Genetic expression of bacterial merC fused with plant SNARE in Saccharomyces cerevisiae increased mercury accumulation
► We demonstrate Arabidopsis SNAREs can be used as organelle-targeting markers to direct bacterial heavy metal transporter, MerC, to specific membranes in the model eukaryotic organism, yeast. ► We show yeast genetically engineered to express MerC in its plasma membrane accumulated significantly mor...
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creator | Kiyono, Masako Sone, Yuka Miyahara, Kiyomi Oka, Yumiko Nakamura, Masumi Nakamura, Ryosuke Sato, Masa H. Pan-Hou, Hidemitsu Sakabe, Kou Inoue, Ken-ichiro |
description | ► We demonstrate Arabidopsis SNAREs can be used as organelle-targeting markers to direct bacterial heavy metal transporter, MerC, to specific membranes in the model eukaryotic organism, yeast. ► We show yeast genetically engineered to express MerC in its plasma membrane accumulated significantly more mercury than the control cells. ► The use of plant SNARE to direct metal transporter MerC to particular membrane may open new avenues for designing and improving biomass to be more suitable for use in the environmental remediation of toxic metals.
MerC encoded by
merC in the Tn
21 mer operon, is a heavy metal transporter that may be a useful molecular tool for the bioremediation of cadmium and mercury. To regulate subcellular localization, the Arabidopsis SNARE proteins SYP111 and AtVAM3 were fused to the C-terminal end of MerC. In
Saccharomyces cerevisiae, green fluorescent protein (GFP)-MerC-SYP111 fusion proteins located primarily to the plasma membrane, whereas GFP-MerC-AtVAM3 was detected in the vacuolar membranes. These results suggest that SYP111 and AtVAM3 direct MerC fusion proteins to the plasma and vacuolar membranes, respectively. Yeast cells expressing MerC-SYP111 accumulated significantly more mercury than control cells or cells expressing MerC-AtVAM3. Thus, it is possible that localizing MerC to the plasma membrane of plants may represent a similarly promising strategy for improving phytoaccumulation and sequestration of mercury at polluted sites. |
doi_str_mv | 10.1016/j.bej.2011.05.009 |
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MerC encoded by
merC in the Tn
21 mer operon, is a heavy metal transporter that may be a useful molecular tool for the bioremediation of cadmium and mercury. To regulate subcellular localization, the Arabidopsis SNARE proteins SYP111 and AtVAM3 were fused to the C-terminal end of MerC. In
Saccharomyces cerevisiae, green fluorescent protein (GFP)-MerC-SYP111 fusion proteins located primarily to the plasma membrane, whereas GFP-MerC-AtVAM3 was detected in the vacuolar membranes. These results suggest that SYP111 and AtVAM3 direct MerC fusion proteins to the plasma and vacuolar membranes, respectively. Yeast cells expressing MerC-SYP111 accumulated significantly more mercury than control cells or cells expressing MerC-AtVAM3. Thus, it is possible that localizing MerC to the plasma membrane of plants may represent a similarly promising strategy for improving phytoaccumulation and sequestration of mercury at polluted sites.</description><identifier>ISSN: 1369-703X</identifier><identifier>EISSN: 1873-295X</identifier><identifier>DOI: 10.1016/j.bej.2011.05.009</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Arabidopsis ; Bacteria ; Bacterial heavy metal transport ; Biological and medical sciences ; Bioremediation ; Biotechnology ; blood proteins ; cadmium ; Fundamental and applied biological sciences. Psychology ; green fluorescent protein ; heavy metals ; MerC ; Mercury ; operon ; Plant SNARE ; plasma membrane ; Saccharomyces cerevisiae ; yeasts</subject><ispartof>Biochemical engineering journal, 2011-10, Vol.56 (3), p.137-141</ispartof><rights>2011 Elsevier B.V.</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c383t-bbfc04875669b5ae4096f601d0a22a09fd73ed5a491c59c4a18b1978997ff3683</citedby><cites>FETCH-LOGICAL-c383t-bbfc04875669b5ae4096f601d0a22a09fd73ed5a491c59c4a18b1978997ff3683</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1369703X11001501$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=24488423$$DView record in Pascal Francis$$Hfree_for_read</backlink></links><search><creatorcontrib>Kiyono, Masako</creatorcontrib><creatorcontrib>Sone, Yuka</creatorcontrib><creatorcontrib>Miyahara, Kiyomi</creatorcontrib><creatorcontrib>Oka, Yumiko</creatorcontrib><creatorcontrib>Nakamura, Masumi</creatorcontrib><creatorcontrib>Nakamura, Ryosuke</creatorcontrib><creatorcontrib>Sato, Masa H.</creatorcontrib><creatorcontrib>Pan-Hou, Hidemitsu</creatorcontrib><creatorcontrib>Sakabe, Kou</creatorcontrib><creatorcontrib>Inoue, Ken-ichiro</creatorcontrib><title>Genetic expression of bacterial merC fused with plant SNARE in Saccharomyces cerevisiae increased mercury accumulation</title><title>Biochemical engineering journal</title><description>► We demonstrate Arabidopsis SNAREs can be used as organelle-targeting markers to direct bacterial heavy metal transporter, MerC, to specific membranes in the model eukaryotic organism, yeast. ► We show yeast genetically engineered to express MerC in its plasma membrane accumulated significantly more mercury than the control cells. ► The use of plant SNARE to direct metal transporter MerC to particular membrane may open new avenues for designing and improving biomass to be more suitable for use in the environmental remediation of toxic metals.
