Heat-induced chaperone activity of serine/threonine protein phosphatase 5 enhances thermotolerance in Arabidopsis thaliana
• This study reports that Arabidopsis thaliana protein serine/threonine phosphatase 5 (AtPP5) plays a pivotal role in heat stress resistance. A high-molecular-weight (HMW) form of AtPP5 was isolated from heat-treated A. thaliana suspension cells. AtPP5 performs multiple functions, acting as a protei...
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| Veröffentlicht in: | The New phytologist 2011-08, Vol.191 (3), p.692-705 |
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| creator | Park, Jin Ho Lee, Sun Yong Kim, Woe Yeon Jung, Young Jun Chae, Ho Byoung Jung, Hyun Suk Kang, Chang Ho Shin, Mi Rim Kim, Sun Young Su'udi, Mukhamad Yun, Dae Jin Lee, Kyun Oh Kim, Min Gab Lee, Sang Yeol |
| description | • This study reports that Arabidopsis thaliana protein serine/threonine phosphatase 5 (AtPP5) plays a pivotal role in heat stress resistance. A high-molecular-weight (HMW) form of AtPP5 was isolated from heat-treated A. thaliana suspension cells. AtPP5 performs multiple functions, acting as a protein phosphatase, foldase chaperone, and holdase chaperone. The enzymatic activities of this versatile protein are closely associated with its oligomeric status, ranging from low oligomeric protein species to HMW complexes. • The phosphatase and foldase chaperone functions of AtPP5 are associated primarily with the low-molecular-weight (LMW) form, whereas the HMW form exhibits holdase chaperone activity. Transgenic over-expression of AtPP5 conferred enhanced heat shock resistance to wild-type A. thaliana and a T-DNA insertion knock-out mutant was defective in acquired thermotolerance. A recombinant phosphatase mutant (H290N) showed markedly increased holdase chaperone activity. • In addition, enhanced thermotolerance was observed in transgenic plants over-expressing H290N, which suggests that the holdase chaperone activity of AtPP5 is primarily responsible for AtPP5-mediated thermotolerance. • Collectively, the results from this study provide the first evidence that AtPP5 performs multiple enzymatic activities that are mediated by conformational changes induced by heat-shock stress. |
| doi_str_mv | 10.1111/j.1469-8137.2011.03734.x |
| format | Article |
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A high-molecular-weight (HMW) form of AtPP5 was isolated from heat-treated A. thaliana suspension cells. AtPP5 performs multiple functions, acting as a protein phosphatase, foldase chaperone, and holdase chaperone. The enzymatic activities of this versatile protein are closely associated with its oligomeric status, ranging from low oligomeric protein species to HMW complexes. • The phosphatase and foldase chaperone functions of AtPP5 are associated primarily with the low-molecular-weight (LMW) form, whereas the HMW form exhibits holdase chaperone activity. Transgenic over-expression of AtPP5 conferred enhanced heat shock resistance to wild-type A. thaliana and a T-DNA insertion knock-out mutant was defective in acquired thermotolerance. A recombinant phosphatase mutant (H290N) showed markedly increased holdase chaperone activity. • In addition, enhanced thermotolerance was observed in transgenic plants over-expressing H290N, which suggests that the holdase chaperone activity of AtPP5 is primarily responsible for AtPP5-mediated thermotolerance. • Collectively, the results from this study provide the first evidence that AtPP5 performs multiple enzymatic activities that are mediated by conformational changes induced by heat-shock stress.