Molecular characterization of a 2-Cys peroxiredoxin induced by abiotic stress in mungbean
A mungbean low temperature-inducible VrPrx1 encoding 2-Cys peroxiredoxin (2-Cys Prx) was cloned by subtractive suppression hybridization. The deduced VrPrx1 amino acid sequence showed highest sequence homology to 2-Cys Prxs of Phaseolus vulgaris (95%), Pisum sativum (89%), and Arabidopsis thaliana (...
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| Veröffentlicht in: | Plant cell, tissue and organ culture tissue and organ culture, 2012-03, Vol.108 (3), p.473-484 |
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| container_title | Plant cell, tissue and organ culture |
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| creator | Cho, Chang-Woo Chung, Eunsook Heo, Jee-Eun So, Hyun-Ah Choi, Hong-Kyu Kim, Doh Hoon Chung, Young Soo Chae, Ho Zoon Lee, Jai-Heon |
| description | A mungbean low temperature-inducible
VrPrx1
encoding 2-Cys peroxiredoxin (2-Cys Prx) was cloned by subtractive suppression hybridization. The deduced
VrPrx1
amino acid sequence showed highest sequence homology to 2-Cys Prxs of
Phaseolus vulgaris
(95%),
Pisum sativum
(89%), and
Arabidopsis thaliana
(87%).
VrPrx1
RNA and protein levels were increased by low temperature, hydrogen peroxide (H
2
O
2
), and wounding but decreased by high salinity, drought, and exogenous abscisic acid. Recombinant His-tagged VrPrx1 recombinant protein protected DNA and glutamine synthetase activity from degradation via the thiol/Fe(III) oxygen mixed-function oxidation system, and exhibited peroxidase activity to H
2
O
2
in the presence of the reducing agent dithiothreitol (DTT) in vitro. The oxidized dimers and oligomers of the VrPrx1 recombinant protein were reduced to monomers by DTT or thioredoxin. Subcellular localization studies confirmed that VrPrx1-GFP was targeted to the plastid. To evaluate the function of
VrPrx1
in planta
, the antioxidant activities and photosynthetic efficiency were investigated in
VrPrx1
-overexpressing
Arabidopsis
plants.
VrPrx1
ectopic expression conferred improved photosynthetic efficiency under oxidative stress conditions. Hence, mungbean
VrPrx1
may play an important role in protecting the photosynthetic apparatus against oxidative and abiotic stress conditions. |
| doi_str_mv | 10.1007/s11240-011-0061-1 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_journals_2259386173</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2259386173</sourcerecordid><originalsourceid>FETCH-LOGICAL-c316t-1468b9c45010e35e7660572d37cdebf7edf579581a2f4d6e7c9f44814a2ce63a3</originalsourceid><addsrcrecordid>eNp1kD1PwzAQhi0EEqXwA9gsMRt8_kxGVPElFbHAwGQ5zqWkapNiJxLl1-MqSEwsd8M973vSQ8gl8Gvg3N4kAKE44wCMcwMMjsgMtJVMc6WOyYyDscwU2p6Ss5TWPENSwYy8P_cbDOPGRxo-fPRhwNh--6HtO9o31FPBFvtEdxj7rzZinWdH264eA9a02lNftf3QBpqGiCnlC92O3apC352Tk8ZvEl787jl5u797XTyy5cvD0-J2yYIEMzBQpqjKoDQHjlKjNYZrK2ppQ41VY7FutC11AV40qjZoQ9koVYDyIqCRXs7J1dS7i_3niGlw636MXX7phNClLAxYmSmYqBD7lCI2bhfbrY97B9wdDLrJoMsG3cGgg5wRUyZltlth_Gv-P_QDbz1zVg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2259386173</pqid></control><display><type>article</type><title>Molecular characterization of a 2-Cys peroxiredoxin induced by abiotic stress in mungbean</title><source>SpringerLink Journals</source><creator>Cho, Chang-Woo ; Chung, Eunsook ; Heo, Jee-Eun ; So, Hyun-Ah ; Choi, Hong-Kyu ; Kim, Doh Hoon ; Chung, Young Soo ; Chae, Ho Zoon ; Lee, Jai-Heon</creator><creatorcontrib>Cho, Chang-Woo ; Chung, Eunsook ; Heo, Jee-Eun ; So, Hyun-Ah ; Choi, Hong-Kyu ; Kim, Doh Hoon ; Chung, Young Soo ; Chae, Ho Zoon ; Lee, Jai-Heon</creatorcontrib><description>A mungbean low temperature-inducible
VrPrx1
encoding 2-Cys peroxiredoxin (2-Cys Prx) was cloned by subtractive suppression hybridization. The deduced
VrPrx1
amino acid sequence showed highest sequence homology to 2-Cys Prxs of
Phaseolus vulgaris
(95%),
Pisum sativum
(89%), and
Arabidopsis thaliana
(87%).
