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Volumn 180, Issue 23, 1998, Pages 6260-6268

Characterization of mutations that allow p-aminobenzoyl-glutamate utilization by Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBENZOIC ACID; FOLIC ACID; GLUTAMIC ACID;

EID: 0031725643     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/.180.23.6260-6268.1998     Document Type: Article
Times cited : (43)

References (39)
  • 2
    • 0017351109 scopus 로고
    • Initiation of protein synthesis without formylation in a mutant of Escherichia coli that grows in the absence of tetrahydrofolate
    • Baumstark, B. R., L. L. Spremulli, U. L. RajBhandary, and G. M. Brown. 1977. Initiation of protein synthesis without formylation in a mutant of Escherichia coli that grows in the absence of tetrahydrofolate. J. Bacteriol. 129:457-471.
    • (1977) J. Bacteriol. , vol.129 , pp. 457-471
    • Baumstark, B.R.1    Spremulli, L.L.2    RajBhandary, U.L.3    Brown, G.M.4
  • 3
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H., and J. Doly. 1979. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.1    Doly, J.2
  • 5
    • 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. 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.1
  • 6
    • 0031660814 scopus 로고    scopus 로고
    • The gene for indole-3-acetyl-aspartic acid hydrolase from Entembacter agglomerans: Molecular cloning, nucleotide sequence, and expression in Escherichia coli
    • Chou, J. C, W. W. Mulbry, and J. D. Cohen. 1998. The gene for indole-3-acetyl-aspartic acid hydrolase from Entembacter agglomerans: molecular cloning, nucleotide sequence, and expression in Escherichia coli. Mol. Gen. Genet. 259:172-178.
    • (1998) Mol. Gen. Genet. , vol.259 , pp. 172-178
    • Chou, J.C.1    Mulbry, W.W.2    Cohen, J.D.3
  • 8
    • 0021245317 scopus 로고
    • Cyclic AMP receptor protein: Role in transcription activation
    • deCrombrugghe, B., S. Busby, and H. Buc. 1984. Cyclic AMP receptor protein: role in transcription activation. Science 224:831-838.
    • (1984) Science , vol.224 , pp. 831-838
    • DeCrombrugghe, B.1    Busby, S.2    Buc, H.3
  • 9
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • Eisengerg, D., E. Schwarz, M. Komaromy, and R. Wall. 1984. Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179:125-142.
    • (1984) J. Mol. Biol. , vol.179 , pp. 125-142
    • Eisengerg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 10
    • 0027443625 scopus 로고
    • TdcA, a transcriptional activator of the tdcABC operon of Escherichia coli, is a member of the LysR family of proteins
    • Ganduri, Y. L., S. R. Sadda, M. W. Datta, R. K. Jambukeswaran, and P. Datta. 1993. TdcA, a transcriptional activator of the tdcABC operon of Escherichia coli, is a member of the LysR family of proteins. Mol. Gen. Genet. 240:395-402.
    • (1993) Mol. Gen. Genet. , vol.240 , pp. 395-402
    • Ganduri, Y.L.1    Sadda, S.R.2    Datta, M.W.3    Jambukeswaran, R.K.4    Datta, P.5
  • 11
    • 0026544125 scopus 로고
    • Conserved motifs in a divergent nod box of Azorhizobium caulinodans ORS571 reveal a common structure in promoters regulated by LysR-type proteins
    • Goethals, K., M. Van Montagu, and M. Holsters. 1992. Conserved motifs in a divergent nod box of Azorhizobium caulinodans ORS571 reveal a common structure in promoters regulated by LysR-type proteins. Proc. Natl. Acad. Sci. USA 89:1646-1650.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1646-1650
    • Goethals, K.1    Van Montagu, M.2    Holsters, M.3
  • 12
    • 0025737957 scopus 로고
    • p-Aminobenzoate biosynthesis in Escherichia coli: Purification of aminodeoxychorismate lyase and cloning of pabC
    • Green, J. M., and B. P. Nichols. 1991. p-Aminobenzoate biosynthesis in Escherichia coli: purification of aminodeoxychorismate lyase and cloning of pabC. J. Biol. Chem. 266:12971-12975.
    • (1991) J. Biol. Chem. , vol.266 , pp. 12971-12975
    • Green, J.M.1    Nichols, B.P.2
  • 13
    • 0024790643 scopus 로고
    • Selection, adaptation, and bacterial operons
    • Hall, B. G. 1989. Selection, adaptation, and bacterial operons. Genome 31: 265-271.
