PoplarV1, Main, Exploration, bibRecord, 001245

PrLPAAT4, a Putative Lysophosphatidic Acid Acyltransferase from Paeonia rockii, Plays an Important Role in Seed Fatty Acid Biosynthesis.

Identifieur interne : 001245 ( Main/Exploration ); précédent : 001244; suivant : 001246

PrLPAAT4, a Putative Lysophosphatidic Acid Acyltransferase from Paeonia rockii, Plays an Important Role in Seed Fatty Acid Biosynthesis.

Auteurs : Qingyu Zhang [République populaire de Chine] ; Rui Yu [République populaire de Chine] ; Daoyang Sun [République populaire de Chine] ; Zhangzhen Bai [République populaire de Chine] ; Hong Li [République populaire de Chine] ; Liang Xue [République populaire de Chine] ; Yanlong Zhang [République populaire de Chine] ; Lixin Niu [République populaire de Chine]

Source :

Molecules (Basel, Switzerland) [ 1420-3049 ] ; 2017.

RBID : pubmed:28994730

Descripteurs français

KwdFr :
- Acide oléique (biosynthèse), Acides gras (biosynthèse), Acylation (MeSH), Acyltransferases (génétique), Acyltransferases (métabolisme), Arabidopsis (métabolisme), Biologie informatique (MeSH), Cadres ouverts de lecture (MeSH), Expression des gènes (MeSH), Graines (métabolisme), Lysophospholipides (métabolisme), Paeonia (enzymologie), Régulation de l'expression des gènes végétaux (MeSH).
MESH :
- biosynthèse : Acide oléique, Acides gras.
- enzymologie : Paeonia.
- génétique : Acyltransferases.
- métabolisme : Acyltransferases, Arabidopsis, Graines, Lysophospholipides.
- Acylation, Biologie informatique, Cadres ouverts de lecture, Expression des gènes, Régulation de l'expression des gènes végétaux.

English descriptors

KwdEn :
- Acylation (MeSH), Acyltransferases (genetics), Acyltransferases (metabolism), Arabidopsis (metabolism), Computational Biology (MeSH), Fatty Acids (biosynthesis), Gene Expression (MeSH), Gene Expression Regulation, Plant (MeSH), Lysophospholipids (metabolism), Oleic Acid (biosynthesis), Open Reading Frames (MeSH), Paeonia (enzymology), Seeds (metabolism).
MESH :
- chemical , biosynthesis : Fatty Acids, Oleic Acid.
- chemical , genetics : Acyltransferases.
- chemical , metabolism : Acyltransferases, Lysophospholipids.
- enzymology : Paeonia.
- metabolism : Arabidopsis, Seeds.
- Acylation, Computational Biology, Gene Expression, Gene Expression Regulation, Plant, Open Reading Frames.

Abstract

Lysophosphatidic acid acyltransferases (LPAATs) are essential for the acylation of lysophosphatidic acid (LPA) and the synthesis of phosphatidic acid (PA), a key intermediate in the synthesis of membrane phospholipids and storage lipids. Here, a putative lysophosphatidic acid acyltransferase gene, designated PrLPAAT4, was isolated from seed unsaturated fatty acid (UFA)-rich P. rockii. The complete PrLPAAT4 cDNA contained a 1116-bp open reading frame (ORF), encoding a 42.9 kDa protein with 371 amino acid residues. Bioinformatic analysis indicates that PrLPAAT4 is a plasma membrane protein belonging to acyl-CoA:1-acylglycerol-sn-3-phosphate acyltranferases (AGPAT) family. PrLPAAT4 shared high sequence similarity with its homologs from Citrus clementina, Populus trichocarpa, Manihot esculenta, and Ricinus communis. In Arabidopsis, overexpression of PrLPAAT4 resulted in a significant increase in the content of oleic acid (OA) and total fatty acids (FAs) in seeds. AtDGAT1, AtGPAT9, and AtOleosin, involved in TAG assembly, were upregulated in PrLPAAT4-overexpressing lines. These results indicated that PrLPAAT4 functions may be as a positive regulator in seed FA biosynthesis.

