Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae
Phytochelatins (PCs) are cysteine-rich peptides that chelate heavy metal ions, thereby mediating heavy metal tolerance in plants, fission yeast, and Caenorhabditis elegans. They are synthesized from glutathione by PC synthase, a specific dipeptidyltransferase. While Saccharomyces cerevisiae synthesi...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 2007-04, Vol.581 (8), p.1681-1687 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1687 |
|---|---|
| container_issue | 8 |
| container_start_page | 1681 |
| container_title | FEBS letters |
| container_volume | 581 |
| creator | Wünschmann, Jana Beck, Andreas Meyer, Laurent Letzel, Thomas Grill, Erwin Lendzian, Klaus J. |
| description | Phytochelatins (PCs) are cysteine-rich peptides that chelate heavy metal ions, thereby mediating heavy metal tolerance in plants, fission yeast, and
Caenorhabditis elegans. They are synthesized from glutathione by PC synthase, a specific dipeptidyltransferase. While
Saccharomyces cerevisiae synthesizes PCs upon exposure to heavy metal ions, the
S. cerevisiae genome does not encode a PC synthase homologue. How PCs are synthesized in yeast is unclear. This study shows that the vacuolar serine carboxypeptidases CPY and CPC are responsible for PC synthesis in yeast. The finding of a PCS-like activity of these enzymes
in vivo discloses another route for PC biosynthesis in eukaryotes. |
| doi_str_mv | 10.1016/j.febslet.2007.03.039 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_70371593</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0014579307003079</els_id><sourcerecordid>19717578</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5259-6c4653c29d8a383f458307d00d55a2fd4d441f7b1e29d16392bc2e2dac2b72f23</originalsourceid><addsrcrecordid>eNqNkV1rFDEUhoModq3-BCVX3s02H5PJ5Eq0tLZQUKheh8zJGTbL7GRNZreOv94Mu-BlhUNCwnPehPMQ8p6zNWe8udque-zygNNaMKbXTJYyL8iKt1pWsm7al2TFGK8rpY28IG9y3rJybrl5TS64rlnbcLMi8H0zTxE2OLgpjJm6hDTP47TBHP6gp91Mp6dIjw4OcXCJZkxhRAoudfH3vMf9FLzLmGkY6aMD2LgUdzOUC8CEx5CDw7fkVe-GjO_O-yX5eXvz4_quevj29f7680MFSihTNVA3SoIwvnWylX2tWsm0Z8wr5UTva1_XvNcdx4LwRhrRgUDhHYhOi17IS_LxlLtP8dcB82R3IQMOgxsxHrLVTGqujHwW5EZzrXRbQHUCIcWcE_Z2n8LOpdlyZhcNdmvPGuyiwTJZypS-D-cHDt0O_b-u89wLcHcCnsKA8_-l2tubL-JxcbooZZqxsixRn05RWEZ7DJhshoAjoA8JYbI-hmd--xf8krL_</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>19717578</pqid></control><display><type>article</type><title>Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae</title><source>Wiley Free Content</source><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Wünschmann, Jana ; Beck, Andreas ; Meyer, Laurent ; Letzel, Thomas ; Grill, Erwin ; Lendzian, Klaus J.</creator><creatorcontrib>Wünschmann, Jana ; Beck, Andreas ; Meyer, Laurent ; Letzel, Thomas ; Grill, Erwin ; Lendzian, Klaus J.</creatorcontrib><description>Phytochelatins (PCs) are cysteine-rich peptides that chelate heavy metal ions, thereby mediating heavy metal tolerance in plants, fission yeast, and
Caenorhabditis elegans. They are synthesized from glutathione by PC synthase, a specific dipeptidyltransferase. While
Saccharomyces cerevisiae synthesizes PCs upon exposure to heavy metal ions, the
S. cerevisiae genome does not encode a PC synthase homologue. How PCs are synthesized in yeast is unclear. This study shows that the vacuolar serine carboxypeptidases CPY and CPC are responsible for PC synthesis in yeast. The finding of a PCS-like activity of these enzymes
