{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,1]],"date-time":"2026-08-01T00:10:45Z","timestamp":1785543045899,"version":"3.56.0"},"reference-count":29,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2003,2,1]],"date-time":"2003-02-01T00:00:00Z","timestamp":1044057600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2003,2,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>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 mercury to MerB limits the rate of the coupled reaction with MerA (Bizily et al., 2000). To optimize reaction kinetics for organic mercury compounds, themerB gene was engineered to target MerB for accumulation in the endoplasmic reticulum and for secretion to the cell wall. Plants expressing the targeted MerB proteins and cytoplasmic MerA are highly resistant to organic mercury and degrade organic mercury at 10 to 70 times higher specific activity than plants with the cytoplasmically distributed wild-type MerB enzyme. MerB protein in endoplasmic reticulum-targeted plants appears to accumulate in large vesicular structures that can be visualized in immunolabeled plant cells. These results suggest that the toxic effects of organic mercury are focused in microenvironments of the secretory pathway, that these hydrophobic compartments provide more favorable reaction conditions for MerB activity, and that moderate increases in targeted MerB expression will lead to significant gains in detoxification. In summary, to maximize phytoremediation efficiency of hydrophobic pollutants in plants, it may be beneficial to target enzymes to specific subcellular environments.<\/jats:p>","DOI":"10.1104\/pp.010124","type":"journal-article","created":{"date-parts":[[2003,2,13]],"date-time":"2003-02-13T22:03:05Z","timestamp":1045173785000},"page":"463-471","source":"Crossref","is-referenced-by-count":109,"title":["Subcellular Targeting of Methylmercury Lyase Enhances Its Specific Activity for Organic Mercury Detoxification in Plants"],"prefix":"10.1093","volume":"131","author":[{"given":"Scott P.","family":"Bizily","sequence":"first","affiliation":[{"name":"Genetics Department, University of Georgia, Athens, Georgia 30602"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tehryung","family":"Kim","sequence":"additional","affiliation":[{"name":"Genetics Department, University of Georgia, Athens, Georgia 30602"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Muthugapatti K.","family":"Kandasamy","sequence":"additional","affiliation":[{"name":"Genetics Department, University of Georgia, Athens, Georgia 30602"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Richard B.","family":"Meagher","sequence":"additional","affiliation":[{"name":"Genetics Department, University of Georgia, Athens, Georgia 30602"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2003,2,1]]},"reference":[{"key":"2021042809342976900_R1","doi-asserted-by":"crossref","first-page":"1665","DOI":"10.1021\/es011265w","article-title":"Episodes of elevated methylmercury concentrations in prairie streams.","volume":"36","author":"Balogh","year":"2002","journal-title":"Environ Sci Technol"},{"key":"2021042809342976900_R2","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1104\/pp.119.1.331","article-title":"Regulation of S-like ribonuclease levels in Arabidopsis. 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