VrPrx1
RNA and protein levels were increased by low temperature, hydrogen peroxide (H
2
O
2
), and wounding but decreased by high salinity, drought, and exogenous abscisic acid. Recombinant His-tagged VrPrx1 recombinant protein protected DNA and glutamine synthetase activity from degradation via the thiol/Fe(III) oxygen mixed-function oxidation system, and exhibited peroxidase activity to H
2
O
2
in the presence of the reducing agent dithiothreitol (DTT) in vitro. The oxidized dimers and oligomers of the VrPrx1 recombinant protein were reduced to monomers by DTT or thioredoxin. Subcellular localization studies confirmed that VrPrx1-GFP was targeted to the plastid. To evaluate the function of
VrPrx1
in planta
, the antioxidant activities and photosynthetic efficiency were investigated in
VrPrx1
-overexpressing
Arabidopsis
plants.
VrPrx1
ectopic expression conferred improved photosynthetic efficiency under oxidative stress conditions. Hence, mungbean
VrPrx1
may play an important role in protecting the photosynthetic apparatus against oxidative and abiotic stress conditions.</description><identifier>ISSN: 0167-6857</identifier><identifier>EISSN: 1573-5044</identifier><identifier>DOI: 10.1007/s11240-011-0061-1</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Abiotic stress ; Abscisic acid ; Amino acid sequence ; Amino acids ; Antioxidants ; Beans ; Biomedical and Life Sciences ; Deoxyribonucleic acid ; Dimers ; Dithiothreitol ; DNA ; Drought ; Ectopic expression ; Glutamate-ammonia ligase ; Glutamine ; Homology ; Hybridization ; Hydrogen peroxide ; Iron ; Life Sciences ; Localization ; Low temperature ; Monomers ; Oligomers ; Original Paper ; Oxidation ; Oxidative stress ; Peroxidase ; Peroxiredoxin ; Photosynthesis ; Photosynthetic apparatus ; Plant Genetics and Genomics ; Plant Pathology ; Plant Physiology ; Plant Sciences ; Proteins ; Reducing agents ; Ribonucleic acid ; RNA ; Thioredoxin ; Wounding</subject><ispartof>Plant cell, tissue and organ culture, 2012-03, Vol.108 (3), p.473-484</ispartof><rights>Springer Science+Business Media B.V. 2011</rights><rights>Plant Cell, Tissue and Organ Culture (PCTOC) is a copyright of Springer, (2011). All Rights Reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c316t-1468b9c45010e35e7660572d37cdebf7edf579581a2f4d6e7c9f44814a2ce63a3</citedby><cites>FETCH-LOGICAL-c316t-1468b9c45010e35e7660572d37cdebf7edf579581a2f4d6e7c9f44814a2ce63a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s11240-011-0061-1$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s11240-011-0061-1$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids></links><search><creatorcontrib>Cho, Chang-Woo</creatorcontrib><creatorcontrib>Chung, Eunsook</creatorcontrib><creatorcontrib>Heo, Jee-Eun</creatorcontrib><creatorcontrib>So, Hyun-Ah</creatorcontrib><creatorcontrib>Choi, Hong-Kyu</creatorcontrib><creatorcontrib>Kim, Doh Hoon</creatorcontrib><creatorcontrib>Chung, Young Soo</creatorcontrib><creatorcontrib>Chae, Ho Zoon</creatorcontrib><creatorcontrib>Lee, Jai-Heon</creatorcontrib><title>Molecular characterization of a 2-Cys peroxiredoxin induced by abiotic stress in mungbean</title><title>Plant cell, tissue and organ culture</title><addtitle>Plant Cell Tiss Organ Cult</addtitle><description>A mungbean low temperature-inducible
VrPrx1
encoding 2-Cys peroxiredoxin (2-Cys Prx) was cloned by subtractive suppression hybridization. The deduced
VrPrx1
amino acid sequence showed highest sequence homology to 2-Cys Prxs of
Phaseolus vulgaris
(95%),
Pisum sativum
(89%), and
Arabidopsis thaliana
(87%).
VrPrx1
RNA and protein levels were increased by low temperature, hydrogen peroxide (H
2
O
2
), and wounding but decreased by high salinity, drought, and exogenous abscisic acid. Recombinant His-tagged VrPrx1 recombinant protein protected DNA and glutamine synthetase activity from degradation via the thiol/Fe(III) oxygen mixed-function oxidation system, and exhibited peroxidase activity to H
2
O
2
in the presence of the reducing agent dithiothreitol (DTT) in vitro. The oxidized dimers and oligomers of the VrPrx1 recombinant protein were reduced to monomers by DTT or thioredoxin. Subcellular localization studies confirmed that VrPrx1-GFP was targeted to the plastid. To evaluate the function of
VrPrx1
in planta
, the antioxidant activities and photosynthetic efficiency were investigated in
VrPrx1
-overexpressing
Arabidopsis
plants.
