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Trimethoprim resistance transposon Tn 4003 from Staphylococcus aureus encodes genes for a dihydrofolate reductase and thymidylate synthetase flanked by three copies of IS 257

Rouch, D. A., Messerotti, L. J., Loo, L. S. L., Jackson, C. A., Skurray, R. A.·1989·Molecular Microbiology

Abstract

Summary: Trimethoprim resistance mediated by the Staphylococcus aureus multi‐resistance plasmid pSK1 is encoded by a structure with characteristics of a composite transposon which we have designated Tn 4003. Nucleotide sequence analysis of Tn 4003 revealed it to be 4717 bp in length and to contain three copies of the insertion element IS 257 (789‐790 bp), the outside two of which are flanked by directly repeated 8‐bp target sequences. IS 257 has imperfect terminal inverted repeats of 27‐28 bp and encodes for a putative transposase with two potential α‐helix‐turn‐α‐helix DNA recognition motifs. IS 257 shares sequence similarities with members of the IS 15 family of insertion sequences from Gram‐negative bacteria and with ISS 1 from Streptococcus lactis. The central region of the transposon contains the dfrA gene that specifies the S1 dihydrofolate reductase (DHFR) responsible for trimethoprim resistance. The S1 enzyme shows sequence homology with type I and V trimethoprim‐resistant DHFRs from Gram‐negative bacteria and with chromosomally encoded DHFRs from Gram‐positive and Gram‐negative bacteria. 5’to dfrA is a thymidylate synthetase gene, designated thyE.

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Research works printed but not linked: 85

