메뉴 건너뛰기




Volumn 266, Issue 1, 1997, Pages 23-30

A single amino acid substitution in Staphylococcus aureus dihydrofolate reductase determines trimethoprim resistance

Author keywords

DHFR; NMR; S. aureus; TMP resistance; X ray structure

Indexed keywords

DIHYDROFOLATE REDUCTASE; METHOTREXATE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PHENYLALANINE; TRIMETHOPRIM; TYROSINE;

EID: 0031566958     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0770     Document Type: Article
Times cited : (151)

References (53)
  • 2
    • 0028289341 scopus 로고
    • Dissemination among staphylococci of DNA sequences associated with methicillin resistance
    • Archer G. L., Niemeyer D. M., Thanassi J. A., Pucci M. J. Dissemination among staphylococci of DNA sequences associated with methicillin resistance. Antimicrob. Agents Chemother. 38:1994;447-454.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 447-454
    • Archer, G.L.1    Niemeyer, D.M.2    Thanassi, J.A.3    Pucci, M.J.4
  • 3
    • 0027266017 scopus 로고
    • Genetics and mechanisms of glycpeptide resistance in enterococci
    • Arthur M., Courvalin P. Genetics and mechanisms of glycpeptide resistance in enterococci. Antimicrob. Agents Chemother. 37:1993;1563-1571.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1563-1571
    • Arthur, M.1    Courvalin, P.2
  • 4
    • 0345311216 scopus 로고
    • 13C assignments from sensitivity enhanced detection of heteronuclear multiple bond connectivity by 2D multiple quantum NMR
    • 13C assignments from sensitivity enhanced detection of heteronuclear multiple bond connectivity by 2D multiple quantum NMR. J. Am. Chem. Soc. 108:1986;2093-2094.
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 2093-2094
    • Bax, A.1    Summers, M.F.2
  • 5
    • 33644757144 scopus 로고
    • Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR
    • Bax A., Griffey R. H., Hawkins B. L. Correlation of proton and nitrogen-15 chemical shifts by multiple quantum NMR. J. Magn. Reson. 55:1983;301-315.
    • (1983) J. Magn. Reson. , vol.55 , pp. 301-315
    • Bax, A.1    Griffey, R.H.2    Hawkins, B.L.3
  • 6
    • 0021894727 scopus 로고
    • 15N NMR studies of protonation and hydrogen-bonding in the binding of trimethoprim to dihydrofolate reductase
    • 15N NMR studies of protonation and hydrogen-bonding in the binding of trimethoprim to dihydrofolate reductase. Eur. Biophys. J. 11:1985;211-218.
    • (1985) Eur. Biophys. J. , vol.11 , pp. 211-218
    • Bevan, A.W.1    Roberts, G.C.K.2    Feeney, J.3    Kuyper, L.4
  • 7
    • 0024498518 scopus 로고
    • Dihydrofolate reductase: Multiple conformations and alternative modes of substrate binding
    • Birdsall B., Feeney J., Tendler S. J., Hammond S. J., Roberts G. C. Dihydrofolate reductase: multiple conformations and alternative modes of substrate binding. Biochemistry. 28:1989;2297-2305.
    • (1989) Biochemistry , vol.28 , pp. 2297-2305
    • Birdsall, B.1    Feeney, J.2    Tendler, S.J.3    Hammond, S.J.4    Roberts, G.C.5
  • 8
    • 0000899457 scopus 로고
    • Dihydrofolate reductase
    • New York: John Wiley and Sons
    • Blakley R. L. Dihydrofolate reductase. Folates and Pterins. 1984;John Wiley and Sons, New York.
    • (1984) Folates and Pterins
    • Blakley, R.L.1
  • 9
    • 0020441466 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution
    • Bolin J. T., Filman D. J., Matthews D. A., Hamlin R. C., Kraut J. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. J. Biol. Chem. 257:1982;13650-13662.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13650-13662
    • Bolin, J.T.1    Filman, D.J.2    Matthews, D.A.3    Hamlin, R.C.4    Kraut, J.5
  • 10
    • 0020561080 scopus 로고
    • Evidence for a slowing in trimethoprim resistance during 1981- a comparison with earlier years
    • Brumfitt W., Hamilton-Miller J. M. T., Wood A. Evidence for a slowing in trimethoprim resistance during 1981- a comparison with earlier years. J. Antimicrob. Chemother. 11:1983;503-509.
