[Functional divergence of betaine aldehyde dehydrogenase genes in Populus euphratica].
Identifieur interne : 002836 ( Main/Exploration ); précédent : 002835; suivant : 002837[Functional divergence of betaine aldehyde dehydrogenase genes in Populus euphratica].
Auteurs : Jiaqi Liu [République populaire de Chine] ; Xue Yang ; Li Di ; Hailing YangSource :
- Sheng wu gong cheng xue bao = Chinese journal of biotechnology [ 1000-3061 ] ; 2012.
Descripteurs français
- KwdFr :
- Betaine-aldehyde dehydrogenase (biosynthèse), Betaine-aldehyde dehydrogenase (génétique), Clonage moléculaire (MeSH), Données de séquences moléculaires (MeSH), Escherichia coli (génétique), Escherichia coli (métabolisme), Isoformes de protéines (composition chimique), Isoformes de protéines (métabolisme), Populus (génétique), Protéines recombinantes (biosynthèse), Protéines recombinantes (génétique), Protéines recombinantes (isolement et purification), Protéines végétales (biosynthèse), Protéines végétales (composition chimique), Protéines végétales (génétique), Régulation de l'expression des gènes végétaux (physiologie), Spécificité du substrat (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- biosynthèse : Betaine-aldehyde dehydrogenase, Protéines recombinantes, Protéines végétales.
- composition chimique : Isoformes de protéines, Protéines végétales.
- génétique : Betaine-aldehyde dehydrogenase, Escherichia coli, Populus, Protéines recombinantes, Protéines végétales.
- isolement et purification : Protéines recombinantes.
- métabolisme : Escherichia coli, Isoformes de protéines.
- physiologie : Régulation de l'expression des gènes végétaux.
- Clonage moléculaire, Données de séquences moléculaires, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Betaine-Aldehyde Dehydrogenase (biosynthesis), Betaine-Aldehyde Dehydrogenase (genetics), Cloning, Molecular (MeSH), Escherichia coli (genetics), Escherichia coli (metabolism), Gene Expression Regulation, Plant (physiology), Molecular Sequence Data (MeSH), Plant Proteins (biosynthesis), Plant Proteins (chemistry), Plant Proteins (genetics), Populus (genetics), Protein Isoforms (chemistry), Protein Isoforms (metabolism), Recombinant Proteins (biosynthesis), Recombinant Proteins (genetics), Recombinant Proteins (isolation & purification), Substrate Specificity (MeSH).
- MESH :
- chemical , biosynthesis : Betaine-Aldehyde Dehydrogenase, Plant Proteins, Recombinant Proteins.
- chemical , chemistry : Plant Proteins, Protein Isoforms.
- chemical , genetics : Betaine-Aldehyde Dehydrogenase, Plant Proteins, Recombinant Proteins.
- genetics : Escherichia coli, Populus.
- chemical , isolation & purification : Recombinant Proteins.
- metabolism : Escherichia coli, Protein Isoforms.
- physiology : Gene Expression Regulation, Plant.
- Amino Acid Sequence, Cloning, Molecular, Molecular Sequence Data, Substrate Specificity.
Abstract
Plant betaine aldehyde dehydrogenase (BADH) is a physiologically important enzyme in response to salt or drought stress. In this study, two BADH genes (PeBADH1 and PeBADH2) were cloned from Populus euphratica. Both PeBADH1 and PeBADH2 genes encode the proteins of 503 amino acid residues, with a calculated molecular mass of 54.93 kDa and 54.90 kDa, respectively. Reverse transcription PCR showed the divergence of expression pattern between the PeBADH1 and PeBADH2 genes in P. euphratica. The recombinant PeBADH1 and PeBADH2 proteins were overexpressed in E. coli, and purified by Ni-affinity chromatography. The PeBADH2 protein had 1.5-fold higher enzymatic activity towards the substrate aldehyde than PeBADH1 protein. The PeBADH1 protein revealed higher thermal stability than PeBADH2 protein. These results indicated obvious functional divergence between the PeBADH1 and PeBADH2 genes.