  1. 10.1016/0167-4781(88)90157-1 · doi:10.1016/0167-4781(88)90157-1
  2. Baccanari D.P., 1984, Characterization and amino acid sequence of Neisseria gonorrhoeae dihydrofolate reductase, J Biol Chem, 259, 12291, 10.1016/S0021-9258(20)71353-0 · doi:10.1016/s0021-9258(20)71353-0
  3. 10.1016/0378-1119(87)90271-X · DOI
  4. 10.1136/jcp.25.12.1086 · doi:10.1136/jcp.25.12.1086
  5. 10.1073/pnas.80.16.4914 · doi:10.1073/pnas.80.16.4914
  6. 10.1073/pnas.70.8.2276 · DOI · Paper page
  7. 10.1007/978-1-4613-2447-8_5 · doi:10.1007/978-1-4613-2447-8_5
  8. Bolin J.T., 1982, Crystal structures of Escherichia coii and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. I. General features and binding of methotrexate, J Biol Chem, 257, 13650, 10.1016/S0021-9258(18)33497-5 · DOI · Paper page
  9. 10.1007/BF00337820 · doi:10.1007/bf00337820
  10. 10.1007/BF00327434 · DOI
  11. Brown A.M.C., 1984, Characterization of IS46, an insertion sequence found on two IncN plasmids, J Baoteriol, 159, 472, 10.1128/jb.159.2.472-481.1984 · doi:10.1128/jb.159.2.472-481.1984
  12. 10.1073/pnas.81.10.3049 · doi:10.1073/pnas.81.10.3049
  13. Dekio S., 1984, Secondary structure and phylogeny of Staphylococcus and Micrococcus 5S rRNAs, J Bacteriol, 159, 233, 10.1128/jb.159.1.233-237.1984 · doi:10.1128/jb.159.1.233-237.1984
  14. 10.1016/0092-8674(86)90586-6 · DOI
  15. Filman D.J., 1982, Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Å resolution. II. Environment of bound NADPH and implications for catalysis, J Biol Chem, 257, 13663, 10.1016/S0021-9258(18)33498-7 · doi:10.1016/s0021-9258(18)33498-7
  16. 10.1093/nar/11.15.5147 · DOI
  17. 10.1093/nar/14.14.5933 · DOI
  18. Freisham J.H., 1978, Dihydrofolate reductase from amethopterin‐resistant Lactobacillus casei, J Biol Chem, 253, 6437, 10.1016/S0021-9258(19)46952-4 · doi:10.1016/s0021-9258(19)46952-4
  19. 10.1016/0022-2836(85)90262-1 · DOI · Paper page
  20. 10.1128/AAC.31.11.1683 · doi:10.1128/aac.31.11.1683
  21. 10.1016/0022-2836(78)90297-8 · DOI · Paper page
  22. Gentz R., 1985, Promoters recognized by Escherichia coli RNA polymerase selected by function: highly efficient promoters from bacteriophage T5, J Bacteriol, 164, 70, 10.1128/jb.164.1.70-77.1985 · doi:10.1128/jb.164.1.70-77.1985
  23. 10.1111/j.1574-6968.1987.tb02117.x · DOI
  24. Gillespie M.T., 1988, Structural and evolutionary relationships of β‐lactamase transposons from Staphylococcus aureus, J Gen Microbiol, 134, 2857
  25. 10.1073/pnas.71.8.3001 · doi:10.1073/pnas.71.8.3001
  26. 10.1016/S0021-9258(18)67400-9 · DOI · Paper page
  27. 10.1016/0092-8674(82)90007-1 · doi:10.1016/0092-8674(82)90007-1
  28. 10.1073/pnas.83.15.5387 · doi:10.1073/pnas.83.15.5387
  29. 10.1093/nar/15.13.5479 · doi:10.1093/nar/15.13.5479
  30. 10.1126/science.3099389 · DOI
  31. 10.1016/0092-8674(79)90228-9 · DOI · Paper page
  32. 10.1126/science.3107125 · DOI · Paper page
  33. 10.1016/0378-1119(88)90476-3 · doi:10.1016/0378-1119(88)90476-3
  34. 10.1126/science.3082007 · DOI · Paper page
  35. 10.1016/0378-1119(85)90142-8 · doi:10.1016/0378-1119(85)90142-8
  36. Koch A.L., 1981, Evolution of antibiotic resistance gene function, Microbiol Rev, 4, 355, 10.1128/mr.45.2.355-378.1981 · DOI
  37. 10.1038/320501a0 · DOI · Paper page
  38. 10.1038/297159a0 · doi:10.1038/297159a0
  39. 10.1007/BF00293927 · doi:10.1007/bf00293927
  40. 10.1016/0003-2697(85)90016-8 · DOI
  41. 10.1128/MMBR.51.1.88-134.1987 · doi:10.1128/mmbr.51.1.88-134.1987 · Paper page
  42. 10.1007/BF00382099 · DOI · Paper page
  43. 10.1111/j.1574-6968.1986.tb01269.x · doi:10.1111/j.1574-6968.1986.tb01269.x
  44. Maley G.F., 1979, The primary structure of Lactobacillus casei thymidylate synthetase. III. The use of 2‐(2‐nitrophenylsulfenyl)‐3‐methyl‐3‐bromoindolenine and limited tryptic peptides to establish the complete amino acid sequence of the enzyme, J Biol Chem, 254, 1301, 10.1016/S0021-9258(17)34202-3 · doi:10.1016/s0021-9258(17)34202-3
  45. 10.1016/0003-9861(82)90244-2 · doi:10.1016/0003-9861(82)90244-2
  46. 10.1073/pnas.79.24.7664 · DOI · Paper page
  47. 10.1002/bip.360270404 · DOI
  48. 10.1016/S0021-9258(18)89743-5 · DOI · Paper page
  49. Matthews P.R., 1987, The cloning of chromosomal DNA associated with methicillin and other resistances in Staphylococcus aureus, J Gen Microbiol, 133, 1919
