 0023186448 scopus 로고
    • Genetic analysis in Salmonella typhimurium with a small collection of randomly spaced insertions of transposon Tn10Δ16Δ17
    • Kukral, A. M., K. L. Strauch, R. A. Maurer, and C. G. Miller. 1987. Genetic analysis in Salmonella typhimurium with a small collection of randomly spaced insertions of transposon Tn10Δ16Δ17. J. Bacteriol. 169:1787-1793.
    • (1987) J. Bacteriol. , vol.169 , pp. 1787-1793
    • Kukral, A.M.1    Strauch, K.L.2    Maurer, R.A.3    Miller, C.G.4
  • 24
    • 0030029817 scopus 로고    scopus 로고
    • DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen
    • Lazazzera, B. A., H. Beinert, N. Khoroshilova, M. C. Kennedy, and P. J. Kiley. 1996. DNA binding and dimerization of the Fe-S-containing FNR protein from Escherichia coli are regulated by oxygen. J. Biol. Chem. 271: 2762-2768.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2762-2768
    • Lazazzera, B.A.1    Beinert, H.2    Khoroshilova, N.3    Kennedy, M.C.4    Kiley, P.J.5
  • 25
    • 0030904024 scopus 로고    scopus 로고
    • Regulation of the Salmonella typhimurium pepT gene by cyclic AMP receptor protein (CRP) and FNR acting at a hybrid CRP-FNR site
    • Lombardo, M.-J., A. A. Lee, T. M. Knox, and C. G. Miller. 1997. Regulation of the Salmonella typhimurium pepT gene by cyclic AMP receptor protein (CRP) and FNR acting at a hybrid CRP-FNR site. J. Bacteriol. 179:1909-1917.
    • (1997) J. Bacteriol. , vol.179 , pp. 1909-1917
    • Lombardo, M.-J.1    Lee, A.A.2    Knox, T.M.3    Miller, C.G.4
  • 26
    • 0021182323 scopus 로고
    • Functional interchangeability of DNA replication genes in Salmonella typhimurium and Escherichia coli demonstrated by a general complementation procedure
    • Maurer, R., B. C. Osmond, E. Shekhtman, A. Wong, and D. Botstein. 1984. Functional interchangeability of DNA replication genes in Salmonella typhimurium and Escherichia coli demonstrated by a general complementation procedure. Genetics 108:1-23.
    • (1984) Genetics , vol.108 , pp. 1-23
    • Maurer, R.1    Osmond, B.C.2    Shekhtman, E.3    Wong, A.4    Botstein, D.5
  • 29
    • 0003582512 scopus 로고
    • A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence
    • Miller, S. I., A. M. Kukral, and J. J. Mekalanos. 1989. A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence. Proc. Natl. Acad. Sci. USA 86:5054-5058.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5054-5058
    • Miller, S.I.1    Kukral, A.M.2    Mekalanos, J.J.3
  • 30
    • 0027482679 scopus 로고
    • The nik operon of Escherichia coli encodes a periplasmic binding-protein-dependent transport system for nickel
    • Navarro, C., L. F. Wu, and M. A. Mandrand-Berthelot. 1993. The nik operon of Escherichia coli encodes a periplasmic binding-protein-dependent transport system for nickel. Mol. Microbiol. 9:1181-1191.
    • (1993) Mol. Microbiol. , vol.9 , pp. 1181-1191
    • Navarro, C.1    Wu, L.F.2    Mandrand-Berthelot, M.A.3
  • 31
    • 0026051251 scopus 로고
    • A Salmonella typhimurium virulence protein is similar to a Yersinia enterocolitica invasion protein and a bacteriophage lambda outer membrane protein
    • Pulkkinen, W. S., and S. I. Miller. 1991. A Salmonella typhimurium virulence protein is similar to a Yersinia enterocolitica invasion protein and a bacteriophage lambda outer membrane protein. J. Bacteriol. 173:86-93.
