Molecular Characterization of a Dehydroascorbate Reductase from Pinus bungeana
Dehydroascorbate reductase （DHAR） plays a critical role in the ascorbate-glutathione recycling reaction for most higher plants. To date, studies on DHAR in higher plants have focused largely on Arabidopsis and agricultural plants, and there is virtually no information on the molecular characteristic...
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| Veröffentlicht in: | Journal of integrative plant biology 2009-11, Vol.51 (11), p.993-1001 |
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| creator | Yang, Hai-Ling Zhao, Ying-Ru Wang, Cai-Ling Yang, Zhi-Ling Zeng, Qing-Yin Lu, Hai |
| description | Dehydroascorbate reductase （DHAR） plays a critical role in the ascorbate-glutathione recycling reaction for most higher plants. To date, studies on DHAR in higher plants have focused largely on Arabidopsis and agricultural plants, and there is virtually no information on the molecular characteristics of DHAR in gymnosperms. The present study reports the cloning and characteristics of a DHAR （PbDHAR） from a pine, Pinus bungeana Zucc. ex Endl. The PbDHAR gene encodes a protein of 215 amino acid residues with a calculated molecular mass of 24.26 kDa. The predicted 3-D structure of PbDHAR showed a typical glutathione S-transferase fold. Reverse transcripUon-polymerase chain reaction revealed that the PbDHAR was a constitutive expression gene in P. bungeana. The expression level of PbDHAR mRNA in P. bungeana seedlings did not show significant change under high temperature stress. The recombinant PbDHAR was overexpressed in Escherichia coil following purification with affinity chromatography. The recombinant PbDHAR exhibited enzymatic activity （19.84 i.mnol/min per mg） and high affinity （a Krn of 0.08 mM） towards the substrates dehydroascorbate （DHA）. Moreover, the recombinant PbDHAR was a thermostable enzyme, and retained 77% of its initial activity at 55℃. The present study is the first to provide a detailed molecular characterization of the DHAR in P. bungeana. |
| doi_str_mv | 10.1111/j.1744-7909.2009.00848.x |
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To date, studies on DHAR in higher plants have focused largely on Arabidopsis and agricultural plants, and there is virtually no information on the molecular characteristics of DHAR in gymnosperms. The present study reports the cloning and characteristics of a DHAR （PbDHAR） from a pine, Pinus bungeana Zucc. ex Endl. The PbDHAR gene encodes a protein of 215 amino acid residues with a calculated molecular mass of 24.26 kDa. The predicted 3-D structure of PbDHAR showed a typical glutathione S-transferase fold. Reverse transcripUon-polymerase chain reaction revealed that the PbDHAR was a constitutive expression gene in P. bungeana. The expression level of PbDHAR mRNA in P. bungeana seedlings did not show significant change under high temperature stress. The recombinant PbDHAR was overexpressed in Escherichia coil following purification with affinity chromatography. The recombinant PbDHAR exhibited enzymatic activity （19.84 i.mnol/min per mg） and high affinity （a Krn of 0.08 mM） towards the substrates dehydroascorbate （DHA）. Moreover, the recombinant PbDHAR was a thermostable enzyme, and retained 77% of its initial activity at 55℃. The present study is the first to provide a detailed molecular characterization of the DHAR in P. bungeana.</description><identifier>ISSN: 1672-9072</identifier><identifier>EISSN: 1744-7909</identifier><identifier>DOI: 10.1111/j.1744-7909.2009.00848.x</identifier><identifier>PMID: 19903221</identifier><language>eng</language><publisher>Melbourne, Australia: Melbourne, Australia : Blackwell Publishing Asia</publisher><subject>Amino Acid Sequence ; Arabidopsis ; Base Sequence ; cloning ; Cloning, Molecular ; dehydroascorbate reductase ; Dehydroascorbic Acid - metabolism ; DNA, Complementary - genetics ; Electrophoresis, Polyacrylamide Gel ; enzyme activity ; Enzyme Stability ; Escherichia coli ; Gene Expression Profiling ; Gene Expression Regulation, Plant ; Genes, Plant - genetics ; Glutathione - metabolism ; glutathione dehydrogenase (ascorbate) ; gymnosperm ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; mRNA表达水平 ; Oxidoreductases - chemistry ; Oxidoreductases - genetics ; Oxidoreductases - metabolism ; Pinus ; Pinus - enzymology ; Pinus - genetics ; Protein Structure, Secondary ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; Sequence Alignment ; Sequence Analysis, DNA ; Structural Homology, Protein ; Substrate Specificity ; Temperature ; 分子特征 ; 白皮松 ; 聚合酶链反应 ; 脱氢抗坏血酸还原酶 ; 谷胱甘肽 ; 高等植物</subject><ispartof>Journal of integrative plant biology, 2009-11, Vol.51 (11), p.993-1001</ispartof><rights>2009 Institute of Botany, the Chinese Academy of Sciences</rights><rights>Copyright © Wanfang Data Co. Ltd. All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5848-a3b1f8fc2b492facc13e39583e873e9cc6c08a0f52e54b5b85c3737a317a14e03</citedby><cites>FETCH-LOGICAL-c5848-a3b1f8fc2b492facc13e39583e873e9cc6c08a0f52e54b5b85c3737a317a14e03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://image.cqvip.com/vip1000/qk/94176A/94176A.jpg</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1744-7909.2009.00848.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1744-7909.2009.00848.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19903221$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Hai-Ling</creatorcontrib><creatorcontrib>Zhao, Ying-Ru</creatorcontrib><creatorcontrib>Wang, Cai-Ling</creatorcontrib><creatorcontrib>Yang, Zhi-Ling</creatorcontrib><creatorcontrib>Zeng, Qing-Yin</creatorcontrib><creatorcontrib>Lu, Hai</creatorcontrib><title>Molecular Characterization of a Dehydroascorbate Reductase from Pinus bungeana</title><title>Journal of integrative plant biology</title><addtitle>Journal of Integrative Plant Biology</addtitle><description>Dehydroascorbate reductase （DHAR） plays a critical role in the ascorbate-glutathione recycling reaction for most higher plants. To date, studies on DHAR in higher plants have focused largely on Arabidopsis and agricultural plants, and there is virtually no information on the molecular characteristics of DHAR in gymnosperms. The present study reports the cloning and characteristics of a DHAR （PbDHAR） from a pine, Pinus bungeana Zucc. ex Endl. The PbDHAR gene encodes a protein of 215 amino acid residues with a calculated molecular mass of 24.26 kDa. The predicted 3-D structure of PbDHAR showed a typical glutathione S-transferase fold. Reverse transcripUon-polymerase chain reaction revealed that the PbDHAR was a constitutive expression gene in P. bungeana. The expression level of PbDHAR mRNA in P. bungeana seedlings did not show significant change under high temperature stress. The recombinant PbDHAR was overexpressed in Escherichia coil following purification with affinity chromatography. The recombinant PbDHAR exhibited enzymatic activity （19.84 i.mnol/min per mg） and high affinity （a Krn of 0.08 mM） towards the substrates dehydroascorbate （DHA）. Moreover, the recombinant PbDHAR was a thermostable enzyme, and retained 77% of its initial activity at 55℃. The present study is the first to provide a detailed molecular characterization of the DHAR in P. bungeana.</description><subject>Amino Acid Sequence</subject><subject>Arabidopsis</subject><subject>Base Sequence</subject><subject>cloning</subject><subject>Cloning, Molecular</subject><subject>dehydroascorbate reductase</subject><subject>Dehydroascorbic Acid - metabolism</subject><subject>DNA, Complementary - genetics</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>enzyme activity</subject><subject>Enzyme Stability</subject><subject>Escherichia coli</subject><subject>Gene Expression Profiling</subject><subject>Gene Expression Regulation, Plant</subject><subject>Genes, Plant - genetics</subject><subject>Glutathione - metabolism</subject><subject>glutathione dehydrogenase (ascorbate)</subject><subject>gymnosperm</subject><subject>Kinetics</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>mRNA表达水平</subject><subject>Oxidoreductases - chemistry</subject><subject>Oxidoreductases - genetics</subject><subject>Oxidoreductases - metabolism</subject><subject>Pinus</subject><subject>Pinus - enzymology</subject><subject>Pinus - genetics</subject><subject>Protein Structure, Secondary</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>Sequence Alignment</subject><subject>Sequence Analysis, DNA</subject><subject>Structural Homology, Protein</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><subject>分子特征</subject><subject>白皮松</subject><subject>聚合酶链反应</subject><subject>脱氢抗坏血酸还原酶</subject><subject>谷胱甘肽</subject><subject>高等植物</subject><issn>1672-9072</issn><issn>1744-7909</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkV1v0zAUhiMEYh_wFyBCYlyl-COJ7QsuoMA2VsoETFwenbh2my6NNzvR2v16HFKNO4Qv7CP5ec_XmyQpJRMaz9v1hIo8z4QiasJIvAiRuZxsHyWHDx-PY1wKliki2EFyFMKaEC5JyZ4mB1Qpwhmjh8n8q2uM7hv06XSFHnVnfH2PXe3a1NkU049mtVt4h0E7X2Fn0u9m0esOg0mtd5v0sm77kFZ9uzTY4rPkicUmmOf79zi5-vzp5_Qsm307PZ--n2W6iI1myCtqpdWsyhWzqDXlhqtCciMFN0rrUhOJxBbMFHlVVLLQXHCBnAqkuSH8OHk95r3D1mK7hLXrfRsrwv3dthpWQikhLHJvRu7Gu9vehA42ddCmabA1rg8gOJdK5eWQ8eSfJKMsLyXhEZQjqL0LwRsLN77eoN8BJTC4A2sYTIDBBBhagT_uwDZKX-xr9NXGLP4K93ZE4N1-rLoxu_9ODF_OLz_EKOqzUV-Hzmwf9OivoYz7K-DX_BQu1IzkF_MZnEX-5chbdIBLXwe4-sEI5YSWqiyFiMSr_bQr1y5v67jqCvW1jf0BZ1QJGXfyGx7lwL8</recordid><startdate>200911</startdate><enddate>200911</enddate><creator>Yang, Hai-Ling</creator><creator>Zhao, Ying-Ru</creator><creator>Wang, Cai-Ling</creator><creator>Yang, Zhi-Ling</creator><creator>Zeng, Qing-Yin</creator><creator>Lu, Hai</creator><general>Melbourne, Australia : Blackwell Publishing Asia</general><general>Blackwell Publishing Asia</general><general>College of life Sciences and Biotechnology,Beijing Forestry University,Beijing 100083,China%State Key Laboratory of Systematic and Evolutionary Botany,Institute of Botany,the Chinese Academy of Sciences,Beijing 100093,China</general><scope>2RA</scope><scope>92L</scope><scope>CQIGP</scope><scope>W94</scope><scope>WU4</scope><scope>~WA</scope><scope>FBQ</scope><scope>BSCLL</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>7QL</scope><scope>C1K</scope><scope>7X8</scope><scope>2B.</scope><scope>4A8</scope><scope>92I</scope><scope>93N</scope><scope>PSX</scope><scope>TCJ</scope></search><sort><creationdate>200911</creationdate><title>Molecular Characterization of a Dehydroascorbate Reductase from Pinus bungeana</title><author>Yang, Hai-Ling ; Zhao, Ying-Ru ; Wang, Cai-Ling ; Yang, Zhi-Ling ; Zeng, Qing-Yin ; Lu, Hai</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5848-a3b1f8fc2b492facc13e39583e873e9cc6c08a0f52e54b5b85c3737a317a14e03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Sequence</topic><topic>Arabidopsis</topic><topic>Base Sequence</topic><topic>cloning</topic><topic>Cloning, Molecular</topic><topic>dehydroascorbate reductase</topic><topic>Dehydroascorbic Acid - metabolism</topic><topic>DNA, Complementary - genetics</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>enzyme activity</topic><topic>Enzyme Stability</topic><topic>Escherichia coli</topic><topic>Gene Expression Profiling</topic><topic>Gene Expression Regulation, Plant</topic><topic>Genes, Plant - genetics</topic><topic>Glutathione - metabolism</topic><topic>glutathione dehydrogenase (ascorbate)</topic><topic>gymnosperm</topic><topic>Kinetics</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>mRNA表达水平</topic><topic>Oxidoreductases - chemistry</topic><topic>Oxidoreductases - genetics</topic><topic>Oxidoreductases - metabolism</topic><topic>Pinus</topic><topic>Pinus - enzymology</topic><topic>Pinus - genetics</topic><topic>Protein Structure, Secondary</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>Sequence Alignment</topic><topic>Sequence Analysis, DNA</topic><topic>Structural Homology, Protein</topic><topic>Substrate Specificity</topic><topic>Temperature</topic><topic>分子特征</topic><topic>白皮松</topic><topic>聚合酶链反应</topic><topic>脱氢抗坏血酸还原酶</topic><topic>谷胱甘肽</topic><topic>高等植物</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Hai-Ling</creatorcontrib><creatorcontrib>Zhao, Ying-Ru</creatorcontrib><creatorcontrib>Wang, Cai-Ling</creatorcontrib><creatorcontrib>Yang, Zhi-Ling</creatorcontrib><creatorcontrib>Zeng, Qing-Yin</creatorcontrib><creatorcontrib>Lu, Hai</creatorcontrib><collection>中文科技期刊数据库</collection><collection>中文科技期刊数据库-CALIS站点</collection><collection>中文科技期刊数据库-7.0平台</collection><collection>中文科技期刊数据库-自然科学</collection><collection>中文科技期刊数据库-自然科学-生物科学</collection><collection>中文科技期刊数据库- 