VrPrx1
ectopic expression conferred improved photosynthetic efficiency under oxidative stress conditions. Hence, mungbean
VrPrx1
may play an important role in protecting the photosynthetic apparatus against oxidative and abiotic stress conditions.</description><subject>Abiotic stress</subject><subject>Abscisic acid</subject><subject>Amino acid sequence</subject><subject>Amino acids</subject><subject>Antioxidants</subject><subject>Beans</subject><subject>Biomedical and Life Sciences</subject><subject>Deoxyribonucleic acid</subject><subject>Dimers</subject><subject>Dithiothreitol</subject><subject>DNA</subject><subject>Drought</subject><subject>Ectopic expression</subject><subject>Glutamate-ammonia ligase</subject><subject>Glutamine</subject><subject>Homology</subject><subject>Hybridization</subject><subject>Hydrogen peroxide</subject><subject>Iron</subject><subject>Life Sciences</subject><subject>Localization</subject><subject>Low temperature</subject><subject>Monomers</subject><subject>Oligomers</subject><subject>Original Paper</subject><subject>Oxidation</subject><subject>Oxidative stress</subject><subject>Peroxidase</subject><subject>Peroxiredoxin</subject><subject>Photosynthesis</subject><subject>Photosynthetic apparatus</subject><subject>Plant Genetics and Genomics</subject><subject>Plant Pathology</subject><subject>Plant Physiology</subject><subject>Plant Sciences</subject><subject>Proteins</subject><subject>Reducing agents</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>Thioredoxin</subject><subject>Wounding</subject><issn>0167-6857</issn><issn>1573-5044</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>BENPR</sourceid><recordid>eNp1kD1PwzAQhi0EEqXwA9gsMRt8_kxGVPElFbHAwGQ5zqWkapNiJxLl1-MqSEwsd8M973vSQ8gl8Gvg3N4kAKE44wCMcwMMjsgMtJVMc6WOyYyDscwU2p6Ss5TWPENSwYy8P_cbDOPGRxo-fPRhwNh--6HtO9o31FPBFvtEdxj7rzZinWdH264eA9a02lNftf3QBpqGiCnlC92O3apC352Tk8ZvEl787jl5u797XTyy5cvD0-J2yYIEMzBQpqjKoDQHjlKjNYZrK2ppQ41VY7FutC11AV40qjZoQ9koVYDyIqCRXs7J1dS7i_3niGlw636MXX7phNClLAxYmSmYqBD7lCI2bhfbrY97B9wdDLrJoMsG3cGgg5wRUyZltlth_Gv-P_QDbz1zVg</recordid><startdate>20120301</startdate><enddate>20120301</enddate><creator>Cho, Chang-Woo</creator><creator>Chung, Eunsook</creator><creator>Heo, Jee-Eun</creator><creator>So, Hyun-Ah</creator><creator>Choi, Hong-Kyu</creator><creator>Kim, Doh Hoon</creator><creator>Chung, Young Soo</creator><creator>Chae, Ho Zoon</creator><creator>Lee, Jai-Heon</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X2</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M0K</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope></search><sort><creationdate>20120301</creationdate><title>Molecular characterization of a 2-Cys peroxiredoxin induced by abiotic stress in mungbean</title><author>Cho, Chang-Woo ; Chung, Eunsook ; Heo, Jee-Eun ; So, Hyun-Ah ; Choi, Hong-Kyu ; Kim, Doh Hoon ; Chung, Young Soo ; Chae, Ho Zoon ; Lee, Jai-Heon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c316t-1468b9c45010e35e7660572d37cdebf7edf579581a2f4d6e7c9f44814a2ce63a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Abiotic stress</topic><topic>Abscisic acid</topic><topic>Amino acid sequence</topic><topic>Amino acids</topic><topic>Antioxidants</topic><topic>Beans</topic><topic>Biomedical and Life Sciences</topic><topic>Deoxyribonucleic acid</topic><topic>Dimers</topic><topic>Dithiothreitol</topic><topic>DNA</topic><topic>Drought</topic><topic>Ectopic expression</topic><topic>Glutamate-ammonia ligase</topic><topic>Glutamine</topic><topic>Homology</topic><topic>Hybridization</topic><topic>Hydrogen peroxide</topic><topic>Iron</topic><topic>Life Sciences</topic><topic>Localization</topic><topic>Low temperature</topic><topic>Monomers</topic><topic>Oligomers</topic><topic>Original Paper</topic><topic>Oxidation</topic><topic>Oxidative stress</topic><topic>Peroxidase</topic><topic>Peroxiredoxin</topic><topic>Photosynthesis</topic><topic>Photosynthetic apparatus</topic><topic>Plant Genetics and Genomics</topic><topic>Plant Pathology</topic><topic>Plant