DOI: 10.3390/molecules22101694
PubMed: 28994730
PubMed Central: PMC6151692

Affiliations:

République populaire de Chine

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 001131
to stream Main, to step Curation: 001131

Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en">PrLPAAT4, a Putative Lysophosphatidic Acid Acyltransferase from Paeonia rockii, Plays an Important Role in Seed Fatty Acid Biosynthesis.</title>
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<author><name sortKey="Bai, Zhangzhen" sort="Bai, Zhangzhen" uniqKey="Bai Z" first="Zhangzhen" last="Bai">Zhangzhen Bai</name>
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<series><title level="j">Molecules (Basel, Switzerland)</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acylation (MeSH)</term>
<term>Acyltransferases (genetics)</term>
<term>Acyltransferases (metabolism)</term>
<term>Arabidopsis (metabolism)</term>
<term>Computational Biology (MeSH)</term>
<term>Fatty Acids (biosynthesis)</term>
<term>Gene Expression (MeSH)</term>
<term>Gene Expression Regulation, Plant (MeSH)</term>
<term>Lysophospholipids (metabolism)</term>
<term>Oleic Acid (biosynthesis)</term>
<term>Open Reading Frames (MeSH)</term>
<term>Paeonia (enzymology)</term>
<term>Seeds (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Acide oléique (biosynthèse)</term>
<term>Acides gras (biosynthèse)</term>
<term>Acylation (MeSH)</term>
<term>Acyltransferases (génétique)</term>
<term>Acyltransferases (métabolisme)</term>
<term>Arabidopsis (métabolisme)</term>
<term>Biologie informatique (MeSH)</term>
<term>Cadres ouverts de lecture (MeSH)</term>
<term>Expression des gènes (MeSH)</term>
<term>Graines (métabolisme)</term>
<term>Lysophospholipides (métabolisme)</term>
<term>Paeonia (enzymologie)</term>
<term>Régulation de l'expression des gènes végétaux (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Fatty Acids</term>
<term>Oleic Acid</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Acyltransferases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acyltransferases</term>
<term>Lysophospholipids</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Acide oléique</term>
<term>Acides gras</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Paeonia</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Paeonia</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Acyltransferases</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arabidopsis</term>
<term>Seeds</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acyltransferases</term>
<term>Arabidopsis</term>
<term>Graines</term>
<term>Lysophospholipides</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Acylation</term>
<term>Computational Biology</term>
<term>Gene Expression</term>
<term>Gene Expression Regulation, Plant</term>
<term>Open Reading Frames</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Acylation</term>
<term>Biologie informatique</term>
<term>Cadres ouverts de lecture</term>
<term>Expression des gènes</term>
<term>Régulation de l'expression des gènes végétaux</term>
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<front><div type="abstract" xml:lang="en">Lysophosphatidic acid acyltransferases (LPAATs) are essential for the acylation of lysophosphatidic acid (LPA) and the synthesis of phosphatidic acid (PA), a key intermediate in the synthesis of membrane phospholipids and storage lipids. Here, a putative lysophosphatidic acid acyltransferase gene, designated <i>PrLPAAT4</i>
, was isolated from seed unsaturated fatty acid (UFA)-rich <i>P. rockii</i>
. The complete <i>PrLPAAT4</i>
 cDNA contained a 1116-bp open reading frame (ORF), encoding a 42.9 kDa protein with 371 amino acid residues. Bioinformatic analysis indicates that PrLPAAT4 is a plasma membrane protein belonging to acyl-CoA:1-acylglycerol-sn-3-phosphate acyltranferases (AGPAT) family. PrLPAAT4 shared high sequence similarity with its homologs from <i>Citrus clementina</i>
, <i>Populus trichocarpa</i>
, <i>Manihot esculenta</i>
, and <i>Ricinus communis</i>
. In Arabidopsis, overexpression of <i>PrLPAAT4</i>
 resulted in a significant increase in the content of oleic acid (OA) and total fatty acids (FAs) in seeds. <i>AtDGAT1</i>
, <i>AtGPAT9</i>
, and <i>AtOleosin</i>
, involved in TAG assembly, were upregulated in <i>PrLPAAT4</i>
-overexpressing lines. These results indicated that PrLPAAT4 functions may be as a positive regulator in seed FA biosynthesis.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28994730</PMID>
<DateCompleted><Year>2019</Year>
<Month>03</Month>
<Day>07</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>03</Month>
