Regeneration of Peroxiredoxins by p53-Regulated Sestrins, Homologs of Bacterial AhpD
Acting as a signal, hydrogen peroxide circumvents antioxidant defense by overoxidizing peroxiredoxins (Prxs), the enzymes that metabolize peroxides. We show that sestrins, a family of proteins whose expression is modulated by p53, are required for regeneration of Prxs containing$Cys-SO_2H$, thus ree...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2004-04, Vol.304 (5670), p.596-600 |
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| creator | Budanov, Andrei V. Sablina, Anna A. Feinstein, Elena Koonin, Eugene V. Chumakov, Peter M. |
| description | Acting as a signal, hydrogen peroxide circumvents antioxidant defense by overoxidizing peroxiredoxins (Prxs), the enzymes that metabolize peroxides. We show that sestrins, a family of proteins whose expression is modulated by p53, are required for regeneration of Prxs containing$Cys-SO_2H$, thus reestablishing the antioxidant firewall. Sestrins contain a predicted redox-active domain homologous to AhpD, the enzyme catalyzing the reduction of a bacterial Prx, AhpC. Purified Hi95 (sestrin 2) protein supports adenosine triphosphate-dependent reduction of overoxidized PrxI in vitro, indicating that unlike AhpD, which is a disulfide reductase, sestrins are cysteine sulfinyl reductases. As modulators of peroxide signaling and antioxidant defense, sestrins constitute potential therapeutic targets. |
| doi_str_mv | 10.1126/science.1095569 |
| format | Article |
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As modulators of peroxide signaling and antioxidant defense, sestrins constitute potential therapeutic targets.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1095569</identifier><identifier>PMID: 15105503</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Amino Acid Sequence ; Amino Acid Substitution ; Antibodies ; Antioxidants ; Antioxidants (Nutrients) ; By products ; Cell Division ; Cell Line, Tumor ; Cell Survival ; Cells ; Cells, Cultured ; Chemical properties ; Disulfides ; Enzymes ; Gels ; Heat-Shock Proteins - chemistry ; Heat-Shock Proteins - genetics ; Heat-Shock Proteins - metabolism ; Humans ; Hydrogen ; Hydrogen peroxide ; Hydrogen Peroxide - metabolism ; Metabolism ; Molecular Sequence Data ; Mutation ; Nuclear Proteins - chemistry ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Oxidation-Reduction ; Oxidoreductases - genetics ; Oxidoreductases - metabolism ; Peroxidases - chemistry ; Peroxidases - metabolism ; Peroxides ; Peroxiredoxins ; Physiological aspects ; Proteins ; Reactive oxygen species ; Reactive Oxygen Species - metabolism ; Recombinant Proteins - metabolism ; RNA, Small Interfering ; Small interfering RNA ; Thioredoxin ; Tumor Suppressor Protein p53 - metabolism</subject><ispartof>Science (American Association for the Advancement of Science), 2004-04, Vol.304 (5670), p.596-600</ispartof><rights>Copyright 2004 American Association for the Advancement of Science</rights><rights>COPYRIGHT 2004 American Association for the Advancement of Science</rights><rights>COPYRIGHT 2004 American Association for the Advancement of Science</rights><rights>Copyright American Association for the Advancement of Science Apr 23, 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c751t-c7b9ac613afa0b258f9b260e7807f077a42e6f366c9843a242f2145521630ff43</citedby><cites>FETCH-LOGICAL-c751t-c7b9ac613afa0b258f9b260e7807f077a42e6f366c9843a242f2145521630ff43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3836727$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3836727$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,777,781,800,2871,2872,27905,27906,57998,58231</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15105503$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Budanov, Andrei V.</creatorcontrib><creatorcontrib>Sablina, Anna A.</creatorcontrib><creatorcontrib>Feinstein, Elena</creatorcontrib><creatorcontrib>Koonin, Eugene V.