    • (1991) J. Bacteriol. , vol.173 , pp. 86-93
    • Pulkkinen, W.S.1    Miller, S.I.2
  • 32
    • 0017839245 scopus 로고
    • Cluster of genes controlling proline degradation in Salmonella typhimurium
    • Ratzkin, B., and J. Roth. 1978. Cluster of genes controlling proline degradation in Salmonella typhimurium. J. Bacteriol. 133:744-754.
    • (1978) J. Bacteriol. , vol.133 , pp. 744-754
    • Ratzkin, B.1    Roth, J.2
  • 33
    • 0027298448 scopus 로고
    • Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis
    • Rivers, S. L., E. McNairn, F. Blasco, G. Giordano, and D. H. Boxer. 1993. Molecular genetic analysis of the moa operon of Escherichia coli K-12 required for molybdenum cofactor biosynthesis. Mol. Microbiol. 8:1071-1081.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1071-1081
    • Rivers, S.L.1    McNairn, E.2    Blasco, F.3    Giordano, G.4    Boxer, D.H.5
  • 34
    • 0029658689 scopus 로고    scopus 로고
    • Cobalamin (coenzyme B12): Synthesis and biological significance
    • Roth, J. R., J. G. Lawrence, and T. A. Bobik. 1996. Cobalamin (coenzyme B12): synthesis and biological significance. Annu. Rev. Microbiol. 50:137-181.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 137-181
    • Roth, J.R.1    Lawrence, J.G.2    Bobik, T.A.3
  • 36
    • 0028566978 scopus 로고
    • The hydrogenases and formate dehydrogenases of Escherichia coli
    • Sawers, G. 1994. The hydrogenases and formate dehydrogenases of Escherichia coli. Antonie Van Leeuwenhoek 66:57-88.
    • (1994) Antonie Van Leeuwenhoek , vol.66 , pp. 57-88
    • Sawers, G.1
  • 37
    • 0022489526 scopus 로고
    • Characterization and physiological roles of membrane-bound hydrogenase isoenzymes from Salmonella typhimurium
    • Sawers, R. G., D. J. Jamieson, C. F. Higgins, and D. H. Boxer. 1986. Characterization and physiological roles of membrane-bound hydrogenase isoenzymes from Salmonella typhimurium. J. Bacteriol. 168:398-404.
    • (1986) J. Bacteriol. , vol.168 , pp. 398-404
    • Sawers, R.G.1    Jamieson, D.J.2    Higgins, C.F.3    Boxer, D.H.4
  • 38
    • 0015449701 scopus 로고
    • Phage P22 mutants with increased or decreased transduction abilities
    • Schmieger, H. 1972. Phage P22 mutants with increased or decreased transduction abilities. Mol. Gen. Genet. 119:75-88.
    • (1972) Mol. Gen. Genet. , vol.119 , pp. 75-88
    • Schmieger, H.1
  • 39
    • 0026002819 scopus 로고
    • Determinants of DNA sequence divergence between Escherichia coli and Salmonella typhimurium: Codon usage, map position, and concerted evolution
    • Sharp, P. M. 1991. Determinants of DNA sequence divergence between Escherichia coli and Salmonella typhimurium: codon usage, map position, and concerted evolution. J. Mol. Evol. 33:23-33.
    • (1991) J. Mol. Evol. , vol.33 , pp. 23-33
    • Sharp, P.M.1
  • 40
    • 0028151310 scopus 로고
    • Escherichia coli possesses two homologous anaerobic C4-dicarboxylate membrane transporters (DcuA and DcuB) distinct from the aerobic dicarboxylate transport system (Dct)
    • Six, S., S. C. Andrews, G. Unden, and J. R. Guest. 1994. Escherichia coli possesses two homologous anaerobic C4-dicarboxylate membrane transporters (DcuA and DcuB) distinct from the aerobic dicarboxylate transport system (Dct). J. Bacteriol. 176:6470-6478.