<Day>07</Day>
</DateRevised>
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<JournalIssue CitedMedium="Internet"><Volume>22</Volume>
<Issue>10</Issue>
<PubDate><Year>2017</Year>
<Month>Oct</Month>
<Day>10</Day>
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<Title>Molecules (Basel, Switzerland)</Title>
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<ArticleTitle>PrLPAAT4, a Putative Lysophosphatidic Acid Acyltransferase from Paeonia rockii, Plays an Important Role in Seed Fatty Acid Biosynthesis.</ArticleTitle>
<ELocationID EIdType="pii" ValidYN="Y">E1694</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.3390/molecules22101694</ELocationID>
<Abstract><AbstractText>Lysophosphatidic acid acyltransferases (LPAATs) are essential for the acylation of lysophosphatidic acid (LPA) and the synthesis of phosphatidic acid (PA), a key intermediate in the synthesis of membrane phospholipids and storage lipids. Here, a putative lysophosphatidic acid acyltransferase gene, designated <i>PrLPAAT4</i>
, was isolated from seed unsaturated fatty acid (UFA)-rich <i>P. rockii</i>
. The complete <i>PrLPAAT4</i>
 cDNA contained a 1116-bp open reading frame (ORF), encoding a 42.9 kDa protein with 371 amino acid residues. Bioinformatic analysis indicates that PrLPAAT4 is a plasma membrane protein belonging to acyl-CoA:1-acylglycerol-sn-3-phosphate acyltranferases (AGPAT) family. PrLPAAT4 shared high sequence similarity with its homologs from <i>Citrus clementina</i>
, <i>Populus trichocarpa</i>
, <i>Manihot esculenta</i>
, and <i>Ricinus communis</i>
. In Arabidopsis, overexpression of <i>PrLPAAT4</i>
 resulted in a significant increase in the content of oleic acid (OA) and total fatty acids (FAs) in seeds. <i>AtDGAT1</i>
, <i>AtGPAT9</i>
, and <i>AtOleosin</i>
, involved in TAG assembly, were upregulated in <i>PrLPAAT4</i>
-overexpressing lines. These results indicated that PrLPAAT4 functions may be as a positive regulator in seed FA biosynthesis.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Qingyu</ForeName>
<Initials>Q</Initials>
<AffiliationInfo><Affiliation>College of Landscape Architecture and Arts, Northwest A&F University, Yangling, Shaanxi 712100, China. zhangqingyu@nwsuaf.edu.cn.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Yu</LastName>
<ForeName>Rui</ForeName>
<Initials>R</Initials>
<Identifier Source="ORCID">0000-0002-2519-4548</Identifier>
<AffiliationInfo><Affiliation>College of Landscape Architecture and Arts, Northwest A&F University, Yangling, Shaanxi 712100, China. yurui@nwsuaf.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sun</LastName>
<ForeName>Daoyang</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>College of Landscape Architecture and Arts, Northwest A&F University, Yangling, Shaanxi 712100, China. sundaoyang2009@163.com.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Bai</LastName>
<ForeName>Zhangzhen</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>College of Landscape Architecture and Arts, Northwest A&F University, Yangling, Shaanxi 712100, China. baizhangzhen@nwsuaf.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Hong</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China. hong.li@sibcb.ac.cn.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xue</LastName>
<ForeName>Liang</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China. xueliang@sibcb.ac.cn.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Yanlong</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>College of Landscape Architecture and Arts, Northwest A&F University, Yangling, Shaanxi 712100, China. zhangyanlong@nwsuaf.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Niu</LastName>
<ForeName>Lixin</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>College of Landscape Architecture and Arts, Northwest A&F University, Yangling, Shaanxi 712100, China. niulixin@nwsuaf.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
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<Language>eng</Language>
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</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2017</Year>
<Month>10</Month>
<Day>10</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>Switzerland</Country>
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PrLPAAT4, a Putative Lysophosphatidic Acid Acyltransferase from Paeonia rockii, Plays an Important Role in Seed Fatty Acid Biosynthesis.

PrLPAAT4, a Putative Lysophosphatidic Acid Acyltransferase from Paeonia rockii, Plays an Important Role in Seed Fatty Acid Biosynthesis.

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