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PMID: 6277863 Published · ppublish English Journal Article

Comparison of transcription of beta-lactamase genes specified by various ampicillin transposons.

Journal of bacteriology ·Vol. 150 ·No. 1 ·1982-04-00 ·Pages 269-76

Yamamoto T, Yamagata S, Horii K, Yamagishi S

Abstract

The beta-lactamase gene from four kinds of ampicillin transposons, Tn2601, Tn3, Tn2602 and Tn1, specifying the type I (or TEM type, alternatively) beta-lactamase was cloned onto plasmid pACYC184, and the level of in vivo transcription from each beta-lactamase gene was determined by DNA-RNA hybridization. Type I beta-lactamase is very uniform enzymologically, but heterogeneous in absolute levels of enzyme activity. The results demonstrated that the heterogeneity can be explained by the efficiency of transcription of each beta-lactamase gene, suggesting a difference in its promoter efficiency. A comparison of the levels of transcription of the beta-lactamase gene and the whole ampicillin transposon suggested that the beta-lactamase gene has the strongest promoter all of the genes in the ampicillin transposon.

MeSH Terms
Ampicillin/pharmacology Cloning, Molecular DNA Transposable Elements Escherichia coli/genetics Genes Genes, Bacterial Operon Transcription, Genetic beta-Lactamases/genetics,metabolism
Chemicals
DNA Transposable Elements Ampicillin beta-Lactamases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Yamamoto T
Yamagata S
Horii K
Yamagishi S
References (25)
25 references, click to expand
  1. The relation of resistance transfer factors to the F-factor (sex-factor) of Escherichia coli K12.
    Genet Res. 1966 Feb;7(1):134-40 PMID: 5324663
  2. Comparison of penicillinases produced by R factors isolated from ampicillin-resistant gram-negative bacteria.
    Jpn J Microbiol. 1970 Mar;14(2):123-8 PMID: 4910534
  3. Variant of penicillinase mediated by an R factor in Escherichia coli.
    J Bacteriol. 1970 Nov;104(2):620-9 PMID: 4923065
  4. Properties of an R factor from Pseudomonas aeruginosa.
    J Bacteriol. 1971 Dec;108(3):1244-9 PMID: 4945193
  5. Properties of a R factor which originated in Pseudomonas aeruginosa 1822.
    J Bacteriol. 1972 May;110(2):529-37 PMID: 4336689
  6. Molecular specificities of R factor-determined beta-lactamases: correlation with plasmid compatibility.
    J Bacteriol. 1974 Jan;117(1):56-62 PMID: 4587613
  7. Transposition of ampicillin resistance from RP4 to other replicons.
    Mol Gen Genet. 1974;132(1):31-40 PMID: 4609125
  8. Origin of the TEM-beta-lactamase gene found on plasmids.
    J Bacteriol. 1975 Apr;122(1):250-6 PMID: 1091625
  9. Site specific recA--independent recombination between bacterial plasmids: involvement of palindromes at the recombinational loci.
    Proc Natl Acad Sci U S A. 1975 Apr;72(4):1373-7 PMID: 1093180
  10. Analytical isoelectric focusing of R factor-determined beta-lactamases: correlation with plasmid compatibility.
    J Bacteriol. 1976 Feb;125(2):713-8 PMID: 1107329
  11. In vivo transcription of R-plasmid deoxyribonucleic acid in Escherichia coli strains with altered antibiotic resistance levels and/or conjugal proficiency.
    J Bacteriol. 1976 Mar;125(3):1148-55 PMID: 767321
  12. Simple agarose gel electrophoretic method for the identification and characterization of plasmid deoxyribonucleic acid.
    J Bacteriol. 1976 Sep;127(3):1529-37 PMID: 821935
  13. Transposition of a plasmid deoxyribonucleic acid sequence that mediates ampicillin resistance: independence from host rec functions and orientation of insertion.
    J Bacteriol. 1976 Oct;128(1):425-34 PMID: 789346
  14. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid.
    J Bacteriol. 1978 Jun;134(3):1141-56 PMID: 149110
  15. Iodometric assay method for beta-lactamase with various beta-lactam antibiotics as substrates.
    Antimicrob Agents Chemother. 1978 Jun;13(6):910-3 PMID: 677858
  16. Location of promoter sites on plasmid NTP1 which contains the ampicillin resistance transposon Tn1701.
    J Mol Biol. 1979 Feb 5;127(4):397-409 PMID: 372545
  17. Identification and characterization of a self-regulated repressor of translocation of the Tn3 element.
    Proc Natl Acad Sci U S A. 1979 Aug;76(8):4020-4 PMID: 386354
  18. Identification of the protein encoded by the transposable element Tn3 which is required for its transposition.
    Nature. 1979 Dec 20-27;282(5741):797-801 PMID: 390401
  19. Transposition protein of Tn3: identification and characterisation of an essential repressor-controlled gene product.
    Nature. 1979 Dec 20-27;282(5741):801-6 PMID: 390402
  20. Construction of a physical map of a kanamycin (Km) transposon, Tn5, and a comparison to another Km transposon, Tn903.
    Mol Gen Genet. 1980 Apr;178(1):77-83 PMID: 6247620
  21. Gene expression of ampicillin resistance transposons, Tn2601 and Tn2602.
    Microbiol Immunol. 1980;24(6):479-94 PMID: 6251343
  22. Quantitative correlation between penicillin resistance and beta-lactamase activity specified by the R plasmids R1, R1 bla-45, and RP1 in Escherichia coli K-12.
    Antimicrob Agents Chemother. 1980 Nov;18(5):675-9 PMID: 7004346
  23. Restriction endonuclease cleavage maps of the ampicillin transposons Tn2601 and Tn2602.
    Microbiol Immunol. 1980;24(12):1139-49 PMID: 6261093
  24. Protein measurement with the Folin phenol reagent.
    J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
  25. Transduction of linked genetic characters of the host by bacteriophage P1.
    Virology. 1955 Jul;1(2):190-206 PMID: 13267987
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1982-04-00
Pages
269-76
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC220109
Subset
IM
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