in vivo discloses another route for PC biosynthesis in eukaryotes.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2007.03.039</identifier><identifier>PMID: 17408619</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Sequence ; Caenorhabditis elegans ; Carboxypeptidase C ; Carboxypeptidase Y ; Carboxypeptidases - genetics ; Carboxypeptidases - metabolism ; Glutathione ; Glutathione - biosynthesis ; Glutathione - genetics ; Metal tolerance ; Molecular Sequence Data ; Phytochelatins ; S. cerevisiae ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Schizosaccharomyces pombe ; Vacuoles - enzymology</subject><ispartof>FEBS letters, 2007-04, Vol.581 (8), p.1681-1687</ispartof><rights>2007 Federation of European Biochemical Societies</rights><rights>FEBS Letters 581 (2007) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5259-6c4653c29d8a383f458307d00d55a2fd4d441f7b1e29d16392bc2e2dac2b72f23</citedby><cites>FETCH-LOGICAL-c5259-6c4653c29d8a383f458307d00d55a2fd4d441f7b1e29d16392bc2e2dac2b72f23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2007.03.039$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579307003079$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17408619$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wünschmann, Jana</creatorcontrib><creatorcontrib>Beck, Andreas</creatorcontrib><creatorcontrib>Meyer, Laurent</creatorcontrib><creatorcontrib>Letzel, Thomas</creatorcontrib><creatorcontrib>Grill, Erwin</creatorcontrib><creatorcontrib>Lendzian, Klaus J.</creatorcontrib><title>Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Phytochelatins (PCs) are cysteine-rich peptides that chelate heavy metal ions, thereby mediating heavy metal tolerance in plants, fission yeast, and
Caenorhabditis elegans. They are synthesized from glutathione by PC synthase, a specific dipeptidyltransferase. While
Saccharomyces cerevisiae synthesizes PCs upon exposure to heavy metal ions, the
S. cerevisiae genome does not encode a PC synthase homologue. How PCs are synthesized in yeast is unclear. This study shows that the vacuolar serine carboxypeptidases CPY and CPC are responsible for PC synthesis in yeast. The finding of a PCS-like activity of these enzymes
in vivo discloses another route for PC biosynthesis in eukaryotes.</description><subject>Amino Acid Sequence</subject><subject>Caenorhabditis elegans</subject><subject>Carboxypeptidase C</subject><subject>Carboxypeptidase Y</subject><subject>Carboxypeptidases - genetics</subject><subject>Carboxypeptidases - metabolism</subject><subject>Glutathione</subject><subject>Glutathione - biosynthesis</subject><subject>Glutathione - genetics</subject><subject>Metal tolerance</subject><subject>Molecular Sequence Data</subject><subject>Phytochelatins</subject><subject>S. cerevisiae</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Schizosaccharomyces pombe</subject><subject>Vacuoles - enzymology</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkV1rFDEUhoModq3-BCVX3s02H5PJ5Eq0tLZQUKheh8zJGTbL7GRNZreOv94Mu-BlhUNCwnPehPMQ8p6zNWe8udque-zygNNaMKbXTJYyL8iKt1pWsm7al2TFGK8rpY28IG9y3rJybrl5TS64rlnbcLMi8H0zTxE2OLgpjJm6hDTP47TBHP6gp91Mp6dIjw4OcXCJZkxhRAoudfH3vMf9FLzLmGkY6aMD2LgUdzOUC8CEx5CDw7fkVe-GjO_O-yX5eXvz4_quevj29f7680MFSihTNVA3SoIwvnWylX2tWsm0Z8wr5UTva1_XvNcdx4LwRhrRgUDhHYhOi17IS_LxlLtP8dcB82R3IQMOgxsxHrLVTGqujHwW5EZzrXRbQHUCIcWcE_Z2n8LOpdlyZhcNdmvPGuyiwTJZypS-D-cHDt0O_b-u89wLcHcCnsKA8_-l2tubL-JxcbooZZqxsixRn05RWEZ7DJhshoAjoA8JYbI-hmd--xf8krL_</recordid><startdate>20070417</startdate><enddate>20070417</enddate><creator>Wünschmann, Jana</creator><creator>Beck, Andreas</creator><creator>Meyer, Laurent</creator><creator>Letzel, Thomas</creator><creator>Grill, Erwin</creator><creator>Lendzian, Klaus J.