Metalloregulatory DNA-Binding Protein Encoded by the merR Gene: Isolation and Characterization

Details Metalloregulatory DNA-Binding Protein Encoded by the merR Gene: Isolation and Characterization Metalloregulatory DNA-Binding Protein Encoded by the merR Gene: Isolation and Characterization

Jan 1987

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1987sci...235..211o&link_type=abstract

Science, Volume 235, Issue 4785, pp. 211-214

Computer Science

4

Scientific paper

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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