</description><identifier>ISSN: 0028-646X</identifier><identifier>EISSN: 1469-8137</identifier><identifier>DOI: 10.1111/j.1469-8137.2011.03734.x</identifier><identifier>PMID: 21564098</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Adaptation, Physiological ; Arabidopsis - chemistry ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis - physiology ; Arabidopsis proteins ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - isolation & purification ; Arabidopsis Proteins - metabolism ; Arabidopsis thaliana ; Biochemistry ; Cells, Cultured ; Deoxyribonucleic acid ; DNA ; Enzymatic activity ; Enzyme activity ; foldase chaperone ; Gels ; Gene Expression Regulation, Plant ; Gene Library ; gene overexpression ; Heat shock ; Heat stress ; Heat stress disorders ; Heat tolerance ; Heat-Shock Response - physiology ; holdase chaperone ; Hot Temperature ; Molecular Chaperones - genetics ; Molecular Chaperones - isolation & purification ; Molecular Chaperones - metabolism ; Mutants ; Mutation ; Nuclear Proteins - genetics ; Nuclear Proteins - isolation & purification ; Nuclear Proteins - metabolism ; Phosphatase ; Phosphatases ; phosphoprotein phosphatase ; Phosphoprotein Phosphatases - genetics ; Phosphoprotein Phosphatases - isolation & purification ; Phosphoprotein Phosphatases - metabolism ; Plants ; Plants, Genetically Modified - chemistry ; Plants, Genetically Modified - genetics ; Plants, Genetically Modified - metabolism ; Plants, Genetically Modified - physiology ; Protein Multimerization ; Protein phosphatase ; Protein-serine/threonine phosphatase ; Proteins ; Recombinant Proteins ; Recombinants ; Seedlings ; Serine ; Shock heating ; Shock resistance ; stress tolerance ; Temperature tolerance ; thermotolerance ; Threonine ; Threonine phosphatase ; transfer DNA ; Transgenic plants ; Weight</subject><ispartof>The New phytologist, 2011-08, Vol.191 (3), p.692-705</ispartof><rights>Copyright © 2011 New Phytologist Trust</rights><rights>2011 The Authors. New Phytologist © 2011 New Phytologist Trust</rights><rights>2011 The Authors. New Phytologist © 2011 New Phytologist Trust.</rights><rights>Copyright Wiley Subscription Services, Inc. Aug 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4924-3c41c7784cfbfb2f855e0179d133ce63e3fed0c72c12a5d6eeddaea518b92193</citedby><cites>FETCH-LOGICAL-c4924-3c41c7784cfbfb2f855e0179d133ce63e3fed0c72c12a5d6eeddaea518b92193</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/20869204$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/20869204$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,1411,1427,27901,27902,45550,45551,46384,46808,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21564098$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Park, Jin Ho</creatorcontrib><creatorcontrib>Lee, Sun Yong</creatorcontrib><creatorcontrib>Kim, Woe Yeon</creatorcontrib><creatorcontrib>Jung, Young Jun</creatorcontrib><creatorcontrib>Chae, Ho Byoung</creatorcontrib><creatorcontrib>Jung, Hyun Suk</creatorcontrib><creatorcontrib>Kang, Chang Ho</creatorcontrib><creatorcontrib>Shin, Mi Rim</creatorcontrib><creatorcontrib>Kim, Sun Young</creatorcontrib><creatorcontrib>Su'udi, Mukhamad</creatorcontrib><creatorcontrib>Yun, Dae Jin</creatorcontrib><creatorcontrib>Lee, Kyun Oh</creatorcontrib><creatorcontrib>Kim, Min Gab</creatorcontrib><creatorcontrib>Lee, Sang Yeol</creatorcontrib><title>Heat-induced chaperone activity of serine/threonine protein phosphatase 5 enhances thermotolerance in Arabidopsis thaliana</title><title>The New phytologist</title><addtitle>New Phytol</addtitle><description>• This study reports that Arabidopsis thaliana protein serine/threonine phosphatase 5 (AtPP5) plays a pivotal role in heat stress resistance. A high-molecular-weight (HMW) form of AtPP5 was isolated from heat-treated A. thaliana suspension cells. AtPP5 performs multiple functions, acting as a protein phosphatase, foldase chaperone, and holdase chaperone. The enzymatic activities of this versatile protein are closely associated with its oligomeric status, ranging from low oligomeric protein species to HMW complexes. • The phosphatase and foldase chaperone functions of AtPP5 are associated primarily with the low-molecular-weight (LMW) form, whereas the HMW form exhibits holdase chaperone activity. Transgenic over-expression of AtPP5 conferred enhanced heat shock resistance to wild-type A. thaliana and a T-DNA insertion knock-out mutant was defective in acquired thermotolerance. A recombinant phosphatase mutant (H290N) showed markedly increased holdase chaperone activity. • In addition, enhanced thermotolerance was observed in transgenic plants over-expressing H290N, which suggests that the holdase chaperone activity of AtPP5 is primarily responsible for AtPP5-mediated thermotolerance. • Collectively, the results from this study provide the first evidence that AtPP5 performs multiple enzymatic activities that are mediated by conformational changes induced by heat-shock stress.