Activation of Mitochondrial Protein Phosphatase SLP2 by MIA40 Regulates Seed Germination
Reversible protein phosphorylation catalyzed by protein kinases and phosphatases represents the most prolific and wellcharacterized posttranslational modification known. Here, we demonstrate that Arabidopsis (Arabidopsis thaliana) Shewanella-like protein phosphatase 2 (AtSLP2) is a bona fide Ser/Thr...
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| Veröffentlicht in: | Plant physiology (Bethesda) 2017-02, Vol.173 (2), p.956-969 |
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| container_title | Plant physiology (Bethesda) |
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| creator | Uhrig, R. Glen Labandera, Anne-Marie Tang, Lay-Yin Sieben, Nicolas A. Goudreault, Marilyn Yeung, Edward Gingras, Anne-Claude Samuel, Marcus A. Moorhead, Greg B.G. |
| description | Reversible protein phosphorylation catalyzed by protein kinases and phosphatases represents the most prolific and wellcharacterized posttranslational modification known. Here, we demonstrate that Arabidopsis (Arabidopsis thaliana) Shewanella-like protein phosphatase 2 (AtSLP2) is a bona fide Ser/Thr protein phosphatase that is targeted to the mitochondrial intermembrane space (IMS) where it interacts with the mitochondrial oxidoreductase import and assembly protein 40 (AtMIA40), forming a protein complex. Interaction with AtMIA40 is necessary for the phosphatase activity of AtSLP2 and is dependent on the formation of disulfide bridges on AtSLP2. Furthermore, by utilizing atslp2 null mutant, AtSLP2 complemented and AtSLP2 overexpressing plants, we identify a function for the AtSLP2-AtMIA40 complex in negatively regulating gibberellic acid-related processes during seed germination. Results presented here characterize a mitochondrial IMS-localized protein phosphatase identified in photosynthetic eukaryotes as well as a protein phosphatase target of the highly conserved eukaryotic MIA40 IMS oxidoreductase. |
| doi_str_mv | 10.1104/pp.16.01641 |
| format | Article |
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Glen ; Labandera, Anne-Marie ; Tang, Lay-Yin ; Sieben, Nicolas A. ; Goudreault, Marilyn ; Yeung, Edward ; Gingras, Anne-Claude ; Samuel, Marcus A. ; Moorhead, Greg B.G.</creator><creatorcontrib>Uhrig, R. Glen ; Labandera, Anne-Marie ; Tang, Lay-Yin ; Sieben, Nicolas A. ; Goudreault, Marilyn ; Yeung, Edward ; Gingras, Anne-Claude ; Samuel, Marcus A. ; Moorhead, Greg B.G.</creatorcontrib><description>Reversible protein phosphorylation catalyzed by protein kinases and phosphatases represents the most prolific and wellcharacterized posttranslational modification known. Here, we demonstrate that Arabidopsis (Arabidopsis thaliana) Shewanella-like protein phosphatase 2 (AtSLP2) is a bona fide Ser/Thr protein phosphatase that is targeted to the mitochondrial intermembrane space (IMS) where it interacts with the mitochondrial oxidoreductase import and assembly protein 40 (AtMIA40), forming a protein complex. Interaction with AtMIA40 is necessary for the phosphatase activity of AtSLP2 and is dependent on the formation of disulfide bridges on AtSLP2. Furthermore, by utilizing atslp2 null mutant, AtSLP2 complemented and AtSLP2 overexpressing plants, we identify a function for the AtSLP2-AtMIA40 complex in negatively regulating gibberellic acid-related processes during seed germination. Results presented here characterize a mitochondrial IMS-localized protein phosphatase identified in photosynthetic eukaryotes as well as a protein phosphatase target of the highly conserved eukaryotic MIA40 IMS oxidoreductase.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.16.01641</identifier><identifier>PMID: 27923987</identifier><language>eng</language><publisher>United States: American Society of Plant Biologists</publisher><subject>Abscisic Acid - pharmacology ; Amino Acid Sequence ; Arabidopsis - drug effects ; Arabidopsis - embryology ; Arabidopsis - enzymology ; Arabidopsis Proteins - chemistry ; Arabidopsis Proteins - metabolism ; BIOCHEMISTRY AND METABOLISM ; Biosynthetic Pathways - drug effects ; Disulfides - metabolism ; Enzyme Activation - drug effects ; Germination - drug effects ; Gibberellins - biosynthesis ; Mitochondria - drug effects ; Mitochondria - enzymology ; Mitochondrial Membranes - drug effects ; Mitochondrial Membranes - metabolism ; Mitochondrial Proteins - chemistry ; Mitochondrial Proteins - metabolism ; Models, Biological ; Oxidation-Reduction - drug effects ; Protein Binding - drug effects ; Protein Transport - drug effects ; Seeds - drug effects ; Seeds - embryology ; Seeds - metabolism ; Sequence Alignment ; Substrate Specificity - drug effects ; Triazoles - pharmacology</subject><ispartof>Plant physiology (Bethesda), 2017-02, Vol.173 (2), p.956-969</ispartof><rights>Copyright © 2017 American Society of Plant Biologists</rights><rights>2017 American Society of Plant Biologists. All Rights Reserved.