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. 1986 Jun;83(11):3939–3943. doi: 10.1073/pnas.83.11.3939

Chloramphenicol induces translation of the mRNA for a chloramphenicol-resistance gene in Bacillus subtilis.

E J Duvall, P S Lovett
PMCID: PMC323640  PMID: 3086871

Abstract

cat-86 is a plasmid gene specifying chloramphenicol-inducible chloramphenicol acetyltransferase activity in Bacillus subtilis. Inducibility has been suggested to result primarily from activation of the translation of cat-86 mRNA by subinhibitory levels of chloramphenicol. To directly test the involvement of transcription in cat-86 induction, the gene was transcriptionally activated with a strong promoter, resulting in the synthesis of relatively high levels of cat-86 mRNA in uninduced cells. When RNA synthesis was blocked with rifampin (100 micrograms/ml), de novo inducibility of cat-86 by chloramphenicol could be demonstrated for more than 30 min. These results indicate that concurrent transcription is not essential for cat-86 induction. Accordingly, cat-86 is one of only a few inducible bacterial genes in which the primary form of regulation is at the translational level. This form of regulation may apply to other cat genes of Gram-positive origin whose expression is also inducible by chloramphenicol.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Ambulos N. P., Jr, Mongkolsuk S., Kaufman J. D., Lovett P. S. Chloramphenicol-induced translation of cat-86 mRNA requires two cis-acting regulatory regions. J Bacteriol. 1985 Nov;164(2):696–703. doi: 10.1128/jb.164.2.696-703.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ambulos N. P., Jr, Mongkolsuk S., Lovett P. S. A transcription termination signal immediately precedes the coding sequence for the chloramphenicol-inducible plasmid gene cat-86. Mol Gen Genet. 1985;199(1):70–75. doi: 10.1007/BF00327512. [DOI] [PubMed] [Google Scholar]
  3. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1006/abio.1976.9999. [DOI] [PubMed] [Google Scholar]
  4. Brückner R., Matzura H. Regulation of the inducible chloramphenicol acetyltransferase gene of the Staphylococcus aureus plasmid pUB112. EMBO J. 1985 Sep;4(9):2295–2300. doi: 10.1002/j.1460-2075.1985.tb03929.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Byeon W. H., Weisblum B. Post-transcriptional regulation of chloramphenicol acetyl transferase. J Bacteriol. 1984 May;158(2):543–550. doi: 10.1128/jb.158.2.543-550.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Dubnau D. Translational attenuation: the regulation of bacterial resistance to the macrolide-lincosamide-streptogramin B antibiotics. CRC Crit Rev Biochem. 1984;16(2):103–132. doi: 10.3109/10409238409102300. [DOI] [PubMed] [Google Scholar]
  7. Duvall E. J., Mongkolsuk S., Kim U. J., Lovett P. S., Henkin T. M., Chambliss G. H. Induction of the chloramphenicol acetyltransferase gene cat-86 through the action of the ribosomal antibiotic amicetin: involvement of a Bacillus subtilis ribosomal component in cat induction. J Bacteriol. 1985 Feb;161(2):665–672. doi: 10.1128/jb.161.2.665-672.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Duvall E. J., Williams D. M., Lovett P. S., Rudolph C., Vasantha N., Guyer M. Chloramphenicol-inducible gene expression in Bacillus subtilis. Gene. 1983 Oct;24(2-3):171–177. doi: 10.1016/0378-1119(83)90077-x. [DOI] [PubMed] [Google Scholar]