</description><subject>Adaptation, Physiological</subject><subject>Arabidopsis - chemistry</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis - physiology</subject><subject>Arabidopsis proteins</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - isolation & purification</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Arabidopsis thaliana</subject><subject>Biochemistry</subject><subject>Cells, Cultured</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Enzymatic activity</subject><subject>Enzyme activity</subject><subject>foldase chaperone</subject><subject>Gels</subject><subject>Gene Expression Regulation, Plant</subject><subject>Gene Library</subject><subject>gene overexpression</subject><subject>Heat shock</subject><subject>Heat stress</subject><subject>Heat stress disorders</subject><subject>Heat tolerance</subject><subject>Heat-Shock Response - physiology</subject><subject>holdase chaperone</subject><subject>Hot Temperature</subject><subject>Molecular Chaperones - genetics</subject><subject>Molecular Chaperones - isolation & purification</subject><subject>Molecular Chaperones - metabolism</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - isolation & purification</subject><subject>Nuclear Proteins - metabolism</subject><subject>Phosphatase</subject><subject>Phosphatases</subject><subject>phosphoprotein phosphatase</subject><subject>Phosphoprotein Phosphatases - genetics</subject><subject>Phosphoprotein Phosphatases - isolation & purification</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Plants</subject><subject>Plants, Genetically Modified - chemistry</subject><subject>Plants, Genetically Modified - genetics</subject><subject>Plants, Genetically Modified - metabolism</subject><subject>Plants, Genetically Modified - physiology</subject><subject>Protein Multimerization</subject><subject>Protein phosphatase</subject><subject>Protein-serine/threonine phosphatase</subject><subject>Proteins</subject><subject>Recombinant Proteins</subject><subject>Recombinants</subject><subject>Seedlings</subject><subject>Serine</subject><subject>Shock heating</subject><subject>Shock resistance</subject><subject>stress tolerance</subject><subject>Temperature tolerance</subject><subject>thermotolerance</subject><subject>Threonine</subject><subject>Threonine phosphatase</subject><subject>transfer DNA</subject><subject>Transgenic plants</subject><subject>Weight</subject><issn>0028-646X</issn><issn>1469-8137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUstu1TAQtRCIXgqfAFhi0VVSPxLHXrCoKspFqgCJIrGzHGdCHOXGwU6gl6_HIaVIrLAXHvk8ZqQzCGFKcprOeZ_TQqhMUl7ljFCaE17xIr99gHb3wEO0I4TJTBTiywl6EmNPCFGlYI_RCaOlKIiSO_RzD2bO3NgsFhpsOzNB8CNgY2f33c1H7FscIbgRzucugB9ThafgZ3Ajnjofp87MJgIuMYydGS1EPHcQDn72A4T1AyfmRTC1a_wU3QqbwZnRPEWPWjNEeHb3nqKbqzc3l_vs-sPbd5cX15ktFCsybgtqq0oWtq3bmrWyLIHQSjWUcwuCA2-hIbZiljJTNgKgaQyYkspaMar4KTrbbNPU3xaIsz64aGEYzAh-iVpWslQi3cR89Q-z90sY02yalVRUrCyoSCy5sWzwMQZo9RTcwYSjpkSv6eheryHoNQS9pqN_p6Nvk_TFXYOlPkBzL_wTRyK83gg_3ADH_zbW7z_u1yrpn2_6Ps4-_PUnUihGVvzlhrfGa_M1uKg_f0pORVqNtCtK8V9n2rM0</recordid><startdate>201108</startdate><enddate>201108</enddate><creator>Park, Jin Ho</creator><creator>Lee, Sun Yong</creator><creator>Kim, Woe Yeon</creator><creator>Jung, Young Jun</creator><creator>Chae, Ho Byoung</creator><creator>Jung, Hyun Suk</creator><creator>Kang, Chang Ho</creator><creator>Shin, Mi Rim</creator><creator>Kim, Sun Young</creator><creator>Su'udi, Mukhamad</creator><creator>Yun, Dae