Abstract
Experiments involving mercury resistance mer operon-lacZ fusions, point mutations in the mercuric ion reductase merA gene, and transcomplementation have revealed that in Hg2+-resistant cells, the inducer Hg2+ concentration is rate determining for activation of transcription. mer operon expression is activated by the presence of nanomolar concentrations of Hg2+ in liquid media only when the mercuric ion reductase function is artificially inactivated in cells, whereas cells with active mercuric ion reductase require micromolar concentrations of Hg2+ for effective induction of the operon.
Full Text
The Full Text of this article is available as a PDF (176.0 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Condee C. W., Summers A. O. A mer-lux transcriptional fusion for real-time examination of in vivo gene expression kinetics and promoter response to altered superhelicity. J Bacteriol. 1992 Dec;174(24):8094–8101. doi: 10.1128/jb.174.24.8094-8101.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Farinha M. A., Kropinski A. M. Construction of broad-host-range plasmid vectors for easy visible selection and analysis of promoters. J Bacteriol. 1990 Jun;172(6):3496–3499. doi: 10.1128/jb.172.6.3496-3499.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Foster T. J., Ginnity F. Some mercurial resistance plasmids from different incompatibility groups specify merR regulatory functions that both repress and induce the mer operon of plasmid R100. J Bacteriol. 1985 May;162(2):773–776. doi: 10.1128/jb.162.2.773-776.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Griffin H. G., Foster T. J., Silver S., Misra T. K. Cloning and DNA sequence of the mercuric- and organomercurial-resistance determinants of plasmid pDU1358. Proc Natl Acad Sci U S A. 1987 May;84(10):3112–3116. doi: 10.1073/pnas.84.10.3112. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Helmann J. D., Shewchuk L. M., Walsh C. T. Regulation of gene expression by mercury. Adv Inorg Biochem. 1990;8:33–61. [PubMed] [Google Scholar]
- Heltzel A., Lee I. W., Totis P. A., Summers A. O. Activator-dependent preinduction binding of sigma-70 RNA polymerase at the metal-regulated mer promoter. Biochemistry. 1990 Oct 16;29(41):9572–9584. doi: 10.1021/bi00493a011. [DOI] [PubMed] [Google Scholar]
- Lee I. W., Gambill B. D., Summers A. O. Translation of merD in Tn21. J Bacteriol. 1989 Apr;171(4):2222–2225. doi: 10.1128/jb.171.4.2222-2225.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Lund P. A., Ford S. J., Brown N. L. Transcriptional regulation of the mercury-resistance genes of transposon Tn501. J Gen Microbiol. 1986 Feb;132(2):465–480. doi: 10.1099/00221287-132-2-465. [DOI] [PubMed] [Google Scholar]
- Misra T. K. Bacterial resistances to inorganic mercury salts and organomercurials. Plasmid. 1992 Jan;27(1):4–16. doi: 10.1016/0147-619x(92)90002-r. [DOI] [PubMed] [Google Scholar]
- Mukhopadhyay D., Yu H. R., Nucifora G., Misra T. K. Purification and functional characterization of MerD. A coregulator of the mercury resistance operon in gram-negative bacteria. J Biol Chem. 1991 Oct 5;266(28):18538–18542. [PubMed] [Google Scholar]
- Nakahara H., Silver S., Miki T., Rownd R. H. Hypersensitivity to Hg2+ and hyperbinding activity associated with cloned fragments of the mercurial resistance operon of plasmid NR1. J Bacteriol. 1979 Oct;140(1):161–166. doi: 10.1128/jb.140.1.161-166.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ni'Bhriain N. N., Silver S., Foster T. J. Tn5 insertion mutations in the mercuric ion resistance genes derived from plasmid R100. J Bacteriol. 1983 Aug;155(2):690–703. doi: 10.1128/jb.155.2.690-703.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Nucifora G., Chu L., Silver S., Misra T. K. Mercury operon regulation by the merR gene of the organomercurial resistance system of plasmid pDU1358. J Bacteriol. 1989 Aug;171(8):4241–4247. doi: 10.1128/jb.171.8.4241-4247.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
- O'Halloran T. V., Frantz B., Shin M. K., Ralston D. M., Wright J. G. The MerR heavy metal receptor mediates positive activation in a topologically novel transcription complex. Cell. 1989 Jan 13;56(1):119–129. doi: 10.1016/0092-8674(89)90990-2. [DOI] [PubMed] [Google Scholar]
- Ralston D. M., O'Halloran T. V. Metalloregulatory proteins and molecular mechanisms of heavy metal signal transduction. Adv Inorg Biochem. 1990;8:1–31. [PubMed] [Google Scholar]
- Ralston D. M., O'Halloran T. V. Ultrasensitivity and heavy-metal selectivity of the allosterically modulated MerR transcription complex. Proc Natl Acad Sci U S A. 1990 May;87(10):3846–3850. doi: 10.1073/pnas.87.10.3846. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Silver S., Walderhaug M. Gene regulation of plasmid- and chromosome-determined inorganic ion transport in bacteria. Microbiol Rev. 1992 Mar;56(1):195–228. doi: 10.1128/mr.56.1.195-228.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Summers A. O. Untwist and shout: a heavy metal-responsive transcriptional regulator. J Bacteriol. 1992 May;174(10):3097–3101. doi: 10.1128/jb.174.10.3097-3101.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yu H., Mukhopadhyay D., Misra T. K. Purification and characterization of a novel organometallic receptor protein regulating the expression of the broad spectrum mercury-resistant operon of plasmid pDU1358. J Biol Chem. 1994 Jun 3;269(22):15697–15702. [PubMed] [Google Scholar]