MerC encoded by
merC in the Tn
21 mer operon, is a heavy metal transporter that may be a useful molecular tool for the bioremediation of cadmium and mercury. To regulate subcellular localization, the Arabidopsis SNARE proteins SYP111 and AtVAM3 were fused to the C-terminal end of MerC. In
Saccharomyces cerevisiae, green fluorescent protein (GFP)-MerC-SYP111 fusion proteins located primarily to the plasma membrane, whereas GFP-MerC-AtVAM3 was detected in the vacuolar membranes. These results suggest that SYP111 and AtVAM3 direct MerC fusion proteins to the plasma and vacuolar membranes, respectively. Yeast cells expressing MerC-SYP111 accumulated significantly more mercury than control cells or cells expressing MerC-AtVAM3. Thus, it is possible that localizing MerC to the plasma membrane of plants may represent a similarly promising strategy for improving phytoaccumulation and sequestration of mercury at polluted sites.</description><subject>Arabidopsis</subject><subject>Bacteria</subject><subject>Bacterial heavy metal transport</subject><subject>Biological and medical sciences</subject><subject>Bioremediation</subject><subject>Biotechnology</subject><subject>blood proteins</subject><subject>cadmium</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>green fluorescent protein</subject><subject>heavy metals</subject><subject>MerC</subject><subject>Mercury</subject><subject>operon</subject><subject>Plant SNARE</subject><subject>plasma membrane</subject><subject>Saccharomyces cerevisiae</subject><subject>yeasts</subject><issn>1369-703X</issn><issn>1873-295X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNp9kc1u1DAUhSMEEqXwAKzwBrFKsOPEP2JVjUpBqkBiqNSddXNzTT3Kz2AnU-bt8Wgqlqxsyd85vv5cFG8FrwQX6uOu6mhX1VyIircV5_ZZcSGMlmVt2_vneS-VLTWX9y-LVyntOOdKan1RHG5ooiUgoz_7SCmFeWKzZx3gQjHAwEaKG-bXRD17DMsD2w8wLWz77erHNQsT2wLiA8R5PCIlhhTpEFIAymcYCU6x3IBrPLJMruM6wJLveF288DAkevO0XhZ3n69_br6Ut99vvm6ubkuURi5l13nkjdGtUrZrgRpulVdc9BzqGrj1vZbUt9BYga3FBoTphNXGWu29VEZeFh_Ovfs4_14pLW4MCWnIj6B5Tc5YWWsjbJNJcSYxzilF8m4fwwjx6AR3J8Vu57Jid1LseOuy4px5_9QOCWHwESYM6V-wbhpjmlpm7t2Z8zA7-BUzc7fNRSp_Qyt1IzLx6UxQlnEIFF3CQBNSHyLh4vo5_GeOvxfRm7k</recordid><startdate>20111015</startdate><enddate>20111015</enddate><creator>Kiyono, Masako</creator><creator>Sone, Yuka</creator><creator>Miyahara, Kiyomi</creator><creator>Oka, Yumiko</creator><creator>Nakamura, Masumi</creator><creator>Nakamura, Ryosuke</creator><creator>Sato, Masa H.</creator><creator>Pan-Hou, Hidemitsu</creator><creator>Sakabe, Kou</creator><creator>Inoue, Ken-ichiro</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>FBQ</scope><scope>IQODW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QO</scope><scope>7T7</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20111015</creationdate><title>Genetic expression of bacterial merC fused with plant SNARE in Saccharomyces cerevisiae increased mercury accumulation</title><author>Kiyono, Masako ; Sone, Yuka ; Miyahara, Kiyomi ; Oka, Yumiko ; Nakamura, Masumi ; Nakamura, Ryosuke ; Sato, Masa H. ; Pan-Hou, Hidemitsu ; Sakabe, Kou ; Inoue, Ken-ichiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c383t-bbfc04875669b5ae4096f601d0a22a09fd73ed5a491c59c4a18b1978997ff3683</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Arabidopsis</topic><topic>Bacteria</topic><topic>Bacterial heavy metal transport</topic><topic>Biological and medical sciences</topic><topic>Bioremediation</topic><topic>Biotechnology</topic><topic>blood proteins</topic><topic>cadmium</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>green fluorescent protein</topic><topic>heavy metals</topic><topic>MerC</topic><topic>Mercury</topic><topic>operon</topic><topic>Plant SNARE</topic><topic>plasma membrane</topic><topic>Saccharomyces cerevisiae</topic><topic>yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kiyono, Masako</creatorcontrib><creatorcontrib>Sone, Yuka</creatorcontrib><creatorcontrib>Miyahara, Kiyomi</creatorcontrib><creatorcontrib>Oka, Yumiko</creatorcontrib><creatorcontrib>Nakamura, Masumi</creatorcontrib><creatorcontrib>Nakamura, Ryosuke</creatorcontrib><creatorcontrib>Sato, Masa H.