Cyanobacterial metallothionein gene expressed in Escherichia coli Metal-binding properties of the expressed protein
The recently isolated Synechococcus gene smtA encodes the only characterised prokaryotic protein designated to be a metallothionein (MT). To examine the metal-binding properties of its product the smtA gene was expressed in Escherichia coli as a car☐yterminal extension of glutathione- S-transferase....
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| Veröffentlicht in: | FEBS letters 1992-06, Vol.303 (2), p.159-163 |
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| creator | Shi, Jianguo Lindsay, William P. Huckle, James W. Morby, Andrew P. Robinson, Nigel J. |
| description | The recently isolated Synechococcus gene
smtA encodes the only characterised prokaryotic protein designated to be a metallothionein (MT). To examine the metal-binding properties of its product the
smtA gene was expressed in
Escherichia coli as a car☐yterminal extension of glutathione-
S-transferase. The pH of half dissociation of Zn, Cd and Cu ions from the expressed protein was determined to be 4.10, 3.50, 2.35, respectively, indicating a high affinity for these ions (in particular for Zn in comparison to mammalian MT).
E. coli expressing this gene showed enhanced (ca. 3-fold) accumulation of Zn. |
| doi_str_mv | 10.1016/0014-5793(92)80509-F |
| format | Article |
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smtA encodes the only characterised prokaryotic protein designated to be a metallothionein (MT). To examine the metal-binding properties of its product the
smtA gene was expressed in
Escherichia coli as a car☐yterminal extension of glutathione-
S-transferase. The pH of half dissociation of Zn, Cd and Cu ions from the expressed protein was determined to be 4.10, 3.50, 2.35, respectively, indicating a high affinity for these ions (in particular for Zn in comparison to mammalian MT).
E. coli expressing this gene showed enhanced (ca. 3-fold) accumulation of Zn.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/0014-5793(92)80509-F</identifier><identifier>PMID: 1607014</identifier><identifier>CODEN: FEBLAL</identifier><language>eng</language><publisher>Amsterdam: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Anacystis nidulans ; Bacteriology ; Base Sequence ; Biological and medical sciences ; Chromatography, Gel ; Cloning, Molecular ; Cyanobacteria ; Cyanobacteria - genetics ; DNA, Bacterial ; Electrophoresis, Polyacrylamide Gel ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Gene Expression ; Genetics ; Hydrogen-Ion Concentration ; Metal-accumulation ; Metal-tolerance ; Metallothionein - genetics ; Metallothionein - metabolism ; Metals - metabolism ; Microbiology ; Molecular Sequence Data ; Prokaryotic metallothionein ; smtA ; SmtA protein ; Synechococcus</subject><ispartof>FEBS letters, 1992-06, Vol.303 (2), p.159-163</ispartof><rights>1992 Federation of European Biochemical Societies</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-d356baba259b3c2727220a470e579564bec4386283d86166d2c4c60a24f28fd03</citedby><cites>FETCH-LOGICAL-c386t-d356baba259b3c2727220a470e579564bec4386283d86166d2c4c60a24f28fd03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-5793(92)80509-F$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,45974</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5282605$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1607014$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shi, Jianguo</creatorcontrib><creatorcontrib>Lindsay, William P.</creatorcontrib><creatorcontrib>Huckle, James W.</creatorcontrib><creatorcontrib>Morby, Andrew P.</creatorcontrib><creatorcontrib>Robinson, Nigel J.</creatorcontrib><title>Cyanobacterial metallothionein gene expressed in Escherichia coli Metal-binding properties of the expressed protein</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The recently isolated Synechococcus gene
smtA encodes the only characterised prokaryotic protein designated to be a metallothionein (MT). To examine the metal-binding properties of its product the
smtA gene was expressed in
Escherichia coli as a car☐yterminal extension of glutathione-
S-transferase. The pH of half dissociation of Zn, Cd and Cu ions from the expressed protein was determined to be 4.10, 3.50, 2.35, respectively, indicating a high affinity for these ions (in particular for Zn in comparison to mammalian MT).
