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Science 9 January 1987:
Vol. 235. no. 4785, pp. 211 - 214
DOI: 10.1126/science.3798107
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Articles

Science, Vol 235, Issue 4785, 211-214
Copyright © 1987 by American Association for the Advancement of Science

articles

Metalloregulatory DNA-binding protein encoded by the merR gene: isolation and characterization

T O'Halloran and C Walsh

The MerR protein mediates the induction of the mercury resistance phenotype in bacteria; it has been isolated in order to study the effects of metal-ion induced changes in the metabolism of prokaryotic cells at the molecular level. After DNA sequences responsible for negative autoregulation were removed, the 16-kilodalton protein was overproduced and purified to more than 90 percent homogeneity by a salt extraction procedure that yields about 5 milligrams of protein per gram of cells. Complementation data, amino terminal analysis, gel filtration, and deoxyribonuclease I protection studies demonstrate that the purified merR gene product is a dimer under nondenaturing conditions and that it binds specifically to DNA, in the presence and absence of mercury, at a palindromic site which is directly between the -10 and -35 regions of the structural genes and adjacent to its own promoter. These initial results indicate that MerR is a DNA-binding metalloregulatory protein that plays a central role in this heavy metal responsive system and they delineate an operator site in the mer operon.


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DNA Distortion Mechanism for Transcriptional Activation by ZntR, a Zn(II)-responsive MerR Homologue in Escherichia coli.
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Transition metals in control of gene expression.
T. O'Halloran (1993)
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The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer.
J. Helmann, B. Ballard, and C. Walsh (1990)
Science 247, 946-948
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