Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Subcellular targeting of methylmercury lyase enhances its specific activity for organic mercury detoxification in plants.

Plant physiology - 1 Feb 2003

Bizily Scott P, Kim Tehryung, Kandasamy Muthugapatti K, Meagher Richard B

Abstract excerpt

Methylmercury is an environmental pollutant that biomagnifies in the aquatic food chain with severe consequences for humans and other animals. In an effort to remove this toxin in situ, we have been engineering plants that express the bacterial mercury resistance enzymes organomercurial lyase MerB and mercuric ion reductase MerA. In vivo kinetics experiments suggest that the diffusion of hydrophobic organic...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adaptation, Physiological
Share to Arabidopsis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cell Wall

Share to Endoplasmic Reticulum

Share to Gene Expression Regulation, Enzymologic

Share to Lyases

Share to Mercury

Share to Plants, Genetically Modified

Source

Open in PubMed Open full text

Identifiers

PMID: 12586871
DOI: 10.1104/pp.010124
PMCID: PMC166823

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 11 closest

Subcellular targeting of methylmercury lyase enhances its specific activity for organic mercury detoxification in plants.PMID 12586871Read ↗

Phytodetoxification of hazardous organomercurials by genetically engineered plants.Semantic proximity Read ↗

Phytoremediation of organomercurial compounds via chloroplast genetic engineering.Semantic proximity Read ↗

Characterization of mercury bioremediation by transgenic bacteria expressing metallothionein and polyphosphate kinase.Semantic proximity Read ↗

Expression of the bacterial heavy metal transporter MerC fused with a plant SNARE, SYP121, in Arabidopsis thaliana increases cadmium accumulation and tolerance.Semantic proximity Read ↗

An essential role of s-adenosyl-L-methionine:L-methionine s-methyltransferase in selenium volatilization by plants. Methylation of selenomethionine to selenium-methyl-L-selenium- methionine, the precursor of volatile selenium.Semantic proximity Read ↗

Construction of a synthetic gene for the metalloregulatory protein MerR and analysis of regionally mutated proteins for transcriptional regulation.Semantic proximity Read ↗

The role of cysteine residues in the transport of mercuric ions by the Tn501 MerT and MerP mercury-resistance proteins.Semantic proximity Read ↗

Overexpression of MerT, the mercuric ion transport protein of transposon Tn501, and genetic selection of mercury hypersensitivity mutations.Semantic proximity Read ↗

Crystal structures of the organomercurial lyase MerB in its free and mercury-bound forms: insights into the mechanism of methylmercury degradation.Semantic proximity Read ↗

Vacuolar sequestration of glutathione S-conjugates outcompetes a possible degradation of the glutathione moiety by phytochelatin synthase.Semantic proximity Read ↗

Inhibition of systemic onset of post-transcriptional gene silencing by non-toxic concentrations of cadmium.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.