镜像站点</collection><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><collection>Wanfang Data Journals - Hong Kong</collection><collection>WANFANG Data Centre</collection><collection>Wanfang Data Journals</collection><collection>万方数据期刊 - 香港版</collection><collection>China Online Journals (COJ)</collection><collection>China Online Journals (COJ)</collection><jtitle>Journal of integrative plant biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, Hai-Ling</au><au>Zhao, Ying-Ru</au><au>Wang, Cai-Ling</au><au>Yang, Zhi-Ling</au><au>Zeng, Qing-Yin</au><au>Lu, Hai</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Characterization of a Dehydroascorbate Reductase from Pinus bungeana</atitle><jtitle>Journal of integrative plant biology</jtitle><addtitle>Journal of Integrative Plant Biology</addtitle><date>2009-11</date><risdate>2009</risdate><volume>51</volume><issue>11</issue><spage>993</spage><epage>1001</epage><pages>993-1001</pages><issn>1672-9072</issn><eissn>1744-7909</eissn><abstract>Dehydroascorbate reductase （DHAR） plays a critical role in the ascorbate-glutathione recycling reaction for most higher plants. To date, studies on DHAR in higher plants have focused largely on Arabidopsis and agricultural plants, and there is virtually no information on the molecular characteristics of DHAR in gymnosperms. The present study reports the cloning and characteristics of a DHAR （PbDHAR） from a pine, Pinus bungeana Zucc. ex Endl. The PbDHAR gene encodes a protein of 215 amino acid residues with a calculated molecular mass of 24.26 kDa. The predicted 3-D structure of PbDHAR showed a typical glutathione S-transferase fold. Reverse transcripUon-polymerase chain reaction revealed that the PbDHAR was a constitutive expression gene in P. bungeana. The expression level of PbDHAR mRNA in P. bungeana seedlings did not show significant change under high temperature stress. The recombinant PbDHAR was overexpressed in Escherichia coil following purification with affinity chromatography. The recombinant PbDHAR exhibited enzymatic activity （19.84 i.mnol/min per mg） and high affinity （a Krn of 0.08 mM） towards the substrates dehydroascorbate （DHA）. Moreover, the recombinant PbDHAR was a thermostable enzyme, and retained 77% of its initial activity at 55℃. The present study is the first to provide a detailed molecular characterization of the DHAR in P. bungeana.</abstract><cop>Melbourne, Australia</cop><pub>Melbourne, Australia : Blackwell Publishing Asia</pub><pmid>19903221</pmid><doi>10.1111/j.1744-7909.2009.00848.x</doi><tpages>9</tpages></addata></record> |
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| ispartof | Journal of integrative plant biology, 2009-11, Vol.51 (11), p.993-1001 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Arabidopsis Base Sequence cloning Cloning, Molecular dehydroascorbate reductase Dehydroascorbic Acid - metabolism DNA, Complementary - genetics Electrophoresis, Polyacrylamide Gel enzyme activity Enzyme Stability Escherichia coli Gene Expression Profiling Gene Expression Regulation, Plant Genes, Plant - genetics Glutathione - metabolism glutathione dehydrogenase (ascorbate) gymnosperm Kinetics Models, Molecular Molecular Sequence Data mRNA表达水平 Oxidoreductases - chemistry Oxidoreductases - genetics Oxidoreductases - metabolism Pinus Pinus - enzymology Pinus - genetics Protein Structure, Secondary Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism RNA, Messenger - genetics RNA, Messenger - metabolism Sequence Alignment Sequence Analysis, DNA Structural Homology, Protein Substrate Specificity Temperature 分子特征 白皮松 聚合酶链反应 脱氢抗坏血酸还原酶 谷胱甘肽 高等植物 |
| title | Molecular Characterization of a Dehydroascorbate Reductase from Pinus bungeana |
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