    • (1983) J. Antimicrob. Chemother. , vol.11 , pp. 503-509
    • Brumfitt, W.1    Hamilton-Miller, J.M.T.2    Wood, A.3
  • 11
    • 0003769049 scopus 로고
    • New Haven, London: Yale University Press
    • Brünger A. T. X-PLOR Version 3.1. 1992;Yale University Press, New Haven, London.
    • (1992) X-PLOR Version 3.1
    • Brünger, A.T.1
  • 13
    • 0025270551 scopus 로고
    • +ternary complex. Substrate binding and a model for the transition state
    • +ternary complex. Substrate binding and a model for the transition state. Biochemistry. 29:1990;3263-3277.
    • (1990) Biochemistry , vol.29 , pp. 3263-3277
    • Bystroff, C.1    Oatley, S.J.2    Kraut, J.3
  • 14
    • 0000032658 scopus 로고
    • 15N proton-heteroatom coupling constants in the NMR spectra of peptides. Comparison of experimental and theoretical data
    • 15N proton-heteroatom coupling constants in the NMR spectra of peptides. Comparison of experimental and theoretical data. J. Magn. Reson. 19:1975;123-129.
    • (1975) J. Magn. Reson , vol.19 , pp. 123-129
    • Bystrov, V.F.1    Gavrilov, Y.D.2    Solkan, V.N.3
  • 15
    • 0000625192 scopus 로고
    • Collaborative Computational Project, Number 4
    • CCP4 suite. Collaborative Computational Project, Number 4. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 16
    • 0023668136 scopus 로고
    • Probing the functional role of phenylalanine-31 of Escherichia coli dihydrofolate reductase by site directed mutagenesis
    • Chen J.-T., Taira K., Tu C.-P. D., Benkovich S. Probing the functional role of phenylalanine-31 of Escherichia coli dihydrofolate reductase by site directed mutagenesis. Biochemistry. 26:1987;4093-4100.
    • (1987) Biochemistry , vol.26 , pp. 4093-4100
    • Chen, J.-T.1    Taira, K.2    Tu, C.-P.D.3    Benkovich, S.4
  • 17
    • 0027338123 scopus 로고
    • 13C NMR determination of the tautomeric and ionization states of folatew in its complexes with Lactobacillus casei dihydrofolate reductase
    • 13C NMR determination of the tautomeric and ionization states of folatew in its complexes with Lactobacillus casei dihydrofolate reductase. Biochemistry. 32:1993;6846-6854.
    • (1993) Biochemistry , vol.32 , pp. 6846-6854
    • Cheung, H.T.A.1    Birdsall, B.2    Frenkiel, T.A.3    Chau, D.D.4    Feeney, J.5
  • 18
    • 0026705492 scopus 로고
    • Epidemiology of drug resistance: Implications for a post-antimicrobial era
    • Cohen M. L. Epidemiology of drug resistance: implications for a post-antimicrobial era. Science. 257:1992;1050-1055.
    • (1992) Science , vol.257 , pp. 1050-1055
    • Cohen, M.L.1
  • 19
    • 0028063691 scopus 로고
    • Antimicrobial resistance: Prognosis for public health
    • Cohen M. L. Antimicrobial resistance: prognosis for public health. Trends Microbiol. 2:1994;422-425.
    • (1994) Trends Microbiol. , vol.2 , pp. 422-425
    • Cohen, M.L.1
  • 20
    • 0023237141 scopus 로고
    • Characterization of a staphylococcal trimethoprim resistance gene and its product
    • Coughter J. P., Johnston J. L., Archer G. L. Characterization of a staphylococcal trimethoprim resistance gene and its product. Antimicrob. Agents Chemother. 31:1987;1027-1032.
    • (1987) Antimicrob. Agents Chemother. , vol.31 , pp. 1027-1032
    • Coughter, J.P.1    Johnston, J.L.2    Archer, G.L.3
  • 21
    • 0027225417 scopus 로고
    • Characterization of the gene for chromosomal trimethoprim sensitive dihydrofolate reductase of Staphylococcus aureus ATCC 25923
    • Dale G. E., Then R. L., Stüber D. Characterization of the gene for chromosomal trimethoprim sensitive dihydrofolate reductase of Staphylococcus aureus ATCC 25923. Antimicrob. Agents Chemother. 37:1993;1400-1405.
