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Identification of an Arabidopsis cDNA encoding a lipoyltransferase located in plastids
In plant cells, the pyruvate dehydrogenase (PDH) complex that requires lipoic acid as an essential coenzyme is located in plastids and mitochondria. The enzyme complex has to be lipoylated in both organelles. However, the lipoyltransferase located in plastids has not been reported. In this study, an...
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| Published in: | FEBS letters 2001-10, Vol.506 (3), p.286-290 |
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| Language: | English |
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| cites | cdi_FETCH-LOGICAL-c5235-d3581d7b4dd8a7c1b7b38069485fb88bca648c71b883bf0f5053be11df58067e3 |
| container_end_page | 290 |
| container_issue | 3 |
| container_start_page | 286 |
| container_title | FEBS letters |
| container_volume | 506 |
| creator | Wada, Miho Yasuno, Rie Wada, Hajime |
| description | In plant cells, the pyruvate dehydrogenase (PDH) complex that requires lipoic acid as an essential coenzyme is located in plastids and mitochondria. The enzyme complex has to be lipoylated in both organelles. However, the lipoyltransferase located in plastids has not been reported. In this study, an
Arabidopsis thaliana LIP2p cDNA for a lipoyltransferase located in plastids has been identified. We have shown that this cDNA encodes a lipoyltransferase by demonstrating its ability to complement an
Escherichia coli mutant lacking lipoyltransferase activity, and that LIP2p is targeted into chloroplasts. These findings suggest that LIP2p is located in plastids and responsible for lipoylation of the plastidial PDH complex. |
| doi_str_mv | 10.1016/S0014-5793(01)02932-5 |
| format | article |
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Arabidopsis thaliana LIP2p cDNA for a lipoyltransferase located in plastids has been identified. We have shown that this cDNA encodes a lipoyltransferase by demonstrating its ability to complement an
Escherichia coli mutant lacking lipoyltransferase activity, and that LIP2p is targeted into chloroplasts. These findings suggest that LIP2p is located in plastids and responsible for lipoylation of the plastidial PDH complex.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(01)02932-5</identifier><identifier>PMID: 11602263</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>ACP, acyl carrier protein ; Acyltransferases - chemistry ; Acyltransferases - genetics ; Acyltransferases - metabolism ; Amino Acid Sequence ; Arabidopsis - enzymology ; Arabidopsis - genetics ; Arabidopsis thaliana ; Cloning, Molecular ; DNA, Complementary ; Genetic Complementation Test ; GFP, green fluorescent protein ; Lipoic acid ; Lipoylation ; Lipoyltransferase ; Molecular Sequence Data ; OGDH, 2-oxoglutarate dehydrogenase ; ORF, open reading frame ; PCR, polymerase chain reaction ; PDH, pyruvate dehydrogenase ; Plastid ; Plastids - enzymology ; Pyruvate dehydrogenase ; RT-PCR, reverse transcription-PCR ; Sequence Homology, Amino Acid</subject><ispartof>FEBS letters, 2001-10, Vol.506 (3), p.286-290</ispartof><rights>2001 Federation of European Biochemical Societies</rights><rights>FEBS Letters 506 (2001) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5235-d3581d7b4dd8a7c1b7b38069485fb88bca648c71b883bf0f5053be11df58067e3</citedby><cites>FETCH-LOGICAL-c5235-d3581d7b4dd8a7c1b7b38069485fb88bca648c71b883bf0f5053be11df58067e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579301029325$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45779</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11602263$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wada, Miho</creatorcontrib><creatorcontrib>Yasuno, Rie</creatorcontrib><creatorcontrib>Wada, Hajime</creatorcontrib><title>Identification of an Arabidopsis cDNA encoding a lipoyltransferase located in plastids</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>In plant cells, the pyruvate dehydrogenase (PDH) complex that requires lipoic acid as an essential coenzyme is located in plastids and mitochondria. The enzyme complex has to be lipoylated in both organelles. However, the lipoyltransferase located in plastids has not been reported. In this study, an
Arabidopsis thaliana LIP2p cDNA for a lipoyltransferase located in plastids has been identified. We have shown that this cDNA encodes a lipoyltransferase by demonstrating its ability to complement an