Jin</creator><creator>Lee, Kyun Oh</creator><creator>Kim, Min Gab</creator><creator>Lee, Sang Yeol</creator><general>Blackwell Publishing Ltd</general><general>John Wiley & Sons</general><general>Wiley Subscription Services, Inc</general><scope>FBQ</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>7QO</scope><scope>7SN</scope><scope>8FD</scope><scope>C1K</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>201108</creationdate><title>Heat-induced chaperone activity of serine/threonine protein phosphatase 5 enhances thermotolerance in Arabidopsis thaliana</title><author>Park, Jin Ho ; Lee, Sun Yong ; Kim, Woe Yeon ; Jung, Young Jun ; Chae, Ho Byoung ; Jung, Hyun Suk ; Kang, Chang Ho ; Shin, Mi Rim ; Kim, Sun Young ; Su'udi, Mukhamad ; Yun, Dae Jin ; Lee, Kyun Oh ; Kim, Min Gab ; Lee, Sang Yeol</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4924-3c41c7784cfbfb2f855e0179d133ce63e3fed0c72c12a5d6eeddaea518b92193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Adaptation, Physiological</topic><topic>Arabidopsis - chemistry</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis - physiology</topic><topic>Arabidopsis proteins</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - isolation & purification</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Arabidopsis thaliana</topic><topic>Biochemistry</topic><topic>Cells, Cultured</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>Enzymatic activity</topic><topic>Enzyme activity</topic><topic>foldase chaperone</topic><topic>Gels</topic><topic>Gene Expression Regulation, Plant</topic><topic>Gene Library</topic><topic>gene overexpression</topic><topic>Heat shock</topic><topic>Heat stress</topic><topic>Heat stress disorders</topic><topic>Heat tolerance</topic><topic>Heat-Shock Response - physiology</topic><topic>holdase chaperone</topic><topic>Hot Temperature</topic><topic>Molecular Chaperones - genetics</topic><topic>Molecular Chaperones - isolation & purification</topic><topic>Molecular Chaperones - metabolism</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - isolation & purification</topic><topic>Nuclear Proteins - metabolism</topic><topic>Phosphatase</topic><topic>Phosphatases</topic><topic>phosphoprotein phosphatase</topic><topic>Phosphoprotein Phosphatases - genetics</topic><topic>Phosphoprotein Phosphatases - isolation & purification</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Plants</topic><topic>Plants, Genetically Modified - chemistry</topic><topic>Plants, Genetically Modified - genetics</topic><topic>Plants, Genetically Modified - metabolism</topic><topic>Plants, Genetically Modified - physiology</topic><topic>Protein Multimerization</topic><topic>Protein phosphatase</topic><topic>Protein-serine/threonine phosphatase</topic><topic>Proteins</topic><topic>Recombinant Proteins</topic><topic>Recombinants</topic><topic>Seedlings</topic><topic>Serine</topic><topic>Shock heating</topic><topic>Shock resistance</topic><topic>stress tolerance</topic><topic>Temperature tolerance</topic><topic>thermotolerance</topic><topic>Threonine</topic><topic>Threonine phosphatase</topic><topic>transfer DNA</topic><topic>Transgenic plants</topic><topic>Weight</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Park, Jin Ho</creatorcontrib><creatorcontrib>Lee, Sun Yong</creatorcontrib><creatorcontrib>Kim, Woe Yeon</creatorcontrib><creatorcontrib>Jung, Young Jun</creatorcontrib><creatorcontrib>Chae, Ho Byoung</creatorcontrib><creatorcontrib>Jung, Hyun Suk</creatorcontrib><creatorcontrib>Kang, Chang Ho</creatorcontrib><creatorcontrib>Shin, Mi Rim</creatorcontrib><creatorcontrib>Kim, Sun Young</creatorcontrib><creatorcontrib>Su'udi, Mukhamad</creatorcontrib><creatorcontrib>Yun, Dae Jin</creatorcontrib><creatorcontrib>Lee, Kyun Oh</creatorcontrib><creatorcontrib>Kim, Min Gab</creatorcontrib><creatorcontrib>Lee, Sang Yeol</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Ecology Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The New