  50. McLaughlin J.R., 1981, Unique feature in the ribosome binding site sequence of the Gram‐positive Staphylococcus aureusβ‐lactamase gene, J Biol Chem, 256, 11283, 10.1016/S0021-9258(19)68589-3 · DOI · Paper page
  51. 10.1093/nar/11.18.6319 · DOI
  52. Myoda T.T., 1985, Coregulation of dihydrofolate reductase and thymidylate synthase B in Bacillus subtilis, Biochem Biophys Acta, 824, 99
  53. 10.1007/BF02111283 · DOI · Paper page
  54. 10.1146/annurev.bi.53.070184.001453 · DOI · Paper page
  55. Pattishall K.H., 1977, Two distinct types of trimethoprim‐resistant dihydrofolate reductase specified by R‐plasmids of different incompatibility groups, J Biol Chem, 252, 2319, 10.1016/S0021-9258(17)40557-6 · DOI
  56. 10.1089/dna.1988.7.235 · doi:10.1089/dna.1988.7.235
  57. 10.1093/nar/11.7.2065 · doi:10.1093/nar/11.7.2065
  58. 10.1136/bmj.4.5571.71 · DOI
  59. Polzin K.M., 1987, Identification of a new insertion element, similar to Gram‐negative IS26, on the lactose plasmid of Streptococcus iactis ML3, J Bacteriol, 169, 5481, 10.1128/jb.169.12.5481-5488.1987 · DOI
  60. 10.1016/0147-619X(83)90004-5 · doi:10.1016/0147-619x(83)90004-5
  61. Rouch D.A., 1987, The aacA‐aphD gentamicin and kanamycin resistance determinant of Tn4001 from Staphylococcus aureus: expression and nucleotide sequence analysis, J Gen Miorobiol, 133, 3039
  62. 10.1073/pnas.74.12.5463 · DOI · Paper page
  63. 10.1038/320378a0 · doi:10.1038/320378a0
  64. Simonsen C.C., 1983, Identification of the type I trimethoprim‐resistant dihydrofolate reductase specified by the Escherichia coli R‐plasmid R483: comparison with prokaryotic and eucaryotic dihydrofolate reductases, J Bacteriol, 155, 1001, 10.1128/jb.155.3.1001-1008.1983 · DOI
  65. 10.1093/jac/21.suppl_C.19 · DOI
  66. 10.1093/nar/8.10.2255 · DOI · Paper page
  67. 10.1017/S0022172400054991 · doi:10.1017/s0022172400054991
  68. Smith J.T., 1984, Bacterial resistance to antifolate chemotherapeutic agents mediated by plasmids, Br Med Bull, 40, 42, 10.1093/oxfordjournals.bmb.a071946 · doi:10.1093/oxfordjournals.bmb.a071946
  69. 10.1093/nar/14.1.217 · DOI · Paper page
  70. Stone D., 1979, The amino acid sequence of the trimethoprim‐resistant dihydrofolate reductase specified in Escherichia coli by R‐plasmid R67, J Biol Chem, 254, 10857, 10.1016/S0021-9258(19)86600-0 · DOI
  71. 10.1007/BF00339581 · DOI · Paper page
  72. 10.1016/0022-2836(87)90479-7 · doi:10.1016/0022-2836(87)90479-7
  73. 10.1007/BF00428733 · DOI
  74. 10.1093/nar/13.6.2035 · DOI
  75. 10.1128/AAC.27.1.79 · DOI
  76. 10.1099/00222615-26-1-67 · doi:10.1099/00222615-26-1-67
  77. 10.1038/newbio246040a0 · DOI · Paper page
  78. Tolleson W.H., 1987, Cloning of the linked thymidylate synthase and dihydrofolate reductase from aminopterin‐resistant Lactobacillus casei, Fed Proc, 46, 862
  79. 10.1016/0378-1119(84)90111-2 · DOI
  80. 10.1016/0378-1119(83)90137-3 · doi:10.1016/0378-1119(83)90137-3
  81. Vales L.D., 1980, Effect of ssbA1 and lexC113 mutations on lambda prophage induction, bacteriophage growth and cell survival, J Bacteriol, 143, 887, 10.1128/jb.143.2.887-896.1980 · doi:10.1128/jb.143.2.887-896.1980
  82. 10.1016/0167-4781(87)90040-6 · DOI · Paper page
  83. 10.1016/0378-1119(85)90120-9 · DOI · Paper page
  84. 10.1042/bj2430309 · doi:10.1042/bj2430309
  85. 10.1002/j.1460-2075.1987.tb02627.x · doi:10.1002/j.1460-2075.1987.tb02627.x

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Metadata

Authors
Rouch, D. A., Messerotti, L. J., Loo, L. S. L., Jackson, C. A., & Skurray, R. A.
Venue
Molecular Microbiology
Publisher
Wiley
Published
1989-02
Volume
3
Issue
2
Pages
161-175
ISSN
  • 0950-382X
  • 1365-2958
Cited by
131
References
0
Language
en

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CoChat. (2026). Citation check: Trimethoprim resistance transposon Tn 4003 from Staphylococcus aureus encodes genes for a dihydrofolate reductase and thymidylate synthetase flanked by three copies of IS 257. https://app.cochat.ai/papers/10.1111/j.1365-2958.1989.tb01805.x
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Rouch, D. A., Messerotti, L. J., Loo, L. S. L., Jackson, C. A., & Skurray, R. A. (1989). Trimethoprim resistance transposon Tn 4003 from Staphylococcus aureus encodes genes for a dihydrofolate reductase and thymidylate synthetase flanked by three copies of IS 257. Molecular Microbiology. https://doi.org/10.1111/j.1365-2958.1989.tb01805.x

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