    • (1994) J. Bacteriol. , vol.176 , pp. 6470-6478
    • Six, S.1    Andrews, S.C.2    Unden, G.3    Guest, J.R.4
  • 41
    • 0024989737 scopus 로고
    • FNR and its role in oxygen-regulated gene expression in Escherichia coli
    • Spiro, S., and J. R. Guest. 1990. FNR and its role in oxygen-regulated gene expression in Escherichia coli. FEMS Microbiol. Rev. 6:399-428.
    • (1990) FEMS Microbiol. Rev. , vol.6 , pp. 399-428
    • Spiro, S.1    Guest, J.R.2
  • 43
    • 0020560956 scopus 로고
    • Isolation and characterization Salmonella typhimurium mutants lacking a tripeptidase (peptidase T)
    • Strauch, K. L., and C. G. Miller. 1983. Isolation and characterization Salmonella typhimurium mutants lacking a tripeptidase (peptidase T). J. Bacteriol. 154:763-771.
    • (1983) J. Bacteriol. , vol.154 , pp. 763-771
    • Strauch, K.L.1    Miller, C.G.2
  • 44
    • 0027256676 scopus 로고
    • Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria
    • Tam, R., and M. H. Saier, Jr. 1993. Structural, functional, and evolutionary relationships among extracellular solute-binding receptors of bacteria. Microbiol. Rev. 57:320-346.
    • (1993) Microbiol. Rev. , vol.57 , pp. 320-346
    • Tam, R.1    Saier M.H., Jr.2
  • 45
    • 0030738589 scopus 로고    scopus 로고
    • Alternative respiratory pathways of Escherichia coli: Energetics and transcriptional regulation in response to electron acceptors
    • Unden, G., and J. Bongaerts. 1997. Alternative respiratory pathways of Escherichia coli: energetics and transcriptional regulation in response to electron acceptors. Biochim. Biophys. Acta 1318:217-234.
    • (1997) Biochim. Biophys. Acta , vol.1318 , pp. 217-234
    • Unden, G.1    Bongaerts, J.2
  • 46
    • 77049313195 scopus 로고
    • Acetylornithase of E. coli: Partial purification and some properties
    • Vogel, H. J., and D. M. Bonner. 1956. Acetylornithase of E. coli: partial purification and some properties. J. Biol. Chem. 218:97-106.
    • (1956) J. Biol. Chem. , vol.218 , pp. 97-106
    • Vogel, H.J.1    Bonner, D.M.2
  • 47
    • 0023986420 scopus 로고
    • Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity
    • Weiner, J. H., D. P. MacIsaac, R. E. Bishop, and P. T. Bilous. 1988. Purification and properties of Escherichia coli dimethyl sulfoxide reductase, an iron-sulfur molybdoenzyme with broad substrate specificity. J. Bacteriol. 170:1505-1510.
    • (1988) J. Bacteriol. , vol.170 , pp. 1505-1510
    • Weiner, J.H.1    MacIsaac, D.P.2    Bishop, R.E.3    Bilous, P.T.4
  • 48
    • 0022460634 scopus 로고
    • Anaerobically induced genes of Escherichia coli
    • Winkelman, J. W., and D. P. Clark. 1986. Anaerobically induced genes of Escherichia coli. J. Bacteriol. 167:362-367.
    • (1986) J. Bacteriol. , vol.167 , pp. 362-367
    • Winkelman, J.W.1    Clark, D.P.2
  • 49
    • 0024836127 scopus 로고
    • Nickel deficiency gives rise to the defective hydrogenase phenotype of hydC and fnr mutants in Escherichia coli
    • Wu, L. F., M. A. Mandrand-Berthelot, R. Waugh, C. J. Edmonds, S. E. Holt, and D. H. Boxer. 1989. Nickel deficiency gives rise to the defective hydrogenase phenotype of hydC and fnr mutants in Escherichia coli. Mol. Microbiol. 3:1709-1718.
    • (1989) Mol. Microbiol. , vol.3 , pp. 1709-1718
    • Wu, L.F.1    Mandrand-Berthelot, M.A.2    Waugh, R.3    Edmonds, C.J.4    Holt, S.E.5    Boxer, D.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.