Physiology</topic><topic>Plant Sciences</topic><topic>Proteins</topic><topic>Reducing agents</topic><topic>Ribonucleic acid</topic><topic>RNA</topic><topic>Thioredoxin</topic><topic>Wounding</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cho, Chang-Woo</creatorcontrib><creatorcontrib>Chung, Eunsook</creatorcontrib><creatorcontrib>Heo, Jee-Eun</creatorcontrib><creatorcontrib>So, Hyun-Ah</creatorcontrib><creatorcontrib>Choi, Hong-Kyu</creatorcontrib><creatorcontrib>Kim, Doh Hoon</creatorcontrib><creatorcontrib>Chung, Young Soo</creatorcontrib><creatorcontrib>Chae, Ho Zoon</creatorcontrib><creatorcontrib>Lee, Jai-Heon</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Agricultural Science Collection</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><jtitle>Plant cell, tissue and organ culture</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cho, Chang-Woo</au><au>Chung, Eunsook</au><au>Heo, Jee-Eun</au><au>So, Hyun-Ah</au><au>Choi, Hong-Kyu</au><au>Kim, Doh Hoon</au><au>Chung, Young Soo</au><au>Chae, Ho Zoon</au><au>Lee, Jai-Heon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular characterization of a 2-Cys peroxiredoxin induced by abiotic stress in mungbean</atitle><jtitle>Plant cell, tissue and organ culture</jtitle><stitle>Plant Cell Tiss Organ Cult</stitle><date>2012-03-01</date><risdate>2012</risdate><volume>108</volume><issue>3</issue><spage>473</spage><epage>484</epage><pages>473-484</pages><issn>0167-6857</issn><eissn>1573-5044</eissn><abstract>A mungbean low temperature-inducible
VrPrx1
encoding 2-Cys peroxiredoxin (2-Cys Prx) was cloned by subtractive suppression hybridization. The deduced
VrPrx1
amino acid sequence showed highest sequence homology to 2-Cys Prxs of
Phaseolus vulgaris
(95%),
Pisum sativum
(89%), and
Arabidopsis thaliana
(87%).
VrPrx1
RNA and protein levels were increased by low temperature, hydrogen peroxide (H
2
O
2
), and wounding but decreased by high salinity, drought, and exogenous abscisic acid. Recombinant His-tagged VrPrx1 recombinant protein protected DNA and glutamine synthetase activity from degradation via the thiol/Fe(III) oxygen mixed-function oxidation system, and exhibited peroxidase activity to H
2
O
2
in the presence of the reducing agent dithiothreitol (DTT) in vitro. The oxidized dimers and oligomers of the VrPrx1 recombinant protein were reduced to monomers by DTT or thioredoxin. Subcellular localization studies confirmed that VrPrx1-GFP was targeted to the plastid. To evaluate the function of
VrPrx1
in planta
, the antioxidant activities and photosynthetic efficiency were investigated in
VrPrx1
-overexpressing
Arabidopsis
plants.
VrPrx1
ectopic expression conferred improved photosynthetic efficiency under oxidative stress conditions. Hence, mungbean
VrPrx1
may play an important role in protecting the photosynthetic apparatus against oxidative and abiotic stress conditions.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><doi>10.1007/s11240-011-0061-1</doi><tpages>12</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0167-6857 |
| ispartof | Plant cell, tissue and organ culture, 2012-03, Vol.108 (3), p.473-484 |
| issn | 0167-6857 1573-5044 |
| language | eng |
| recordid | cdi_proquest_journals_2259386173 |
| source | SpringerLink Journals |
| subjects | Abiotic stress Abscisic acid Amino acid sequence Amino acids Antioxidants Beans Biomedical and Life Sciences Deoxyribonucleic acid Dimers Dithiothreitol DNA Drought Ectopic expression Glutamate-ammonia ligase Glutamine Homology Hybridization Hydrogen peroxide Iron Life Sciences Localization Low temperature Monomers Oligomers Original Paper Oxidation Oxidative stress Peroxidase Peroxiredoxin Photosynthesis Photosynthetic apparatus Plant Genetics and Genomics Plant Pathology Plant Physiology Plant Sciences Proteins Reducing agents Ribonucleic acid RNA Thioredoxin Wounding |
| title | Molecular characterization of a 2-Cys peroxiredoxin induced by abiotic stress in mungbean |
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