    • (1989) Genome , vol.31 , pp. 265-271
    • Hall, B.G.1
  • 14
    • 0015609161 scopus 로고
    • Growth and initiation of protein synthesis in Escherichia coli in the presence of trimethoprim
    • Harvey, R. J. 1973. Growth and initiation of protein synthesis in Escherichia coli in the presence of trimethoprim. J. Bacteriol. 114:309-322.
    • (1973) J. Bacteriol. , vol.114 , pp. 309-322
    • Harvey, R.J.1
  • 15
    • 0023484188 scopus 로고
    • Unidirectional digestion with exonuclease III in DNA sequence analysis
    • Henikoff, S. 1987. Unidirectional digestion with exonuclease III in DNA sequence analysis. Methods Enzymol. 155:156-165.
    • (1987) Methods Enzymol. , vol.155 , pp. 156-165
    • Henikoff, S.1
  • 16
    • 0014803519 scopus 로고
    • Biosynthesis of 4-aminobenzoate in Escherichia coli
    • Huang, M., and F. Gibson. 1970. Biosynthesis of 4-aminobenzoate in Escherichia coli. J. Bacteriol. 102:767-773.
    • (1970) J. Bacteriol. , vol.102 , pp. 767-773
    • Huang, M.1    Gibson, F.2
  • 17
    • 0014097833 scopus 로고
    • Genetic analysis of mutant strains of Escherichia coli requiring p-aminohenzoate for growth
    • Huang, M., and J. Pittard. 1967. Genetic analysis of mutant strains of Escherichia coli requiring p-aminohenzoate for growth. J. Bacteriol. 93:1938-1942.
    • (1967) J. Bacteriol. , vol.93 , pp. 1938-1942
    • Huang, M.1    Pittard, J.2
  • 19
    • 0021847027 scopus 로고
    • The detection and classification of membrane-spanning proteins, Biochim
    • Klein, P., M. Kanehisa, and C. Delisi. 1985. The detection and classification of membrane-spanning proteins, Biochim. Biophys. Acta 815:468-476.
    • (1985) Biophys. Acta , vol.815 , pp. 468-476
    • Klein, P.1    Kanehisa, M.2    Delisi, C.3
  • 20
    • 0023669069 scopus 로고
    • The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara, Y., K. Akiyama, and K. Inoso. 1987. The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50:495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Inoso, K.3
  • 21
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor. N.Y.
    • Miller, J. H. 1972. Experiments in molecular genetics. Cold Spring Harbor Laboratory Press, Cold Spring Harbor. N.Y.
    • (1972) Experiments in Molecular Genetics
    • Miller, J.H.1
  • 23
    • 0024403436 scopus 로고
    • Para-Aminobenzoate synthesis from chorismate occurs in two steps
    • Nichols, B. P., A. Seibold, and S. Z. Doktor. 1989. para-Aminobenzoate synthesis from chorismate occurs in two steps. J. Biol. Chem. 264:8597-8601.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8597-8601
    • Nichols, B.P.1    Seibold, A.2    Doktor, S.Z.3
  • 24
    • 0004322302 scopus 로고
    • Effect of folic acid analogues on growth and cell division of nonexacting microorganisms
    • Nickerson, W. J., and M. Webb. 1956. Effect of folic acid analogues on growth and cell division of nonexacting microorganisms. J. Bacteriol. 71:129-139.
    • (1956) J. Bacteriol. , vol.71 , pp. 129-139
    • Nickerson, W.J.1    Webb, M.2
  • 25
    • 0030043244 scopus 로고    scopus 로고
    • Engineering specificity for folate into dihydrofolate reductase from Escherichia coli
    • Posner, B. A., L. Li, R. Bethell, T. Tsuji, and S. J. Benkovic. 1996, Engineering specificity for folate into dihydrofolate reductase from Escherichia coli. Biochemistry 35:1653-1663.
    • (1996) Biochemistry , vol.35 , pp. 1653-1663
    • Posner, B.A.1    Li, L.2    Bethell, R.3    Tsuji, T.4    Benkovic, S.J.5
  • 27
    • 0023059178 scopus 로고
    • A conformational preference parameter to predict helices in integral membrane proteins
    • Rao, M. J. K., and P. Argos. 1986. A conformational preference parameter to predict helices in integral membrane proteins. Biochim. Biophys. Acta 869:197-214.