    • (1993) Antimicrob. Agents Chemother. , vol.37 , pp. 1400-1405
    • Dale, G.E.1    Then, R.L.2    Stüber, D.3
  • 22
    • 0028103565 scopus 로고
    • Improving protein solubility through rationally designed amino acid replacements: Solubilization of the trimethoprim resistant type S1 dihydrofolate reductase
    • Dale G. E., Broger C., Langen H., D'Arcy A., Stüber D. Improving protein solubility through rationally designed amino acid replacements: solubilization of the trimethoprim resistant type S1 dihydrofolate reductase. Protein Eng. 7:1994a;933-939.
    • (1994) Protein Eng. , vol.7 , pp. 933-939
    • Dale, G.E.1    Broger, C.2    Langen, H.3    D'Arcy, A.4    Stüber, D.5
  • 23
    • 0028177819 scopus 로고
    • Increased solubility of trimethoprim resistant type S1 DHFR from Staphylococcus aureus in Escherichia coli cells overproducing the chaperonins GroEL and GroES
    • Dale G. E., Langen H., Schoenfeld H., Stieger M. Increased solubility of trimethoprim resistant type S1 DHFR from Staphylococcus aureus in Escherichia coli cells overproducing the chaperonins GroEL and GroES. Protein Eng. 7:1994b;925-931.
    • (1994) Protein Eng. , vol.7 , pp. 925-931
    • Dale, G.E.1    Langen, H.2    Schoenfeld, H.3    Stieger, M.4
  • 24
    • 0029011953 scopus 로고
    • Characterization of the gene for the chromosomal dihydrofolate reductase of Staphylococcus epidermidis ATCC 14990: The origin of the trimethoprim resistant S1 DHFR from S. Aureus ?
    • Dale G. E., Broger C., Hartman P. G., Langen H., Page M. G. P., Then R. L., Stüber D. Characterization of the gene for the chromosomal dihydrofolate reductase of Staphylococcus epidermidis ATCC 14990: the origin of the trimethoprim resistant S1 DHFR from S. aureus ? J. Bacteriol. 177:1995a;2965-2970.
    • (1995) J. Bacteriol. , vol.177 , pp. 2965-2970
    • Dale, G.E.1    Broger, C.2    Hartman, P.G.3    Langen, H.4    Page, M.G.P.5    Then, R.L.6    Stüber, D.7
  • 25
    • 0029166664 scopus 로고
    • Cloning and characterisation of a novel plasmid-encoded trimethoprim-resistant dihydrofolate reductase from Staphylococcus haemolyticus MUR313
    • Dale G. E., Langen H., Page M. G. P., Then R. L., Stüber D. Cloning and characterisation of a novel plasmid-encoded trimethoprim-resistant dihydrofolate reductase from Staphylococcus haemolyticus MUR313. Antimicrob. Agents Chemother. 39:1995b;1920-1924.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 1920-1924
    • Dale, G.E.1    Langen, H.2    Page, M.G.P.3    Then, R.L.4    Stüber, D.5
  • 26
    • 23444440823 scopus 로고
    • Inactivation of antibiotics and the dissemination of resistance genes
    • Davies J. Inactivation of antibiotics and the dissemination of resistance genes. Science. 264:1994;375-382.
    • (1994) Science , vol.264 , pp. 375-382
    • Davies, J.1
  • 27
    • 0028988237 scopus 로고
    • Crystal structure and function of the isoniazide target of Mycobacterium tuberculosis
    • Dessen A., Quemard A., Blanchard J. S., Jacobs W. R., Sacchettini J. C. Crystal structure and function of the isoniazide target of Mycobacterium tuberculosis. Science. 267:1995;1638-1641.
    • (1995) Science , vol.267 , pp. 1638-1641
    • Dessen, A.1    Quemard, A.2    Blanchard, J.S.3    Jacobs, W.R.4    Sacchettini, J.C.5
  • 28
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A, 47:1991;392-400.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 392-400
    • Engh, R.1    Huber, R.2
  • 29
    • 0011167512 scopus 로고
    • Isotope-aided NMR studies of protein-ligand interactions
    • Feeney J. Isotope-aided NMR studies of protein-ligand interactions. Spec. Publ. Roy. Soc. Chem. 148:1995;161-184.
    • (1995) Spec. Publ. Roy. Soc. Chem. , vol.148 , pp. 161-184
    • Feeney, J.1
  • 30
    • 84967852329 scopus 로고
    • MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement
    • Fitzgerald P. M. D. MERLOT, an integrated package of computer programs for the determination of crystal structures by molecular replacement. J. Appl. Crystallog. 21:1988;273-278.
