MerF is a mercury transport protein: different structures but a common mechanism for mercuric ion transporters?

Wilson, J.; Leang, Ching; Morby, Andrew P.; Hobman, Jon L.; Brown, Nigel L.

doi:10.1016/s0014-5793(00)01430-7

Cited by 84 publications

(83 citation statements)

References 32 publications

(36 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In bacteria, genes for mercuric ion transport and cleavage of the carbon-mercury bond are often clustered with those for mercuric ion reduction and transcriptional regulatory control (Wilson et al, 2000). For example, MerT and/or MerC facilitate Hg(II) transport across the plasma membrane.…”

Section: Introductionmentioning

confidence: 99%

Identification of an archaeal mercury regulon by chromatin immunoprecipitation

et al. 2015

View full text Add to dashboard Cite

Mercury is a heavy metal and toxic to all forms of life. Metal exposure can invoke a response to improve survival. In archaea, several components of a mercury response system have been identified, but it is not known whether metal transport is a member of this system. To identify such missing components, a peptide-tagged MerR transcription factor was used to localize enriched chromosome regions by chromosome immunoprecipitation combined with DNA sequence analysis. Such regions could serve as secondary regulatory binding sites to control the expression of additional genes associated with mercury detoxification. Among the 31 highly enriched loci, a subset of five was pursued as potential candidates based on their current annotations. Quantitative reverse transcription-PCR analysis of these regions with and without mercury treatment in WT and mutant strains lacking merR indicated significant regulatory responses under these conditions. Of these, a Family 5 extracellular solute-binding protein and the MarR transcription factor shown previously to control responses to oxidation were most strongly affected. Inactivation of the solute-binding protein by gene disruption increased the resistance of mutant cells to mercury challenge. Inductively coupled plasma-MS analysis of the mutant cell line following metal challenge indicated there was less intracellular mercury compared with the isogenic WT strain. Together, these regulated genes comprise new members of the archaeal MerR regulon and reveal a cascade of transcriptional control not previously demonstrated in this model organism.

show abstract

Section: Introductionmentioning

confidence: 99%

Identification of an archaeal mercury regulon by chromatin immunoprecipitation

et al. 2015

View full text Add to dashboard Cite

show abstract

“…16) In this study, the supportive data for the topological model of MerC are presented; i.e., A. ferrooxidans MerC has four transmembrane domains, two periplasmic loops, and three peptide regions facing the cytoplasm, including both the N-and C-terminal regions. These three proteins have different structures but a common function as mercuric ion transporters.…”

Section: Discussionmentioning

confidence: 83%

“…15) Plasmid pMER327/419 from Pseudomonas fluorescens contains the merF gene between merP and merA, and this gene is also involved in mercuric ion transport. 16) Thus the three genes merT, merC, and merF encode inner membrane mercuric ion transporters in Gram-negative bacteria.…”

Section: -7)mentioning

confidence: 99%

Functional Dissection of a Mercuric Ion Transporter, MerC, fromAcidithiobacillus ferrooxidans

Sasaki

Minakawa

Miyazaki

et al. 2005

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

“…[4][5][6][7][8][9][10][11] These proteins have two, three, or four transmembrane domains (TMD), but TMD I and II are found in all members of the superfamily. 12) In all these proteins, one pair of cysteine residues is predicted to reside within the inner membrane, with or without a second pair of cysteine residues on the cytoplasmic face.…”

mentioning

confidence: 99%

“…6,11,[13][14][15][16] However there is no direct experimental evidence concerning bacterial transport of organomercury until recently.…”

mentioning

confidence: 99%

Role of MerC, MerE, MerF, MerT, and/or MerP in Resistance to Mercurials and the Transport of Mercurials in <i>Escherichia coli</i>

Sone

Nakamura

Pan-Hou

et al. 2013

Biological & Pharmaceutical Bulletin

View full text Add to dashboard Cite

The characteristics of bacteria take up mercury into cells via membrane potential-dependent sequencedivergent members of the mercuric ion (Mer) superfamily, i.e., a periplasmic mercuric ion scavenging protein (MerP) and one or more inner membrane-spanning proteins (MerC, MerE, MerF, and MerT), which transport mercuric ions into the cytoplasm, have been applied in engineering of bioreactor used for mercurial bioremediation. We engineered bacteria to express MerC, MerE, MerF, or MerT with or without MerP to clarify their individual role and potential in transport of mercurial. By immunoblot analysis using specific polyclonal antibody, the proteins encoded by merC, merE, merF, merT or merP, were certainly expressed and identified in the membrane fraction. Bacteria expressing MerC, MerE, MerF or MerT in the absence of MerP transported significantly more C 6 H 5 Hg(I) and Hg(II) across bacterial membrane than their isogenic strain. In vivo expression of MerP in the presence of all the transporters did not cause apparent difference to the C 6 H 5 Hg(I) transport, but gives an apparently higher Hg(II) transport than that did by MerE, MerF or MerT but not by MerC. Among the four transporters studied, MerC showed more potential to transport Hg(II) across bacterial membrane than MerE, MerF and MerT. Together these findings, we demonstrated for the first time that in addition to MerE and MerT, MerF and MerC are broad-spectrum mercury transporters that mediate both Hg(II) and phenylmercury transport into cells. Our results suggested that MerC is the most efficient tool for designing mercurial bioremediation systems, because MerC is sufficient for mercurial transport into cells.

show abstract

MerF is a mercury transport protein: different structures but a common mechanism for mercuric ion transporters?

Cited by 84 publications

References 32 publications

Identification of an archaeal mercury regulon by chromatin immunoprecipitation

Identification of an archaeal mercury regulon by chromatin immunoprecipitation

Functional Dissection of a Mercuric Ion Transporter, MerC, fromAcidithiobacillus ferrooxidans

Role of MerC, MerE, MerF, MerT, and/or MerP in Resistance to Mercurials and the Transport of Mercurials in <i>Escherichia coli</i>

Contact Info

Product

Resources

About