Redundancy and metabolic function of the glutamine synthetase gene family in poplar.
Identifieur interne : 001B61 ( Main/Exploration ); précédent : 001B60; suivant : 001B62Redundancy and metabolic function of the glutamine synthetase gene family in poplar.
Auteurs : Vanessa Castro-Rodríguez [Espagne] ; Angel García-Gutiérrez [Espagne] ; Rafael A. Ca As [Espagne] ; Ma Belén Pascual [Espagne] ; Concepci N Avila [Espagne] ; Francisco M. Cánovas [Espagne]Source :
- BMC plant biology [ 1471-2229 ] ; 2015.
Descripteurs français
- KwdFr :
- ARN messager (génétique), ARN messager (métabolisme), Azote (métabolisme), Biocatalyse (MeSH), Cinétique (MeSH), Concentration en ions d'hydrogène (MeSH), Famille multigénique (MeSH), Glutamate-ammonia ligase (génétique), Glutamate-ammonia ligase (métabolisme), Isoenzymes (génétique), Isoenzymes (métabolisme), Lasers (MeSH), Masse moléculaire (MeSH), Microdissection (MeSH), Peptides (métabolisme), Populus (enzymologie), Populus (génétique), Protéines recombinantes (biosynthèse), Régulation de l'expression des gènes codant pour des enzymes (MeSH), Régulation de l'expression des gènes végétaux (MeSH), Stabilité enzymatique (MeSH), Température (MeSH).
- MESH :
- biosynthèse : Protéines recombinantes.
- enzymologie : Populus.
- génétique : ARN messager, Glutamate-ammonia ligase, Isoenzymes, Populus.
- métabolisme : ARN messager, Azote, Glutamate-ammonia ligase, Isoenzymes, Peptides.
- Biocatalyse, Cinétique, Concentration en ions d'hydrogène, Famille multigénique, Lasers, Masse moléculaire, Microdissection, Régulation de l'expression des gènes codant pour des enzymes, Régulation de l'expression des gènes végétaux, Stabilité enzymatique, Température.
English descriptors
- KwdEn :
- Biocatalysis (MeSH), Enzyme Stability (MeSH), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Plant (MeSH), Glutamate-Ammonia Ligase (genetics), Glutamate-Ammonia Ligase (metabolism), Hydrogen-Ion Concentration (MeSH), Isoenzymes (genetics), Isoenzymes (metabolism), Kinetics (MeSH), Lasers (MeSH), Microdissection (MeSH), Molecular Weight (MeSH), Multigene Family (MeSH), Nitrogen (metabolism), Peptides (metabolism), Populus (enzymology), Populus (genetics), RNA, Messenger (genetics), RNA, Messenger (metabolism), Recombinant Proteins (biosynthesis), Temperature (MeSH).
- MESH :
- chemical , biosynthesis : Recombinant Proteins.
- chemical , genetics : Glutamate-Ammonia Ligase, Isoenzymes, RNA, Messenger.
- chemical , metabolism : Glutamate-Ammonia Ligase, Isoenzymes, Nitrogen, Peptides, RNA, Messenger.
- enzymology : Populus.
- genetics : Populus.
- Biocatalysis, Enzyme Stability, Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant, Hydrogen-Ion Concentration, Kinetics, Lasers, Microdissection, Molecular Weight, Multigene Family, Temperature.
Abstract
BACKGROUND
Glutamine synthetase (GS; EC: 6.3.1.2, L-glutamate: ammonia ligase ADP-forming) is a key enzyme in ammonium assimilation and metabolism in higher plants. In poplar, the GS family is organized in 4 groups of duplicated genes, 3 of which code for cytosolic GS isoforms (GS1.1, GS1.2 and GS1.3) and one group that codes for the choroplastic GS isoform (GS2). Our previous work suggested that GS duplicates may have been retained to increase the amount of enzyme in a particular cell type.
RESULTS
The current study was conducted to test this hypothesis by developing a more comprehensive understanding of the molecular and biochemical characteristics of the poplar GS isoenzymes and by determinating their kinetic parameters. To obtain further insights into the function of the poplar GS genes, in situ hybridization and laser capture microdissections were conducted in different tissues, and the precise GS gene spatial expression patterns were determined in specific cell/tissue types of the leaves, stems and roots. The molecular and functional analysis of the poplar GS family and the precise localization of the corresponding mRNA in different cell types strongly suggest that the GS isoforms play non-redundant roles in poplar tree biology. Furthermore, our results support the proposal that a function of the duplicated genes in specific cell/tissue types is to increase the abundance of the enzymes.
CONCLUSION
Taken together, our results reveal that there is no redundancy in the poplar GS family at the whole plant level but it exists in specific cell types where the two duplicated genes are expressed and their gene expression products have similar metabolic roles. Gene redundancy may contribute to the homeostasis of nitrogen metabolism in functions associated with changes in environmental conditions and developmental stages.