    • (1988) J. Appl. Crystallog. , vol.21 , pp. 273-278
    • Fitzgerald, P.M.D.1
  • 31
    • 0023232652 scopus 로고
    • Molecular epidemiology of trimethoprim resistance among coagulase-negative staphylococci
    • Galetto D. W., Johnston J. L., Archer G. L. Molecular epidemiology of trimethoprim resistance among coagulase-negative staphylococci. Antimicrob. Agents. Chemother. 31:1987;1683-1688.
    • (1987) Antimicrob. Agents. Chemother. , vol.31 , pp. 1683-1688
    • Galetto, D.W.1    Johnston, J.L.2    Archer, G.L.3
  • 32
    • 0026908615 scopus 로고
    • Peptide mechanics: A force field for peptides and proteins working with entire residues as smallest units
    • Gerber P. R. Peptide mechanics: a force field for peptides and proteins working with entire residues as smallest units. Biopolymers. 32:1992;1003-1017.
    • (1992) Biopolymers , vol.32 , pp. 1003-1017
    • Gerber, P.R.1
  • 35
    • 0019958107 scopus 로고
    • Cloning of the dihydrofolate reductase gene from Escherichia coli K12
    • Iwakura M., Shimura Y., Tsuda K. Cloning of the dihydrofolate reductase gene from Escherichia coli K12. J. Biochem. 91:1982;1205-1212.
    • (1982) J. Biochem. , vol.91 , pp. 1205-1212
    • Iwakura, M.1    Shimura, Y.2    Tsuda, K.3
  • 36
    • 0023936311 scopus 로고
    • Nucleotide sequence of the thymidylate synthase B and dihydrofolate reductase genes contained in one Bacillus subtilis operon
    • Iwakura M., Kawata M., Tsuda K., Tanaka T. Nucleotide sequence of the thymidylate synthase B and dihydrofolate reductase genes contained in one Bacillus subtilis operon. Gene. 64:1988;9-20.
    • (1988) Gene , vol.64 , pp. 9-20
    • Iwakura, M.1    Kawata, M.2    Tsuda, K.3    Tanaka, T.4
  • 37
    • 85046526624 scopus 로고
    • Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector
    • Kabsch W. Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. J. Appl. Crystallog. 21:1988;916-924.
    • (1988) J. Appl. Crystallog. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 38
    • 0027964864 scopus 로고
    • Possible role of insertion sequence IS 257 in dissemination and expression of high- and low-level trimethoprim resistance in staphylococci
    • Leelaporn A., Firth N., Byrne M. E., Roper E., Skurray R. A. Possible role of insertion sequence IS 257 in dissemination and expression of high- and low-level trimethoprim resistance in staphylococci. Antimicrob. Agents Chemother. 38:1994;2238-2244.
    • (1994) Antimicrob. Agents Chemother. , vol.38 , pp. 2238-2244
    • Leelaporn, A.1    Firth, N.2    Byrne, M.E.3    Roper, E.4    Skurray, R.A.5
  • 39
    • 0015594095 scopus 로고
    • Present significance of resistance to trimethoprim and sulfonamides in coliforms, Staphylococcus aureus and Streptococcus faecalis
    • Lewis E. L., Lacey R. W. Present significance of resistance to trimethoprim and sulfonamides in coliforms, Staphylococcus aureus and Streptococcus faecalis. J. Clin. Pathol. 25:1973;175-180.
    • (1973) J. Clin. Pathol. , vol.25 , pp. 175-180
    • Lewis, E.L.1    Lacey, R.W.2
  • 40
    • 0020538080 scopus 로고
    • Analysis of plasmids in nocosomial strains of multiple antibiotic resistant Staphylococcus aureus
    • Lyon B. R., May J. W., Skurray R. A. Analysis of plasmids in nocosomial strains of multiple antibiotic resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 23:1983;817-826.
    • (1983) Antimicrob. Agents Chemother. , vol.23 , pp. 817-826
    • Lyon, B.R.1    May, J.W.2    Skurray, R.A.3
  • 42
    • 0026760182 scopus 로고
    • The crisis in antibiotic resistance
    • Neu H. C. The crisis in antibiotic resistance. Science. 257:1992;1064-1073.
    • (1992) Science , vol.257 , pp. 1064-1073
    • Neu, H.C.1
  • 43
    • 23444456920 scopus 로고
    • Prevention of drug access to bacterial targets: Permeability barriers and active efflux
    • Nikaido H. Prevention of drug access to bacterial targets: permeability barriers and active efflux. Science. 264:1994;382-388.
