2010
DOI: 10.1021/bi100802k
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Direct Measurement of Mercury(II) Removal from Organomercurial Lyase (MerB) by Tryptophan Fluorescence: NmerA Domain of Coevolved γ-Proteobacterial Mercuric Ion Reductase (MerA) Is More Efficient Than MerA Catalytic Core or Glutathione,

Abstract: Aerobic and facultative bacteria and archaea harboring mer loci exhibit resistance to the toxic effects of Hg(II) and organomercurials [RHg(I)]. In broad spectrum resistance, RHg(I) is converted to less toxic Hg(0) in the cytosol by the sequential action of organomercurial lyase (MerB: RHg(I) --> RH + Hg(II)) and mercuric ion reductase (MerA: Hg(II) --> Hg(0)) enzymes, requiring transfer of Hg(II) from MerB to MerA. Although previous studies with γ-proteobacterial versions of MerA and a non-physiological Hg(II… Show more

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Cited by 18 publications
(31 citation statements)
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“…MerH trafficking of Hg(II) may have two distinct roles. By analogy to the actions of bacterial MerP (Gambill & Summers, 1992;Morby et al, 1995;Serre et al, 2004) and the N-terminal bacterial MerA motif (Hong et al, 2010;Ledwidge et al, 2005), archaeal MerH could facilitate metal transfer to MerA for reduction followed by metal efflux in its volatile state. However, as described here, MerH can also control derepression of transcription at the merHp promoter indicating its role in trafficking mercury to the MerR transcription factor.…”
Section: Discussionmentioning
confidence: 99%
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“…MerH trafficking of Hg(II) may have two distinct roles. By analogy to the actions of bacterial MerP (Gambill & Summers, 1992;Morby et al, 1995;Serre et al, 2004) and the N-terminal bacterial MerA motif (Hong et al, 2010;Ledwidge et al, 2005), archaeal MerH could facilitate metal transfer to MerA for reduction followed by metal efflux in its volatile state. However, as described here, MerH can also control derepression of transcription at the merHp promoter indicating its role in trafficking mercury to the MerR transcription factor.…”
Section: Discussionmentioning
confidence: 99%
“…In the case of proteobacteria, the mercury-specific transport protein, MerP, binds and transfers this metal to the integral membrane protein MerT, thereby depleting its concentration in the periplasmic space (Morby et al, 1995;Serre et al, 2004). Cytoplasmic trafficking of mercury has also been reported through transfer between cysteine residues encoded in the N-terminal domain of bacterial mercuric reductase (Hong et al, 2010).…”
Section: Introductionmentioning
confidence: 99%
“…1,9,17,18 Both intermolecular and intramolecular metal ion transfers have been demonstrated to occur between several of these proteins/domains and their cognate partners bearing either the same or a very different structure. [19][20][21][22][23] To date, however, only a few metal-mediated complexes of interacting proteins have proven to be sufficiently stable to allow detailed structural characterization, and all have involved intermolecular interactions between two proteins both having this βαββαβ fold. 19,24,25 Here, we characterize the structural interactions involved in the intramolecular transfer of Hg 2+ between the tethered metallochaperone-like NmerA domain and the C-terminal vicinal cysteine pair in the large catalytic core of a mercuric ion reductase enzyme (MerA).…”
Section: Introductionmentioning
confidence: 99%
“…1 Recent phylogenetic analysis suggests this variation may be associated with differences in the bacterial cellular physiology, especially the type and level of small-molecule thiol buffer used by the organism, 26 and may also be associated with structural variations in other mer pathway proteins. 22 Sequences with a single NmerA domain represent more than half of those identified in GenBank 26 and include the most extensively characterized MerA proteins from the mer loci carried by transposons Tn21 and Tn501, 10,11,22,23,[33][34][35][36][37][38] which are the focus of the study here. These operons were originally isolated on plasmid NR1 from Shigella flexneri 39 and plasmid pVS1 from Pseudomonas aeruginosa PAT, 40,41 respectively.…”
Section: Introductionmentioning
confidence: 99%
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