Publication Date:
1987-01-09
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Halloran, T -- Walsh, C -- AI07256/AI/NIAID NIH HHS/ -- GM20011/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 9;235(4785):211-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3798107" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Bacterial Proteins/genetics/*isolation & purification
;
Base Sequence
;
Chromatography, Gel
;
DNA/metabolism
;
DNA-Binding Proteins/genetics/*isolation & purification
;
Macromolecular Substances
;
*Mercury
;
Operator Regions, Genetic
;
R Factors/*genetics
;
Transcription, Genetic
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