    • (1994) Science , vol.264 , pp. 382-388
    • Nikaido, H.1
  • 44
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M., Saudek V., Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR. 2:1992;661-665.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 45
    • 85005688722 scopus 로고
    • A comparison of the binding of the ligand trimethoprim to bacterial and vertabrate dihydrofolate reductases
    • Roberts V. A., Dauber-Osguthorpe P., Osguthorpe D. J., Levin E., Hagler A. T. A comparison of the binding of the ligand trimethoprim to bacterial and vertabrate dihydrofolate reductases. Israel J. Chem. 2:1986;198-210.
    • (1986) Israel J. Chem. , vol.2 , pp. 198-210
    • Roberts, V.A.1    Dauber-Osguthorpe, P.2    Osguthorpe, D.J.3    Levin, E.4    Hagler, A.T.5
  • 46
    • 0039573557 scopus 로고
    • The protonation of 2,4-diaminopyrimidines. I. Dissociation constants and substitution effects
    • Roth B., Sterlitz J. Z. The protonation of 2,4-diaminopyrimidines. I. Dissociation constants and substitution effects. J. Organ. Chem. 34:1969;821-836.
    • (1969) J. Organ. Chem. , vol.34 , pp. 821-836
    • Roth, B.1    Sterlitz, J.Z.2
  • 47
    • 0024458146 scopus 로고
    • Trimethoprim resistance transposon Tn 4003 from Staphylococcus aureus encodes genes for a dihydrofolate reductase and thymidylate synthetase flanked by three copies of IS257
    • Rouch D. A., Messerotti L. J., Loo L. S. L., Jackson C. A., Skurray R. A. Trimethoprim resistance transposon Tn 4003 from Staphylococcus aureus encodes genes for a dihydrofolate reductase and thymidylate synthetase flanked by three copies of IS257. Mol. Microbiol. 3:1989;161-175.
    • (1989) Mol. Microbiol. , vol.3 , pp. 161-175
    • Rouch, D.A.1    Messerotti, L.J.2    Loo, L.S.L.3    Jackson, C.A.4    Skurray, R.A.5
  • 49
    • 49049124842 scopus 로고
    • Elimination of spectral distortion in polarization transfer experiments. Improvements and comparison techniques
    • Sørensen O. W., Ernst R. R. Elimination of spectral distortion in polarization transfer experiments. Improvements and comparison techniques. J. Magn. Reson. 51:1983;477-489.
    • (1983) J. Magn. Reson. , vol.51 , pp. 477-489
    • Sørensen, O.W.1    Ernst, R.R.2
  • 50
    • 0028420272 scopus 로고
    • Resistance to antibiotics mediated by target alterations
    • Spratt B. G. Resistance to antibiotics mediated by target alterations. Science. 264:1994;388-393.
    • (1994) Science , vol.264 , pp. 388-393
    • Spratt, B.G.1
  • 51
    • 0000926770 scopus 로고
    • System for high level production in Escherichia coli and rapid purification of recombinant proteins: Application to epitope mapping, preparation of antibodies and structure function analysis
    • I. Lefkovits, & B. Pernis. Orlando: Academic Press
    • Stüber D., Matile H., Garotta G. System for high level production in Escherichia coli and rapid purification of recombinant proteins: application to epitope mapping, preparation of antibodies and structure function analysis. Lefkovits I., Pernis B. Immunological Methods. 1990;Academic Press, Orlando.
    • (1990) Immunological Methods
    • Stüber, D.1    Matile, H.2    Garotta, G.3
  • 52
    • 0026566669 scopus 로고
    • Frequency and transferability of trimethoprim and sulfonamide resistance in methicillin-resistant Staphylococcus aureus and Staphylococcus epidermidis
    • Then R. L., Kohl I., Burdeska A. Frequency and transferability of trimethoprim and sulfonamide resistance in methicillin-resistant Staphylococcus aureus and Staphylococcus epidermidis. J. Chemother. 4:1992;67-71.
    • (1992) J. Chemother. , vol.4 , pp. 67-71
    • Then, R.L.1    Kohl, I.2    Burdeska, A.3
  • 53
    • 0000004180 scopus 로고
    • Proton-proton Overhauser effects of receptor-bound Cyclosporin A observed with the use of a heteronuclear-resolved half-filter experiment
    • Wider G., Weber C., Wüthrich K. Proton-proton Overhauser effects of receptor-bound Cyclosporin A observed with the use of a heteronuclear-resolved half-filter experiment. J. Am. Chem. Soc. 113:1991;4676-4678.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 4676-4678
    • Wider, G.1    Weber, C.2    Wüthrich, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.