</creatorcontrib><creatorcontrib>Pan-Hou, Hidemitsu</creatorcontrib><creatorcontrib>Sakabe, Kou</creatorcontrib><creatorcontrib>Inoue, Ken-ichiro</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Biochemical engineering journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kiyono, Masako</au><au>Sone, Yuka</au><au>Miyahara, Kiyomi</au><au>Oka, Yumiko</au><au>Nakamura, Masumi</au><au>Nakamura, Ryosuke</au><au>Sato, Masa H.</au><au>Pan-Hou, Hidemitsu</au><au>Sakabe, Kou</au><au>Inoue, Ken-ichiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Genetic expression of bacterial merC fused with plant SNARE in Saccharomyces cerevisiae increased mercury accumulation</atitle><jtitle>Biochemical engineering journal</jtitle><date>2011-10-15</date><risdate>2011</risdate><volume>56</volume><issue>3</issue><spage>137</spage><epage>141</epage><pages>137-141</pages><issn>1369-703X</issn><eissn>1873-295X</eissn><abstract>► We demonstrate Arabidopsis SNAREs can be used as organelle-targeting markers to direct bacterial heavy metal transporter, MerC, to specific membranes in the model eukaryotic organism, yeast. ► We show yeast genetically engineered to express MerC in its plasma membrane accumulated significantly more mercury than the control cells. ► The use of plant SNARE to direct metal transporter MerC to particular membrane may open new avenues for designing and improving biomass to be more suitable for use in the environmental remediation of toxic metals.
MerC encoded by
merC in the Tn
21 mer operon, is a heavy metal transporter that may be a useful molecular tool for the bioremediation of cadmium and mercury. To regulate subcellular localization, the Arabidopsis SNARE proteins SYP111 and AtVAM3 were fused to the C-terminal end of MerC. In
Saccharomyces cerevisiae, green fluorescent protein (GFP)-MerC-SYP111 fusion proteins located primarily to the plasma membrane, whereas GFP-MerC-AtVAM3 was detected in the vacuolar membranes. These results suggest that SYP111 and AtVAM3 direct MerC fusion proteins to the plasma and vacuolar membranes, respectively. Yeast cells expressing MerC-SYP111 accumulated significantly more mercury than control cells or cells expressing MerC-AtVAM3. Thus, it is possible that localizing MerC to the plasma membrane of plants may represent a similarly promising strategy for improving phytoaccumulation and sequestration of mercury at polluted sites.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><doi>10.1016/j.bej.2011.05.009</doi><tpages>5</tpages></addata></record> |
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subjects | Arabidopsis Bacteria Bacterial heavy metal transport Biological and medical sciences Bioremediation Biotechnology blood proteins cadmium Fundamental and applied biological sciences. Psychology green fluorescent protein heavy metals MerC Mercury operon Plant SNARE plasma membrane Saccharomyces cerevisiae yeasts |
title | Genetic expression of bacterial merC fused with plant SNARE in Saccharomyces cerevisiae increased mercury accumulation |
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