</creatorcontrib><creatorcontrib>Chumakov, Peter M.</creatorcontrib><title>Regeneration of Peroxiredoxins by p53-Regulated Sestrins, Homologs of Bacterial AhpD</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Acting as a signal, hydrogen peroxide circumvents antioxidant defense by overoxidizing peroxiredoxins (Prxs), the enzymes that metabolize peroxides. We show that sestrins, a family of proteins whose expression is modulated by p53, are required for regeneration of Prxs containing$Cys-SO_2H$, thus reestablishing the antioxidant firewall. Sestrins contain a predicted redox-active domain homologous to AhpD, the enzyme catalyzing the reduction of a bacterial Prx, AhpC. Purified Hi95 (sestrin 2) protein supports adenosine triphosphate-dependent reduction of overoxidized PrxI in vitro, indicating that unlike AhpD, which is a disulfide reductase, sestrins are cysteine sulfinyl reductases. As modulators of peroxide signaling and antioxidant defense, sestrins constitute potential therapeutic targets.</description><subject>Amino Acid Sequence</subject><subject>Amino Acid Substitution</subject><subject>Antibodies</subject><subject>Antioxidants</subject><subject>Antioxidants (Nutrients)</subject><subject>By products</subject><subject>Cell Division</subject><subject>Cell Line, Tumor</subject><subject>Cell Survival</subject><subject>Cells</subject><subject>Cells, Cultured</subject><subject>Chemical properties</subject><subject>Disulfides</subject><subject>Enzymes</subject><subject>Gels</subject><subject>Heat-Shock Proteins - chemistry</subject><subject>Heat-Shock Proteins - genetics</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Hydrogen</subject><subject>Hydrogen peroxide</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>Metabolism</subject><subject>Molecular Sequence 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We show that sestrins, a family of proteins whose expression is modulated by p53, are required for regeneration of Prxs containing$Cys-SO_2H$, thus reestablishing the antioxidant firewall. Sestrins contain a predicted redox-active domain homologous to AhpD, the enzyme catalyzing the reduction of a bacterial Prx, AhpC. Purified Hi95 (sestrin 2) protein supports adenosine triphosphate-dependent reduction of overoxidized PrxI in vitro, indicating that unlike AhpD, which is a disulfide reductase, sestrins are cysteine sulfinyl reductases. As modulators of peroxide signaling and antioxidant defense, sestrins constitute potential therapeutic targets.</abstract><cop>United States</cop><pub>American Association for the Advancement of Science</pub><pmid>15105503</pmid><doi>10.1126/science.1095569</doi><tpages>5</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 2004-04, Vol.304 (5670), p.596-600 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743415566 |
| source | MEDLINE; American Association for the Advancement of Science; Jstor Complete Legacy |
| subjects | Amino Acid Sequence Amino Acid Substitution Antibodies Antioxidants Antioxidants (Nutrients) By products Cell Division Cell Line, Tumor Cell Survival Cells Cells, Cultured Chemical properties Disulfides Enzymes Gels Heat-Shock Proteins - chemistry Heat-Shock Proteins - genetics Heat-Shock Proteins - metabolism Humans Hydrogen Hydrogen peroxide Hydrogen Peroxide - metabolism Metabolism Molecular Sequence Data Mutation Nuclear Proteins - chemistry Nuclear Proteins - genetics Nuclear Proteins - metabolism Oxidation-Reduction Oxidoreductases - genetics Oxidoreductases - metabolism Peroxidases - chemistry Peroxidases - metabolism Peroxides Peroxiredoxins Physiological aspects Proteins Reactive oxygen species Reactive Oxygen Species - metabolism Recombinant Proteins - metabolism RNA, Small Interfering Small interfering RNA Thioredoxin Tumor Suppressor Protein p53 - metabolism |
| title | Regeneration of Peroxiredoxins by p53-Regulated Sestrins, Homologs of Bacterial AhpD |
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