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EXPLORING PROTEIN‐PROTEIN INTERACTIONS IN METAL ION TRANSFERS BETWEEN ENZYMES INVOLVED IN MERCURY DETOXIFICATION
Author(s) -
Miller Susan M.,
Feng Xiaohua,
Harwood Ian,
Hong Baoyu,
Nauss Rachel
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.113.2
Subject(s) - chemistry , enzyme , cytoplasm , detoxification (alternative medicine) , biochemistry , metal , biophysics , biology , organic chemistry , medicine , alternative medicine , pathology
In the major bacterial pathway for mercury resistance, Hg(II) and organomercurials [RHg(I)] undergo facilitated entry into the cytoplasm via an integral membrane transport protein (MerT) and are “detoxified” there by the concerted effort of two enzymes, organomercurial lyase (MerB), which catalyzes cleavage of RHg(I) to Hg(II) and a hydrocarbon, and mercuric ion reductase (MerA), which catalyzes reduction of Hg(II) to Hg(0) as the ultimate detoxification. With the cytoplasmic location of these enzymes and the high toxicity of RHg(I) and Hg(II) due to their affinity for cellular thiols, it is anticipated that proteins in the pathway would have evolved to transfer Hg(II) through direct protein‐protein interactions (MerT‐MerA and MerB‐MerA). Although appealing, evidence supporting this hypothesis is limited. Our current goal is to elucidate the extent to which protein‐protein interactions play a role in metal ion transfers between proteins in the pathway and to understand what type of complexes have evolved to provide the most efficient handling of metal ion for rapid detoxification. Key questions include which protein domains interact and whether they form thermodynamically stable complexes or interact transiently during metal ion transfers. Studies characterizing key players involved in interactions between these proteins will be discussed.