</rights><rights>2017 American Society of Plant Biologists. All Rights Reserved. 2017</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c403t-28ee64a2a461410730092da7699d598fb9398fa91314dc864a0825931418cb43</citedby><orcidid>0000-0003-3282-7590 ; 0000-0003-2773-4381 ; 0000-0002-0593-4166 ; 0000-0002-7981-7827</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/24877407$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/24877407$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27903,27904,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27923987$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Uhrig, R. Glen</creatorcontrib><creatorcontrib>Labandera, Anne-Marie</creatorcontrib><creatorcontrib>Tang, Lay-Yin</creatorcontrib><creatorcontrib>Sieben, Nicolas A.</creatorcontrib><creatorcontrib>Goudreault, Marilyn</creatorcontrib><creatorcontrib>Yeung, Edward</creatorcontrib><creatorcontrib>Gingras, Anne-Claude</creatorcontrib><creatorcontrib>Samuel, Marcus A.</creatorcontrib><creatorcontrib>Moorhead, Greg B.G.</creatorcontrib><title>Activation of Mitochondrial Protein Phosphatase SLP2 by MIA40 Regulates Seed Germination</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>Reversible protein phosphorylation catalyzed by protein kinases and phosphatases represents the most prolific and wellcharacterized posttranslational modification known. Here, we demonstrate that Arabidopsis (Arabidopsis thaliana) Shewanella-like protein phosphatase 2 (AtSLP2) is a bona fide Ser/Thr protein phosphatase that is targeted to the mitochondrial intermembrane space (IMS) where it interacts with the mitochondrial oxidoreductase import and assembly protein 40 (AtMIA40), forming a protein complex. Interaction with AtMIA40 is necessary for the phosphatase activity of AtSLP2 and is dependent on the formation of disulfide bridges on AtSLP2. Furthermore, by utilizing atslp2 null mutant, AtSLP2 complemented and AtSLP2 overexpressing plants, we identify a function for the AtSLP2-AtMIA40 complex in negatively regulating gibberellic acid-related processes during seed germination. Results presented here characterize a mitochondrial IMS-localized protein phosphatase identified in photosynthetic eukaryotes as well as a protein phosphatase target of the highly conserved eukaryotic MIA40 IMS oxidoreductase.</description><subject>Abscisic Acid - pharmacology</subject><subject>Amino Acid Sequence</subject><subject>Arabidopsis - drug effects</subject><subject>Arabidopsis - embryology</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis Proteins - chemistry</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>BIOCHEMISTRY AND METABOLISM</subject><subject>Biosynthetic Pathways - drug effects</subject><subject>Disulfides - metabolism</subject><subject>Enzyme Activation - drug effects</subject><subject>Germination - drug effects</subject><subject>Gibberellins - biosynthesis</subject><subject>Mitochondria - drug effects</subject><subject>Mitochondria - enzymology</subject><subject>Mitochondrial Membranes - drug effects</subject><subject>Mitochondrial Membranes - metabolism</subject><subject>Mitochondrial Proteins - chemistry</subject><subject>Mitochondrial Proteins - metabolism</subject><subject>Models, Biological</subject><subject>Oxidation-Reduction - drug effects</subject><subject>Protein Binding - drug effects</subject><subject>Protein Transport - drug effects</subject><subject>Seeds - drug effects</subject><subject>Seeds - embryology</subject><subject>Seeds - metabolism</subject><subject>Sequence Alignment</subject><subject>Substrate Specificity - drug effects</subject><subject>Triazoles - pharmacology</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkctLAzEQxoMoWqsnz0qOgrRmstnd5CIU8VFosVgP3kK6m7Up282apIL_venD12lmmB_ffHyD0BmQPgBh123bh6xPIGOwhzqQJrRHU8b3UYeQ2BPOxRE69n5BCIEE2CE6ormgieB5B70OimA-VDC2wbbCYxNsMbdN6Yyq8cTZoE2DJ3Pr27kKyms8HU0onn3i8XDACH7Wb6taBe3xVOsSP2i3NM1G7QQdVKr2-nRXu-jl_u7l9rE3enoY3g5GvYKRJPQo1zpjiiqWAQOSJ4QIWqo8E6JMBa9mIvqslFgbLwseUcJpKuIEvJixpItutrLtarbUZaGb4FQtW2eWyn1Kq4z8v2nMXL7ZD5lSEcNLosDlTsDZ95X2QS6NL3Rdq0bblZfAWZaDEBlE9GqLFs5673T1cwaIXL9Ctq2ETG5eEemLv85-2O_sI3C-BRY-WPe7ZzzPWUziC9JhjQU</recordid><startdate>20170201</startdate><enddate>20170201</enddate><creator>Uhrig, R. 