phytologist</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Park, Jin Ho</au><au>Lee, Sun Yong</au><au>Kim, Woe Yeon</au><au>Jung, Young Jun</au><au>Chae, Ho Byoung</au><au>Jung, Hyun Suk</au><au>Kang, Chang Ho</au><au>Shin, Mi Rim</au><au>Kim, Sun Young</au><au>Su'udi, Mukhamad</au><au>Yun, Dae Jin</au><au>Lee, Kyun Oh</au><au>Kim, Min Gab</au><au>Lee, Sang Yeol</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Heat-induced chaperone activity of serine/threonine protein phosphatase 5 enhances thermotolerance in Arabidopsis thaliana</atitle><jtitle>The New phytologist</jtitle><addtitle>New Phytol</addtitle><date>2011-08</date><risdate>2011</risdate><volume>191</volume><issue>3</issue><spage>692</spage><epage>705</epage><pages>692-705</pages><issn>0028-646X</issn><eissn>1469-8137</eissn><abstract>• This study reports that Arabidopsis thaliana protein serine/threonine phosphatase 5 (AtPP5) plays a pivotal role in heat stress resistance. A high-molecular-weight (HMW) form of AtPP5 was isolated from heat-treated A. thaliana suspension cells. AtPP5 performs multiple functions, acting as a protein phosphatase, foldase chaperone, and holdase chaperone. The enzymatic activities of this versatile protein are closely associated with its oligomeric status, ranging from low oligomeric protein species to HMW complexes. • The phosphatase and foldase chaperone functions of AtPP5 are associated primarily with the low-molecular-weight (LMW) form, whereas the HMW form exhibits holdase chaperone activity. Transgenic over-expression of AtPP5 conferred enhanced heat shock resistance to wild-type A. thaliana and a T-DNA insertion knock-out mutant was defective in acquired thermotolerance. A recombinant phosphatase mutant (H290N) showed markedly increased holdase chaperone activity. • In addition, enhanced thermotolerance was observed in transgenic plants over-expressing H290N, which suggests that the holdase chaperone activity of AtPP5 is primarily responsible for AtPP5-mediated thermotolerance. • Collectively, the results from this study provide the first evidence that AtPP5 performs multiple enzymatic activities that are mediated by conformational changes induced by heat-shock stress.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>21564098</pmid><doi>10.1111/j.1469-8137.2011.03734.x</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adaptation, Physiological Arabidopsis - chemistry Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis - physiology Arabidopsis proteins Arabidopsis Proteins - genetics Arabidopsis Proteins - isolation & purification Arabidopsis Proteins - metabolism Arabidopsis thaliana Biochemistry Cells, Cultured Deoxyribonucleic acid DNA Enzymatic activity Enzyme activity foldase chaperone Gels Gene Expression Regulation, Plant Gene Library gene overexpression Heat shock Heat stress Heat stress disorders Heat tolerance Heat-Shock Response - physiology holdase chaperone Hot Temperature Molecular Chaperones - genetics Molecular Chaperones - isolation & purification Molecular Chaperones - metabolism Mutants Mutation Nuclear Proteins - genetics Nuclear Proteins - isolation & purification Nuclear Proteins - metabolism Phosphatase Phosphatases phosphoprotein phosphatase Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - isolation & purification Phosphoprotein Phosphatases - metabolism Plants Plants, Genetically Modified - chemistry Plants, Genetically Modified - genetics Plants, Genetically Modified - metabolism Plants, Genetically Modified - physiology Protein Multimerization Protein phosphatase Protein-serine/threonine phosphatase Proteins Recombinant Proteins Recombinants Seedlings Serine Shock heating Shock resistance stress tolerance Temperature tolerance thermotolerance Threonine Threonine phosphatase transfer DNA Transgenic plants Weight |
| title | Heat-induced chaperone activity of serine/threonine protein phosphatase 5 enhances thermotolerance in Arabidopsis thaliana |
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