Escherichia coli mutant lacking lipoyltransferase activity, and that LIP2p is targeted into chloroplasts. These findings suggest that LIP2p is located in plastids and responsible for lipoylation of the plastidial PDH complex.</description><subject>ACP, acyl carrier protein</subject><subject>Acyltransferases - chemistry</subject><subject>Acyltransferases - genetics</subject><subject>Acyltransferases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Arabidopsis - enzymology</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis thaliana</subject><subject>Cloning, Molecular</subject><subject>DNA, Complementary</subject><subject>Genetic Complementation Test</subject><subject>GFP, green fluorescent protein</subject><subject>Lipoic acid</subject><subject>Lipoylation</subject><subject>Lipoyltransferase</subject><subject>Molecular Sequence Data</subject><subject>OGDH, 2-oxoglutarate dehydrogenase</subject><subject>ORF, open reading frame</subject><subject>PCR, polymerase chain reaction</subject><subject>PDH, pyruvate dehydrogenase</subject><subject>Plastid</subject><subject>Plastids - enzymology</subject><subject>Pyruvate dehydrogenase</subject><subject>RT-PCR, reverse transcription-PCR</subject><subject>Sequence Homology, Amino Acid</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><recordid>eNqNkUtv1DAURi0EaofSn0DlFYJFwDeOY8-qmpaWVqrKgsfW8uMaucrEqZ0Bzb9vMjOCZVn5cc_9rnVMyFtgH4FB--kbY9BUQi75ewYfWL3kdSVekAUoySvetOolWfxFjsnrUh7YdFawPCLHAC2r65YvyM9bj_0YQ3RmjKmnKVDT01U2Nvo0lFio-3y_oti75GP_ixraxSFtuzGbvgTMpiDt0tSMnsaeDp0pY_TlDXkVTFfw9LCekB_XV98vb6q7r19uL1d3lRM1F5XnQoGXtvFeGenASssVa5eNEsEqZZ1pG-UkTHtuAwuCCW4RwAcxYRL5CXm3zx1yetxgGfU6FoddZ3pMm6JlXTMhQT4LgmqVaFoxgWIPupxKyRj0kOPa5K0Gpmfzemdez1o1A70zr-e-s8OAjV2j_9d1UD0BN3vgT-xw-3-p-vrqot5V5gKD3fU863wfhZPa3xGzLi5OX4Q-ZnSj9ik-89onaKamaw</recordid><startdate>20011012</startdate><enddate>20011012</enddate><creator>Wada, Miho</creator><creator>Yasuno, Rie</creator><creator>Wada, Hajime</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>20011012</creationdate><title>Identification of an Arabidopsis cDNA encoding a lipoyltransferase located in plastids</title><author>Wada, Miho ; Yasuno, Rie ; Wada, Hajime</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5235-d3581d7b4dd8a7c1b7b38069485fb88bca648c71b883bf0f5053be11df58067e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>ACP, acyl carrier protein</topic><topic>Acyltransferases - chemistry</topic><topic>Acyltransferases - genetics</topic><topic>Acyltransferases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Arabidopsis - enzymology</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis thaliana</topic><topic>Cloning, Molecular</topic><topic>DNA, Complementary</topic><topic>Genetic Complementation Test</topic><topic>GFP, green fluorescent protein</topic><topic>Lipoic acid</topic><topic>Lipoylation</topic><topic>Lipoyltransferase</topic><topic>Molecular Sequence Data</topic><topic>OGDH, 2-oxoglutarate dehydrogenase</topic><topic>ORF, open reading frame</topic><topic>PCR, polymerase chain reaction</topic><topic>PDH, pyruvate dehydrogenase</topic><topic>Plastid</topic><topic>Plastids - enzymology</topic><topic>Pyruvate dehydrogenase</topic><topic>RT-PCR, reverse transcription-PCR</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wada, Miho</creatorcontrib><creatorcontrib>Yasuno, Rie</creatorcontrib><creatorcontrib>Wada, Hajime</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wada, Miho</au><au>Yasuno, Rie</au><au>Wada, Hajime</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Identification of an Arabidopsis cDNA encoding a lipoyltransferase located in plastids</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2001-10-12</date><risdate>2001</risdate><volume>506</volume><issue>3</issue><spage>286</spage><epage>290</epage><pages>286-290</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>In plant cells, the pyruvate dehydrogenase (PDH) complex that requires lipoic acid as an essential coenzyme is located in plastids and mitochondria. The enzyme complex has to be lipoylated in both organelles. However, the lipoyltransferase located in plastids has not been reported. In this study, an
Arabidopsis thaliana LIP2p cDNA for a lipoyltransferase located in plastids has been identified. We have shown that this cDNA encodes a lipoyltransferase by demonstrating its ability to complement an
Escherichia coli mutant lacking lipoyltransferase activity, and that LIP2p is targeted into chloroplasts. These findings suggest that LIP2p is located in plastids and responsible for lipoylation of the plastidial PDH complex.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>11602263</pmid><doi>10.1016/S0014-5793(01)02932-5</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 2001-10, Vol.506 (3), p.286-290 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_72205717 |
| source | Wiley; ScienceDirect Journals |
| subjects | ACP, acyl carrier protein Acyltransferases - chemistry Acyltransferases - genetics Acyltransferases - metabolism Amino Acid Sequence Arabidopsis - enzymology Arabidopsis - genetics Arabidopsis thaliana Cloning, Molecular DNA, Complementary Genetic Complementation Test GFP, green fluorescent protein Lipoic acid Lipoylation Lipoyltransferase Molecular Sequence Data OGDH, 2-oxoglutarate dehydrogenase ORF, open reading frame PCR, polymerase chain reaction PDH, pyruvate dehydrogenase Plastid Plastids - enzymology Pyruvate dehydrogenase RT-PCR, reverse transcription-PCR Sequence Homology, Amino Acid |
| title | Identification of an Arabidopsis cDNA encoding a lipoyltransferase located in plastids |
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