Functional Research on Three Presumed Asparagine Synthetase Family Members in Poplar.
Identifieur interne : 000922 ( Main/Curation ); précédent : 000921; suivant : 000923Functional Research on Three Presumed Asparagine Synthetase Family Members in Poplar.
Auteurs : Chunpu Qu [République populaire de Chine] ; Bingqing Hao [République populaire de Chine] ; Xiuyue Xu [République populaire de Chine] ; Yuchen Wang [République populaire de Chine] ; Chengjun Yang [République populaire de Chine] ; Zhiru Xu [République populaire de Chine] ; Guanjun Liu [République populaire de Chine]Source :
- Genes [ 2073-4425 ] ; 2019.
Descripteurs français
- KwdFr :
- Asparagine (métabolisme), Aspartate-ammonia ligase (composition chimique), Aspartate-ammonia ligase (génétique), Azote (métabolisme), Escherichia coli (génétique), Glutamate-ammonia ligase (composition chimique), Glutamate-ammonia ligase (génétique), Glutamine (métabolisme), Populus (enzymologie), Populus (génétique), Régulation de l'expression des gènes végétaux (MeSH).
- MESH :
- composition chimique : Aspartate-ammonia ligase, Glutamate-ammonia ligase.
- enzymologie : Populus.
- génétique : Aspartate-ammonia ligase, Escherichia coli, Glutamate-ammonia ligase, Populus.
- métabolisme : Asparagine, Azote, Glutamine.
- Régulation de l'expression des gènes végétaux.
English descriptors
- KwdEn :
- Asparagine (metabolism), Aspartate-Ammonia Ligase (chemistry), Aspartate-Ammonia Ligase (genetics), Escherichia coli (genetics), Gene Expression Regulation, Plant (MeSH), Glutamate-Ammonia Ligase (chemistry), Glutamate-Ammonia Ligase (genetics), Glutamine (metabolism), Nitrogen (metabolism), Populus (enzymology), Populus (genetics).
- MESH :
- chemical , chemistry : Aspartate-Ammonia Ligase, Glutamate-Ammonia Ligase.
- chemical , genetics : Aspartate-Ammonia Ligase, Glutamate-Ammonia Ligase.
- chemical , metabolism : Asparagine, Glutamine, Nitrogen.
- enzymology : Populus.
- genetics : Escherichia coli, Populus.
- Gene Expression Regulation, Plant.
Abstract
Asparagine synthetase (AS), a key enzyme in plant nitrogen metabolism, plays an important role in plant nitrogen assimilation and distribution. Asparagine (Asn), the product of asparagine synthetase, is one of the main compounds responsible for organic nitrogen transport and storage in plants. In this study, we performed complementation experiments using an Asn-deficient Escherichia coli strain to demonstrate that three putative asparagine synthetase family members in poplar (Populussimonii× P.nigra) function in Asn synthesis. Quantitative real-time PCR revealed that the three members had high expression levels in different tissues of poplar and were regulated by exogenous nitrogen. PnAS1 and PnAS2 were also affected by diurnal rhythm. Long-term dark treatment resulted in a significant increase in PnAS1 and PnAS3 expression levels. Under long-term light conditions, however, PnAS2 expression decreased significantly in the intermediate region of leaves. Exogenous application of ammonium nitrogen, glutamine, and a glutamine synthetase inhibitor revealed that PnAS3 was more sensitive to exogenous glutamine, while PnAS1 and PnAS2 were more susceptible to exogenous ammonium nitrogen. Our results suggest that the various members of the PnAS gene family have distinct roles in different tissues and are regulated in different ways.
DOI: 10.3390/genes10050326
PubMed: 31035411
PubMed Central: PMC6562506
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pubmed:31035411Le document en format XML
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<author><name sortKey="Liu, Guanjun" sort="Liu, Guanjun" uniqKey="Liu G" first="Guanjun" last="Liu">Guanjun Liu</name>
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<term>Aspartate-Ammonia Ligase (chemistry)</term>
<term>Aspartate-Ammonia Ligase (genetics)</term>
<term>Escherichia coli (genetics)</term>
<term>Gene Expression Regulation, Plant (MeSH)</term>
<term>Glutamate-Ammonia Ligase (chemistry)</term>
<term>Glutamate-Ammonia Ligase (genetics)</term>
<term>Glutamine (metabolism)</term>
<term>Nitrogen (metabolism)</term>
<term>Populus (enzymology)</term>
<term>Populus (genetics)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Asparagine (métabolisme)</term>
<term>Aspartate-ammonia ligase (composition chimique)</term>
<term>Aspartate-ammonia ligase (génétique)</term>
<term>Azote (métabolisme)</term>
<term>Escherichia coli (génétique)</term>
<term>Glutamate-ammonia ligase (composition chimique)</term>
<term>Glutamate-ammonia ligase (génétique)</term>
<term>Glutamine (métabolisme)</term>
<term>Populus (enzymologie)</term>
<term>Populus (génétique)</term>
<term>Régulation de l'expression des gènes végétaux (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Aspartate-Ammonia Ligase</term>
<term>Glutamate-Ammonia Ligase</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Aspartate-Ammonia Ligase</term>
<term>Glutamate-Ammonia Ligase</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Asparagine</term>
<term>Glutamine</term>
<term>Nitrogen</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Aspartate-ammonia ligase</term>
<term>Glutamate-ammonia ligase</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Aspartate-ammonia ligase</term>
<term>Escherichia coli</term>
<term>Glutamate-ammonia ligase</term>
<term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Asparagine</term>
<term>Azote</term>
<term>Glutamine</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Gene Expression Regulation, Plant</term>
