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A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance
Glutaredoxins represent a ubiquitous family of proteins that catalyze the reduction of disulfide bonds in their substrate proteins by use of reduced glutathione. In an attempt to identify the full complement of glutaredoxins in baker's yeast, we found three so-far uncharacterized glutaredoxin-l...
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Published in: | Molecular biology of the cell 2008-06, Vol.19 (6), p.2673-2680 |
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description | Glutaredoxins represent a ubiquitous family of proteins that catalyze the reduction of disulfide bonds in their substrate proteins by use of reduced glutathione. In an attempt to identify the full complement of glutaredoxins in baker's yeast, we found three so-far uncharacterized glutaredoxin-like proteins that we named Grx6, Grx7, and Grx8. Grx6 and Grx7 represent closely related monothiol glutaredoxins that are synthesized with N-terminal signal sequences. Both proteins are located in the cis-Golgi, thereby representing the first glutaredoxins found in a compartment of the secretory pathway. In contrast to formerly described monothiol glutaredoxins, Grx6 and Grx7, showed a high glutaredoxin activity in vitro. Grx6 and Grx7 overlap in their activity and deletion mutants lacking both proteins show growth defects and a strongly increased sensitivity toward oxidizing agents such as hydrogen peroxide or diamide. Our observations suggest that Grx6 and Grx7 do not play a general role in the oxidative folding of proteins in the early secretory pathway but rather counteract the oxidation of specific thiol groups in substrate proteins. |
doi_str_mv | 10.1091/mbc.E07-09-0896 |
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In an attempt to identify the full complement of glutaredoxins in baker's yeast, we found three so-far uncharacterized glutaredoxin-like proteins that we named Grx6, Grx7, and Grx8. Grx6 and Grx7 represent closely related monothiol glutaredoxins that are synthesized with N-terminal signal sequences. Both proteins are located in the cis-Golgi, thereby representing the first glutaredoxins found in a compartment of the secretory pathway. In contrast to formerly described monothiol glutaredoxins, Grx6 and Grx7, showed a high glutaredoxin activity in vitro. Grx6 and Grx7 overlap in their activity and deletion mutants lacking both proteins show growth defects and a strongly increased sensitivity toward oxidizing agents such as hydrogen peroxide or diamide. Our observations suggest that Grx6 and Grx7 do not play a general role in the oxidative folding of proteins in the early secretory pathway but rather counteract the oxidation of specific thiol groups in substrate proteins.</description><identifier>ISSN: 1059-1524</identifier><identifier>ISSN: 1939-4586</identifier><identifier>EISSN: 1939-4586</identifier><identifier>DOI: 10.1091/mbc.E07-09-0896</identifier><identifier>PMID: 18400945</identifier><language>eng</language><publisher>United States: The American Society for Cell Biology</publisher><subject>Cell Fractionation ; Cell Membrane - drug effects ; Cell Membrane - metabolism ; Fluorescent Antibody Technique ; Gene Deletion ; Glutaredoxins - chemistry ; Glutaredoxins - metabolism ; Golgi Apparatus - drug effects ; Golgi Apparatus - metabolism ; Oxidants - pharmacology ; Oxidative Stress - drug effects ; Protein Folding ; Protein Structure, Tertiary ; Protein Transport - drug effects ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - drug effects ; Saccharomyces cerevisiae - growth & development ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - metabolism ; Sequence Homology, Amino Acid ; Solubility - drug effects</subject><ispartof>Molecular biology of the cell, 2008-06, Vol.19 (6), p.2673-2680</ispartof><rights>2008 by The American Society for Cell Biology 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c427t-f25f4fcce1ee9e39af31f8686f50ce30e8e55f3c90956c17150b3354b8ebf6063</citedby><cites>FETCH-LOGICAL-c427t-f25f4fcce1ee9e39af31f8686f50ce30e8e55f3c90956c17150b3354b8ebf6063</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2397307/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2397307/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18400945$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Brodsky, Jeffrey</contributor><creatorcontrib>Mesecke, Nikola</creatorcontrib><creatorcontrib>Spang, Anne</creatorcontrib><creatorcontrib>Deponte, Marcel</creatorcontrib><creatorcontrib>Herrmann, Johannes M</creatorcontrib><title>A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance</title><title>Molecular biology of the cell</title><addtitle>Mol Biol Cell</addtitle><description>Glutaredoxins represent a ubiquitous family of proteins that catalyze the reduction of disulfide bonds in their substrate proteins by use of reduced glutathione. In an attempt to identify the full complement of glutaredoxins in baker's yeast, we found three so-far uncharacterized glutaredoxin-like proteins that we named Grx6, Grx7, and Grx8. Grx6 and Grx7 represent closely related monothiol glutaredoxins that are synthesized with N-terminal signal sequences. Both proteins are located in the cis-Golgi, thereby representing the first glutaredoxins found in a compartment of the secretory pathway. In contrast to formerly described monothiol glutaredoxins, Grx6 and Grx7, showed a high glutaredoxin activity in vitro. Grx6 and Grx7 overlap in their activity and deletion mutants lacking both proteins show growth defects and a strongly increased sensitivity toward oxidizing agents such as hydrogen peroxide or diamide. 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Spang, Anne ; Deponte, Marcel ; Herrmann, Johannes M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c427t-f25f4fcce1ee9e39af31f8686f50ce30e8e55f3c90956c17150b3354b8ebf6063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Cell Fractionation</topic><topic>Cell Membrane - drug effects</topic><topic>Cell Membrane - metabolism</topic><topic>Fluorescent Antibody Technique</topic><topic>Gene Deletion</topic><topic>Glutaredoxins - chemistry</topic><topic>Glutaredoxins - metabolism</topic><topic>Golgi Apparatus - drug effects</topic><topic>Golgi Apparatus - metabolism</topic><topic>Oxidants - pharmacology</topic><topic>Oxidative Stress - drug effects</topic><topic>Protein Folding</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Transport - drug effects</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - drug effects</topic><topic>Saccharomyces cerevisiae - growth & development</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Solubility - drug effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mesecke, Nikola</creatorcontrib><creatorcontrib>Spang, Anne</creatorcontrib><creatorcontrib>Deponte, Marcel</creatorcontrib><creatorcontrib>Herrmann, Johannes M</creatorcontrib><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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular biology of the cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mesecke, Nikola</au><au>Spang, Anne</au><au>Deponte, Marcel</au><au>Herrmann, Johannes M</au><au>Brodsky, Jeffrey</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2008-06</date><risdate>2008</risdate><volume>19</volume><issue>6</issue><spage>2673</spage><epage>2680</epage><pages>2673-2680</pages><issn>1059-1524</issn><issn>1939-4586</issn><eissn>1939-4586</eissn><abstract>Glutaredoxins represent a ubiquitous family of proteins that catalyze the reduction of disulfide bonds in their substrate proteins by use of reduced glutathione. 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subjects | Cell Fractionation Cell Membrane - drug effects Cell Membrane - metabolism Fluorescent Antibody Technique Gene Deletion Glutaredoxins - chemistry Glutaredoxins - metabolism Golgi Apparatus - drug effects Golgi Apparatus - metabolism Oxidants - pharmacology Oxidative Stress - drug effects Protein Folding Protein Structure, Tertiary Protein Transport - drug effects Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - drug effects Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Sequence Homology, Amino Acid Solubility - drug effects |
title | A novel group of glutaredoxins in the cis-Golgi critical for oxidative stress resistance |
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