PubMed: 22712391
Affiliations:
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first="Hailing" last="Yang">Hailing Yang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22712391</idno><idno type="pmid">22712391</idno><idno type="wicri:Area/Main/Corpus">002994</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002994</idno><idno type="wicri:Area/Main/Curation">002994</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">002994</idno><idno type="wicri:Area/Main/Exploration">002994</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">[Functional divergence of betaine aldehyde dehydrogenase genes in Populus euphratica].</title><author><name sortKey="Liu, Jiaqi" sort="Liu, Jiaqi" uniqKey="Liu J" first="Jiaqi" last="Liu">Jiaqi Liu</name><affiliation wicri:level="1"><nlm:affiliation>College of Life Sciences and Biotechnology, Beijing Forestry University, Beijing 100083, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>College of Life Sciences and Biotechnology, Beijing Forestry University, Beijing 100083</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Yang, Xue" sort="Yang, Xue" uniqKey="Yang X" first="Xue" last="Yang">Xue Yang</name></author><author><name sortKey="Di, Li" sort="Di, Li" uniqKey="Di L" first="Li" last="Di">Li Di</name></author><author><name sortKey="Yang, Hailing" sort="Yang, Hailing" uniqKey="Yang H" first="Hailing" last="Yang">Hailing Yang</name></author></analytic><series><title level="j">Sheng wu gong cheng xue bao = Chinese journal of biotechnology</title><idno type="ISSN">1000-3061</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Betaine-Aldehyde Dehydrogenase (biosynthesis)</term><term>Betaine-Aldehyde Dehydrogenase (genetics)</term><term>Cloning, Molecular (MeSH)</term><term>Escherichia coli (genetics)</term><term>Escherichia coli (metabolism)</term><term>Gene Expression Regulation, Plant (physiology)</term><term>Molecular Sequence Data (MeSH)</term><term>Plant Proteins (biosynthesis)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (genetics)</term><term>Populus (genetics)</term><term>Protein Isoforms (chemistry)</term><term>Protein Isoforms (metabolism)</term><term>Recombinant Proteins (biosynthesis)</term><term>Recombinant Proteins (genetics)</term><term>Recombinant Proteins (isolation & purification)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Betaine-aldehyde dehydrogenase (biosynthèse)</term><term>Betaine-aldehyde dehydrogenase (génétique)</term><term>Clonage moléculaire (MeSH)</term><term>Données de séquences 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de séquences moléculaires</term><term>Spécificité du substrat</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Plant betaine aldehyde dehydrogenase (BADH) is a physiologically important enzyme in response to salt or drought stress. In this study, two BADH genes (PeBADH1 and PeBADH2) were cloned from Populus euphratica. Both PeBADH1 and PeBADH2 genes encode the proteins of 503 amino acid residues, with a calculated molecular mass of 54.93 kDa and 54.90 kDa, respectively. Reverse transcription PCR showed the divergence of expression pattern between the PeBADH1 and PeBADH2 genes in P. euphratica. The recombinant PeBADH1 and PeBADH2 proteins were overexpressed in E. coli, and purified by Ni-affinity chromatography. The PeBADH2 protein had 1.5-fold higher enzymatic activity towards the substrate aldehyde than PeBADH1 protein. The PeBADH1 protein revealed higher thermal stability than PeBADH2 protein. These results indicated obvious functional divergence between the PeBADH1 and PeBADH2 genes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22712391</PMID><DateCompleted><Year>2013</Year><Month>09</Month><Day>26</Day></DateCompleted><DateRevised><Year>2012</Year><Month>06</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1000-3061</ISSN><JournalIssue CitedMedium="Print"><Volume>28</Volume><Issue>3</Issue><PubDate><Year>2012</Year><Month>Mar</Month></PubDate></JournalIssue><Title>Sheng wu gong cheng xue bao = Chinese journal of biotechnology</Title><ISOAbbreviation>Sheng Wu Gong Cheng Xue Bao</ISOAbbreviation></Journal><ArticleTitle>[Functional divergence of betaine aldehyde dehydrogenase genes in Populus euphratica].</ArticleTitle><Pagination><MedlinePgn>329-39</MedlinePgn></Pagination><Abstract><AbstractText>Plant betaine aldehyde dehydrogenase (BADH) is a physiologically important enzyme in response to salt or drought stress. In this study, two BADH genes (PeBADH1 and PeBADH2) were cloned from Populus euphratica. Both PeBADH1 and PeBADH2 genes encode the proteins of 503 amino acid residues, with a calculated molecular mass of 54.93 kDa and 54.90 kDa, respectively. Reverse transcription PCR showed the divergence of expression pattern between the PeBADH1 and PeBADH2 genes in P. euphratica. The recombinant PeBADH1 and PeBADH2 proteins were overexpressed in E. coli, and purified by Ni-affinity chromatography. The PeBADH2 protein had 1.5-fold higher enzymatic activity towards the substrate aldehyde than PeBADH1 protein. The PeBADH1 protein revealed higher thermal stability than PeBADH2 protein. 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MajorTopicYN="N">Betaine-Aldehyde Dehydrogenase</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018506" MajorTopicYN="N">Gene Expression Regulation, Plant</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020033" MajorTopicYN="N">Protein Isoforms</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>6</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>6</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2013</Year><Month>9</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">22712391</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country><settlement><li>Pékin</li></settlement></list><tree><noCountry><name sortKey="Di, Li" sort="Di, Li" uniqKey="Di L" first="Li" last="Di">Li Di</name><name sortKey="Yang, Hailing" sort="Yang, Hailing" uniqKey="Yang H" first="Hailing" last="Yang">Hailing Yang</name><name sortKey="Yang, Xue" sort="Yang, Xue" uniqKey="Yang X" first="Xue" last="Yang">Xue Yang</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Liu, Jiaqi" sort="Liu, Jiaqi" uniqKey="Liu J" first="Jiaqi" last="Liu">Jiaqi Liu</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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