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<front><div type="abstract" xml:lang="en">Asparagine synthetase (AS), a key enzyme in plant nitrogen metabolism, plays an important role in plant nitrogen assimilation and distribution. Asparagine (Asn), the product of asparagine synthetase, is one of the main compounds responsible for organic nitrogen transport and storage in plants. In this study, we performed complementation experiments using an Asn-deficient <i>Escherichia coli</i>
strain to demonstrate that three putative asparagine synthetase family members in poplar (<i>Populus</i>
<i>simonii</i>
<i>× P.</i>
<i>nigra</i>
) function in Asn synthesis. Quantitative real-time PCR revealed that the three members had high expression levels in different tissues of poplar and were regulated by exogenous nitrogen. <i>PnAS1</i>
and <i>PnAS2</i>
were also affected by diurnal rhythm. Long-term dark treatment resulted in a significant increase in <i>PnAS1</i>
and <i>PnAS3</i>
expression levels. Under long-term light conditions, however, <i>PnAS2</i>
expression decreased significantly in the intermediate region of leaves. Exogenous application of ammonium nitrogen, glutamine, and a glutamine synthetase inhibitor revealed that <i>PnAS3</i>
was more sensitive to exogenous glutamine, while <i>PnAS1</i>
and <i>PnAS2</i>
were more susceptible to exogenous ammonium nitrogen. Our results suggest that the various members of the <i>PnAS</i>
gene family have distinct roles in different tissues and are regulated in different ways.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31035411</PMID>
<DateCompleted><Year>2019</Year>
<Month>12</Month>
<Day>26</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>09</Day>
</DateRevised>
<Article PubModel="Electronic"><Journal><ISSN IssnType="Print">2073-4425</ISSN>
<JournalIssue CitedMedium="Print"><Volume>10</Volume>
<Issue>5</Issue>
<PubDate><Year>2019</Year>
<Month>04</Month>
<Day>28</Day>
</PubDate>
</JournalIssue>
<Title>Genes</Title>
<ISOAbbreviation>Genes (Basel)</ISOAbbreviation>
</Journal>
<ArticleTitle>Functional Research on Three Presumed Asparagine Synthetase Family Members in Poplar.</ArticleTitle>
<ELocationID EIdType="pii" ValidYN="Y">E326</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.3390/genes10050326</ELocationID>
<Abstract><AbstractText>Asparagine synthetase (AS), a key enzyme in plant nitrogen metabolism, plays an important role in plant nitrogen assimilation and distribution. Asparagine (Asn), the product of asparagine synthetase, is one of the main compounds responsible for organic nitrogen transport and storage in plants. In this study, we performed complementation experiments using an Asn-deficient <i>Escherichia coli</i>
strain to demonstrate that three putative asparagine synthetase family members in poplar (<i>Populus</i>
<i>simonii</i>
<i>× P.</i>
<i>nigra</i>
) function in Asn synthesis. Quantitative real-time PCR revealed that the three members had high expression levels in different tissues of poplar and were regulated by exogenous nitrogen. <i>PnAS1</i>
and <i>PnAS2</i>
were also affected by diurnal rhythm. Long-term dark treatment resulted in a significant increase in <i>PnAS1</i>
and <i>PnAS3</i>
expression levels. Under long-term light conditions, however, <i>PnAS2</i>
expression decreased significantly in the intermediate region of leaves. Exogenous application of ammonium nitrogen, glutamine, and a glutamine synthetase inhibitor revealed that <i>PnAS3</i>
was more sensitive to exogenous glutamine, while <i>PnAS1</i>
and <i>PnAS2</i>
were more susceptible to exogenous ammonium nitrogen. Our results suggest that the various members of the <i>PnAS</i>
gene family have distinct roles in different tissues and are regulated in different ways.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Qu</LastName>
<ForeName>Chunpu</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Tree Genetics and Breeding (Northeast Forestry University), School of Forestry, Northeast Forestry University, Harbin 150040, China. qcp_0451@163.com.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>School of Forestry, Northeast Forestry University, Harbin 150040, China. qcp_0451@163.com.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Hao</LastName>
<ForeName>Bingqing</ForeName>
<Initials>B</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Tree Genetics and Breeding (Northeast Forestry University), School of Forestry, Northeast Forestry University, Harbin 150040, China. bqhao2019@163.com.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>School of Forestry, Northeast Forestry University, Harbin 150040, China. bqhao2019@163.com.</Affiliation>
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<AffiliationInfo><Affiliation>Guangxi Forestry Research Institute, Nanning 530000, China. bqhao2019@163.com.</Affiliation>
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<Month>04</Month>
<Day>28</Day>
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<MedlineTA>Genes (Basel)</MedlineTA>
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<MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
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<Keyword MajorTopicYN="Y">asparagine synthetase</Keyword>
<Keyword MajorTopicYN="Y">expression patterns</Keyword>
<Keyword MajorTopicYN="Y">functional research</Keyword>
<Keyword MajorTopicYN="Y">transcriptional regulation</Keyword>
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<CoiStatement>The authors declare no conflict of interest.</CoiStatement>
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<Day>16</Day>
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