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>M7N</scope><scope>7X8</scope></search><sort><creationdate>20070417</creationdate><title>Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae</title><author>Wünschmann, Jana ; Beck, Andreas ; Meyer, Laurent ; Letzel, Thomas ; Grill, Erwin ; Lendzian, Klaus J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5259-6c4653c29d8a383f458307d00d55a2fd4d441f7b1e29d16392bc2e2dac2b72f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Caenorhabditis elegans</topic><topic>Carboxypeptidase C</topic><topic>Carboxypeptidase Y</topic><topic>Carboxypeptidases - genetics</topic><topic>Carboxypeptidases - metabolism</topic><topic>Glutathione</topic><topic>Glutathione - biosynthesis</topic><topic>Glutathione - genetics</topic><topic>Metal tolerance</topic><topic>Molecular Sequence Data</topic><topic>Phytochelatins</topic><topic>S. cerevisiae</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Schizosaccharomyces pombe</topic><topic>Vacuoles - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wünschmann, Jana</creatorcontrib><creatorcontrib>Beck, Andreas</creatorcontrib><creatorcontrib>Meyer, Laurent</creatorcontrib><creatorcontrib>Letzel, Thomas</creatorcontrib><creatorcontrib>Grill, Erwin</creatorcontrib><creatorcontrib>Lendzian, Klaus J.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wünschmann, Jana</au><au>Beck, Andreas</au><au>Meyer, Laurent</au><au>Letzel, Thomas</au><au>Grill, Erwin</au><au>Lendzian, Klaus J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2007-04-17</date><risdate>2007</risdate><volume>581</volume><issue>8</issue><spage>1681</spage><epage>1687</epage><pages>1681-1687</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Phytochelatins (PCs) are cysteine-rich peptides that chelate heavy metal ions, thereby mediating heavy metal tolerance in plants, fission yeast, and
Caenorhabditis elegans. They are synthesized from glutathione by PC synthase, a specific dipeptidyltransferase. While
Saccharomyces cerevisiae synthesizes PCs upon exposure to heavy metal ions, the
S. cerevisiae genome does not encode a PC synthase homologue. How PCs are synthesized in yeast is unclear. This study shows that the vacuolar serine carboxypeptidases CPY and CPC are responsible for PC synthesis in yeast. The finding of a PCS-like activity of these enzymes
in vivo discloses another route for PC biosynthesis in eukaryotes.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>17408619</pmid><doi>10.1016/j.febslet.2007.03.039</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 2007-04, Vol.581 (8), p.1681-1687 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_70371593 |
| source | Wiley Free Content; MEDLINE; ScienceDirect Journals (5 years ago - present); Wiley Online Library Journals Frontfile Complete; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Caenorhabditis elegans Carboxypeptidase C Carboxypeptidase Y Carboxypeptidases - genetics Carboxypeptidases - metabolism Glutathione Glutathione - biosynthesis Glutathione - genetics Metal tolerance Molecular Sequence Data Phytochelatins S. cerevisiae Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Schizosaccharomyces pombe Vacuoles - enzymology |
| title | Phytochelatins are synthesized by two vacuolar serine carboxypeptidases in Saccharomyces cerevisiae |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-02T18%3A40%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Phytochelatins%20are%20synthesized%20by%20two%20vacuolar%20serine%20carboxypeptidases%20in%20Saccharomyces%20cerevisiae&rft.jtitle=FEBS%20letters&rft.au=W%C3%BCnschmann,%20Jana&rft.date=2007-04-17&rft.volume=581&rft.issue=8&rft.spage=1681&rft.epage=1687&rft.pages=1681-1687&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/j.febslet.2007.03.039&rft_dat=%3Cproquest_cross%3E19717578%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=19717578&rft_id=info:pmid/17408619&rft_els_id=S0014579307003079&rfr_iscdi=true |