E. coli expressing this gene showed enhanced (ca. 3-fold) accumulation of Zn.</description><subject>Amino Acid Sequence</subject><subject>Anacystis nidulans</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Chromatography, Gel</subject><subject>Cloning, Molecular</subject><subject>Cyanobacteria</subject><subject>Cyanobacteria - genetics</subject><subject>DNA, Bacterial</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene Expression</subject><subject>Genetics</subject><subject>Hydrogen-Ion Concentration</subject><subject>Metal-accumulation</subject><subject>Metal-tolerance</subject><subject>Metallothionein - genetics</subject><subject>Metallothionein - metabolism</subject><subject>Metals - metabolism</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Prokaryotic metallothionein</subject><subject>smtA</subject><subject>SmtA protein</subject><subject>Synechococcus</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1OAyEUhYnRaP15A01YGKOLUWBmGGZjYhqrJho3uiYM3LGYKVSgRt9eaht1ZVgQON85Fw5Ch5ScU0L5BSG0KuqmLU9bdiZITdpisoFGVDRlUVZcbKLRD7KDdmN8JfksaLuNtiknTdZGKI4_lfOd0gmCVQOeQVLD4NPUegfW4RdwgOFjHiBGMDjfXEc9zayeWoW1Hyx-WFqKzjpj3QueBz-HkCxE7Hucpn_dWUs5dB9t9WqIcLDe99Dz5PppfFvcP97cja_uC10KngpT1rxTnWJ125WaNXkxoqqGQP5RzasOdJVBJkojOOXcMF1pThSreiZ6Q8o9dLLKzXPfFhCTnNmoYRiUA7-IsmFtyzlrMlitQB18jAF6OQ92psKnpEQuu5bLIuWySNky-d21nGTb0Tp_0c3A_JpW5Wb9eK2rqNXQB-W0jT9YzQTjpM7Y5QqD3MW7hSCjtuA0GBtAJ2m8_f8dXyLGnBQ</recordid><startdate>19920601</startdate><enddate>19920601</enddate><creator>Shi, Jianguo</creator><creator>Lindsay, William P.</creator><creator>Huckle, James W.</creator><creator>Morby, Andrew P.</creator><creator>Robinson, Nigel J.</creator><general>Elsevier B.V</general><general>Elsevier</general><scope>6I.</scope><scope>AAFTH</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19920601</creationdate><title>Cyanobacterial metallothionein gene expressed in Escherichia coli Metal-binding properties of the expressed protein</title><author>Shi, Jianguo ; Lindsay, William P. ; Huckle, James W. ; Morby, Andrew P. ; Robinson, Nigel J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-d356baba259b3c2727220a470e579564bec4386283d86166d2c4c60a24f28fd03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Anacystis nidulans</topic><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Chromatography, Gel</topic><topic>Cloning, Molecular</topic><topic>Cyanobacteria</topic><topic>Cyanobacteria - genetics</topic><topic>DNA, Bacterial</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gene Expression</topic><topic>Genetics</topic><topic>Hydrogen-Ion Concentration</topic><topic>Metal-accumulation</topic><topic>Metal-tolerance</topic><topic>Metallothionein - genetics</topic><topic>Metallothionein - metabolism</topic><topic>Metals - metabolism</topic><topic>Microbiology</topic><topic>Molecular Sequence Data</topic><topic>Prokaryotic metallothionein</topic><topic>smtA</topic><topic>SmtA protein</topic><topic>Synechococcus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shi, Jianguo</creatorcontrib><creatorcontrib>Lindsay, William P.</creatorcontrib><creatorcontrib>Huckle, James W.</creatorcontrib><creatorcontrib>Morby, Andrew P.</creatorcontrib><creatorcontrib>Robinson, Nigel J.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shi, Jianguo</au><au>Lindsay, William P.</au><au>Huckle, James W.</au><au>Morby, Andrew P.</au><au>Robinson, Nigel J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cyanobacterial metallothionein gene expressed in Escherichia coli Metal-binding properties of the expressed protein</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1992-06-01</date><risdate>1992</risdate><volume>303</volume><issue>2</issue><spage>159</spage><epage>163</epage><pages>159-163</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><coden>FEBLAL</coden><abstract>The recently isolated Synechococcus gene
smtA encodes the only characterised prokaryotic protein designated to be a metallothionein (MT). To examine the metal-binding properties of its product the
smtA gene was expressed in
Escherichia coli as a car☐yterminal extension of glutathione-
S-transferase. The pH of half dissociation of Zn, Cd and Cu ions from the expressed protein was determined to be 4.10, 3.50, 2.35, respectively, indicating a high affinity for these ions (in particular for Zn in comparison to mammalian MT).
E. coli expressing this gene showed enhanced (ca. 3-fold) accumulation of Zn.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>1607014</pmid><doi>10.1016/0014-5793(92)80509-F</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Anacystis nidulans Bacteriology Base Sequence Biological and medical sciences Chromatography, Gel Cloning, Molecular Cyanobacteria Cyanobacteria - genetics DNA, Bacterial Electrophoresis, Polyacrylamide Gel Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Gene Expression Genetics Hydrogen-Ion Concentration Metal-accumulation Metal-tolerance Metallothionein - genetics Metallothionein - metabolism Metals - metabolism Microbiology Molecular Sequence Data Prokaryotic metallothionein smtA SmtA protein Synechococcus |
| title | Cyanobacterial metallothionein gene expressed in Escherichia coli Metal-binding properties of the expressed protein |
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