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Glen ; Labandera, Anne-Marie ; Tang, Lay-Yin ; Sieben, Nicolas A. ; Goudreault, Marilyn ; Yeung, Edward ; Gingras, Anne-Claude ; Samuel, Marcus A. ; Moorhead, Greg B.G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c403t-28ee64a2a461410730092da7699d598fb9398fa91314dc864a0825931418cb43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Abscisic Acid - pharmacology</topic><topic>Amino Acid Sequence</topic><topic>Arabidopsis - drug effects</topic><topic>Arabidopsis - embryology</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis Proteins - chemistry</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>BIOCHEMISTRY AND METABOLISM</topic><topic>Biosynthetic Pathways - drug effects</topic><topic>Disulfides - metabolism</topic><topic>Enzyme Activation - drug effects</topic><topic>Germination - drug effects</topic><topic>Gibberellins - biosynthesis</topic><topic>Mitochondria - drug effects</topic><topic>Mitochondria - enzymology</topic><topic>Mitochondrial Membranes - drug effects</topic><topic>Mitochondrial Membranes - metabolism</topic><topic>Mitochondrial Proteins - chemistry</topic><topic>Mitochondrial Proteins - metabolism</topic><topic>Models, Biological</topic><topic>Oxidation-Reduction - drug effects</topic><topic>Protein Binding - drug effects</topic><topic>Protein Transport - drug effects</topic><topic>Seeds - drug effects</topic><topic>Seeds - embryology</topic><topic>Seeds - metabolism</topic><topic>Sequence Alignment</topic><topic>Substrate Specificity - drug effects</topic><topic>Triazoles - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Uhrig, R. 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Glen</au><au>Labandera, Anne-Marie</au><au>Tang, Lay-Yin</au><au>Sieben, Nicolas A.</au><au>Goudreault, Marilyn</au><au>Yeung, Edward</au><au>Gingras, Anne-Claude</au><au>Samuel, Marcus A.</au><au>Moorhead, Greg B.G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of Mitochondrial Protein Phosphatase SLP2 by MIA40 Regulates Seed Germination</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2017-02-01</date><risdate>2017</risdate><volume>173</volume><issue>2</issue><spage>956</spage><epage>969</epage><pages>956-969</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><abstract>Reversible protein phosphorylation catalyzed by protein kinases and phosphatases represents the most prolific and wellcharacterized posttranslational modification known. Here, we demonstrate that Arabidopsis (Arabidopsis thaliana) Shewanella-like protein phosphatase 2 (AtSLP2) is a bona fide Ser/Thr protein phosphatase that is targeted to the mitochondrial intermembrane space (IMS) where it interacts with the mitochondrial oxidoreductase import and assembly protein 40 (AtMIA40), forming a protein complex. Interaction with AtMIA40 is necessary for the phosphatase activity of AtSLP2 and is dependent on the formation of disulfide bridges on AtSLP2. Furthermore, by utilizing atslp2 null mutant, AtSLP2 complemented and AtSLP2 overexpressing plants, we identify a function for the AtSLP2-AtMIA40 complex in negatively regulating gibberellic acid-related processes during seed germination. 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| ispartof | Plant physiology (Bethesda), 2017-02, Vol.173 (2), p.956-969 |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current) |
| subjects | Abscisic Acid - pharmacology Amino Acid Sequence Arabidopsis - drug effects Arabidopsis - embryology Arabidopsis - enzymology Arabidopsis Proteins - chemistry Arabidopsis Proteins - metabolism BIOCHEMISTRY AND METABOLISM Biosynthetic Pathways - drug effects Disulfides - metabolism Enzyme Activation - drug effects Germination - drug effects Gibberellins - biosynthesis Mitochondria - drug effects Mitochondria - enzymology Mitochondrial Membranes - drug effects Mitochondrial Membranes - metabolism Mitochondrial Proteins - chemistry Mitochondrial Proteins - metabolism Models, Biological Oxidation-Reduction - drug effects Protein Binding - drug effects Protein Transport - drug effects Seeds - drug effects Seeds - embryology Seeds - metabolism Sequence Alignment Substrate Specificity - drug effects Triazoles - pharmacology |
| title | Activation of Mitochondrial Protein Phosphatase SLP2 by MIA40 Regulates Seed Germination |
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