    • (1986) Biochim. Biophys. Acta , vol.869 , pp. 197-214
    • Rao, M.J.K.1    Argos, P.2
  • 28
    • 0014690235 scopus 로고
    • The biosynthesis of folic acid. IX. Purification and properties of the enzymes required for the formation of dihydropteroic acid
    • Richey, D. P., and G. M. Brown. 1969. The biosynthesis of folic acid. IX. Purification and properties of the enzymes required for the formation of dihydropteroic acid. J. Biol. Chem. 244:1582-1592.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1582-1592
    • Richey, D.P.1    Brown, G.M.2
  • 29
    • 0014965061 scopus 로고
    • A comparison of the effectiveness with which p-aminobenzoic acid and p-aminobenzoyl-glutamate acid are used as substrates by dihydropteroate synthase from Escherichia coli
    • Richey, D. P., and G. Brown. 1970. A comparison of the effectiveness with which p-aminobenzoic acid and p-aminobenzoyl-glutamate acid are used as substrates by dihydropteroate synthase from Escherichia coli. Biochim. Biophys. Acta 222:237-239.
    • (1970) Biochim. Biophys. Acta , vol.222 , pp. 237-239
    • Richey, D.P.1    Brown, G.2
  • 31
    • 0024978323 scopus 로고
    • The complete nucleotide sequence of the tdc region of Escherichia coli
    • Schweizer, H. P., and P. Datta. 1989. The complete nucleotide sequence of the tdc region of Escherichia coli. Nucleic Acids Res. 17:3994.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 3994
    • Schweizer, H.P.1    Datta, P.2
  • 32
    • 0018890312 scopus 로고
    • Thin-layer chromatography of pteroylglutamates and related compounds
    • Scott, J. M. 1980. Thin-layer chromatography of pteroylglutamates and related compounds. Methods Enzymol. 66:437-443.
    • (1980) Methods Enzymol. , vol.66 , pp. 437-443
    • Scott, J.M.1
  • 34
    • 0000179124 scopus 로고
    • The enzymatic synthesis of folate-like compounds from hydroxymethyldihydropteridine pyrophosphate
    • Shiota, T., M. N. Disraely, and M. P. McCann. 1964. The enzymatic synthesis of folate-like compounds from hydroxymethyldihydropteridine pyrophosphate. J. Biol. Chem. 239:2259-2266.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2259-2266
    • Shiota, T.1    Disraely, M.N.2    McCann, M.P.3
  • 36
    • 0025189881 scopus 로고
    • Chromosomal organization and expression of Escherichia coli pabA
    • Tran, P. V., T. A. Bannor, S. Z. Doktor, and B. P. Nichols. 1990. Chromosomal organization and expression of Escherichia coli pabA. J. Bacteriol. 172: 397-410.
    • (1990) J. Bacteriol. , vol.172 , pp. 397-410
    • Tran, P.V.1    Bannor, T.A.2    Doktor, S.Z.3    Nichols, B.P.4
  • 37
    • 15644382312 scopus 로고
    • Differential reversal of inhibitory effects of folic acid analogues on growth, division, and deoxyribonucleic acid synthesis of microorganisms
    • Webb, M., and W. J. Nickerson. 1956. Differential reversal of inhibitory effects of folic acid analogues on growth, division, and deoxyribonucleic acid synthesis of microorganisms. J. Bacteriol. 71:140-148.
    • (1956) J. Bacteriol. , vol.71 , pp. 140-148
    • Webb, M.1    Nickerson, W.J.2
  • 38
    • 0001279038 scopus 로고
    • Preparation of genomic DNA from bacteria
    • F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.) Greene Publishing and Wiley-Interscience, New York, N.Y.
    • Wilson, K. 1987. Preparation of genomic DNA from bacteria, p. 2.4.1-2.4.5. In F. M. Ausubel, R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology. Greene Publishing and Wiley-Interscience, New York, N.Y.
    • (1987) Current Protocols in Molecular Biology , pp. 241-245
    • Wilson, K.1
  • 39
    • 0017139089 scopus 로고
    • Characteristics of guanosine triphosphate cyclohydrolase I purified from Escherichia coli
    • Yim, J. J., and G. M. Brown. 1976. Characteristics of guanosine triphosphate cyclohydrolase I purified from Escherichia coli. J. Biol. Chem. 251:5087-5094.
    • (1976) J. Biol. Chem. , vol.251 , pp. 5087-5094
    • Yim, J.J.1    Brown, G.M.2


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