  9. Duvall E. J., Williams D. M., Mongkolsuk S., Lovett P. S. Regulatory regions that control expression of two chloramphenicol-inducible cat genes cloned in Bacillus subtilis. J Bacteriol. 1984 Jun;158(3):784–790. doi: 10.1128/jb.158.3.784-790.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Guarneros G., Montañez C., Hernandez T., Court D. Posttranscriptional control of bacteriophage lambda gene expression from a site distal to the gene. Proc Natl Acad Sci U S A. 1982 Jan;79(2):238–242. doi: 10.1073/pnas.79.2.238. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Harwood C. R., Williams D. M., Lovett P. S. Nucleotide sequence of a Bacillus pumilus gene specifying chloramphenicol acetyltransferase. Gene. 1983 Oct;24(2-3):163–169. doi: 10.1016/0378-1119(83)90076-8. [DOI] [PubMed] [Google Scholar]
  12. Karam J., Gold L., Singer B. S., Dawson M. Translational regulation: identification of the site on bacteriophage T4 rIIB mRNA recognized by the regA gene function. Proc Natl Acad Sci U S A. 1981 Aug;78(8):4669–4673. doi: 10.1073/pnas.78.8.4669. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  14. Lemaire G., Gold L., Yarus M. Autogenous translational repression of bacteriophage T4 gene 32 expression in vitro. J Mol Biol. 1978 Nov 25;126(1):73–90. doi: 10.1016/0022-2836(78)90280-2. [DOI] [PubMed] [Google Scholar]
  15. Miura A., Krueger J. H., Itoh S., de Boer H. A., Nomura M. Growth-rate-dependent regulation of ribosome synthesis in E. coli: expression of the lacZ and galK genes fused to ribosomal promoters. Cell. 1981 Sep;25(3):773–782. doi: 10.1016/0092-8674(81)90185-9. [DOI] [PubMed] [Google Scholar]
  16. Mongkolsuk S., Ambulos N. P., Jr, Lovett P. S. Chloramphenicol-inducible gene expression in Bacillus subtilis is independent of the chloramphenicol acetyltransferase structural gene and its promoter. J Bacteriol. 1984 Oct;160(1):1–8. doi: 10.1128/jb.160.1.1-8.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Mongkolsuk S., Chiang Y. W., Reynolds R. B., Lovett P. S. Restriction fragments that exert promoter activity during postexponential growth of Bacillus subtilis. J Bacteriol. 1983 Sep;155(3):1399–1406. doi: 10.1128/jb.155.3.1399-1406.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Mongkolsuk S., Duvall E. J., Lovett P. S. Transcription termination signal for the cat-86 indicator gene in a Bacillus subtilis promoter-cloning plasmid. Gene. 1985;37(1-3):83–90. doi: 10.1016/0378-1119(85)90260-4. [DOI] [PubMed] [Google Scholar]
  19. Morikawa N., Imamoto F. Degradation of tryptophan messenger. On the degradation of messenger RNA for the tryptophan operon in Escherichia coli. Nature. 1969 Jul 5;223(5201):37–40. doi: 10.1038/223037a0. [DOI] [PubMed] [Google Scholar]
  20. Morse D. E., Mosteller R., Baker R. F., Yanofsky C. Direction of in vivo degradation of tryptophan messenger RNA--a correction. Nature. 1969 Jul 5;223(5201):40–43. doi: 10.1038/223040a0. [DOI] [PubMed] [Google Scholar]
  21. Shaw W. V. Chloramphenicol acetyltransferase from chloramphenicol-resistant bacteria. Methods Enzymol. 1975;43:737–755. doi: 10.1016/0076-6879(75)43141-x. [DOI] [PubMed] [Google Scholar]
  22. Shaw W. V. Chloramphenicol acetyltransferase: enzymology and molecular biology. CRC Crit Rev Biochem. 1983;14(1):1–46. doi: 10.3109/10409238309102789. [DOI] [PubMed] [Google Scholar]
  23. Yansura D. G., Henner D. J. Use of the Escherichia coli lac repressor and operator to control gene expression in Bacillus subtilis. Proc Natl Acad Sci U S A. 1984 Jan;81(2):439–443. doi: 10.1073/pnas.81.2.439. [DOI] [PMC free article] [PubMed] [Google Scholar]

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