DOI: 10.1186/s12870-014-0365-5
PubMed: 25608602
PubMed Central: PMC4329200
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Ca As</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga, Spain. rcanas@uma.es.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga</wicri:regionArea><wicri:noRegion>Málaga</wicri:noRegion></affiliation></author><author><name sortKey="Pascual, Ma Belen" sort="Pascual, Ma Belen" uniqKey="Pascual M" first="Ma Belén" last="Pascual">Ma Belén Pascual</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga, Spain. bpascual@uma.es.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga</wicri:regionArea><wicri:noRegion>Málaga</wicri:noRegion></affiliation></author><author><name sortKey="Avila, Concepci N" sort="Avila, Concepci N" uniqKey="Avila C" first="Concepci N" last="Avila">Concepci N Avila</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga, Spain. cavila@uma.es.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga</wicri:regionArea><wicri:noRegion>Málaga</wicri:noRegion></affiliation></author><author><name sortKey="Canovas, Francisco M" sort="Canovas, Francisco M" uniqKey="Canovas F" first="Francisco M" last="Cánovas">Francisco M. Cánovas</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga, Spain. canovas@uma.es.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga</wicri:regionArea><wicri:noRegion>Málaga</wicri:noRegion></affiliation></author></analytic><series><title level="j">BMC plant biology</title><idno type="eISSN">1471-2229</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biocatalysis (MeSH)</term><term>Enzyme Stability (MeSH)</term><term>Gene Expression Regulation, Enzymologic (MeSH)</term><term>Gene Expression Regulation, Plant (MeSH)</term><term>Glutamate-Ammonia Ligase (genetics)</term><term>Glutamate-Ammonia Ligase (metabolism)</term><term>Hydrogen-Ion Concentration (MeSH)</term><term>Isoenzymes (genetics)</term><term>Isoenzymes (metabolism)</term><term>Kinetics (MeSH)</term><term>Lasers (MeSH)</term><term>Microdissection (MeSH)</term><term>Molecular Weight (MeSH)</term><term>Multigene Family (MeSH)</term><term>Nitrogen (metabolism)</term><term>Peptides (metabolism)</term><term>Populus (enzymology)</term><term>Populus (genetics)</term><term>RNA, Messenger (genetics)</term><term>RNA, Messenger (metabolism)</term><term>Recombinant Proteins (biosynthesis)</term><term>Temperature (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ARN messager (génétique)</term><term>ARN messager (métabolisme)</term><term>Azote (métabolisme)</term><term>Biocatalyse (MeSH)</term><term>Cinétique (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Famille multigénique (MeSH)</term><term>Glutamate-ammonia ligase (génétique)</term><term>Glutamate-ammonia ligase (métabolisme)</term><term>Isoenzymes (génétique)</term><term>Isoenzymes (métabolisme)</term><term>Lasers (MeSH)</term><term>Masse moléculaire (MeSH)</term><term>Microdissection (MeSH)</term><term>Peptides (métabolisme)</term><term>Populus (enzymologie)</term><term>Populus (génétique)</term><term>Protéines recombinantes (biosynthèse)</term><term>Régulation de l'expression des gènes codant pour des enzymes (MeSH)</term><term>Régulation de l'expression des gènes végétaux (MeSH)</term><term>Stabilité enzymatique (MeSH)</term><term>Température (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutamate-Ammonia Ligase</term><term>Isoenzymes</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Glutamate-Ammonia Ligase</term><term>Isoenzymes</term><term>Nitrogen</term><term>Peptides</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protéines recombinantes</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>Populus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ARN messager</term><term>Glutamate-ammonia ligase</term><term>Isoenzymes</term><term>Populus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ARN messager</term><term>Azote</term><term>Glutamate-ammonia ligase</term><term>Isoenzymes</term><term>Peptides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biocatalysis</term><term>Enzyme Stability</term><term>Gene Expression Regulation, Enzymologic</term><term>Gene Expression Regulation, Plant</term><term>Hydrogen-Ion Concentration</term><term>Kinetics</term><term>Lasers</term><term>Microdissection</term><term>Molecular Weight</term><term>Multigene Family</term><term>Temperature</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biocatalyse</term><term>Cinétique</term><term>Concentration en ions d'hydrogène</term><term>Famille multigénique</term><term>Lasers</term><term>Masse moléculaire</term><term>Microdissection</term><term>Régulation de l'expression des gènes codant pour des enzymes</term><term>Régulation de l'expression des gènes végétaux</term><term>Stabilité enzymatique</term><term>Température</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>BACKGROUND</b></p><p>Glutamine synthetase (GS; EC: 6.3.1.2, L-glutamate: ammonia ligase ADP-forming) is a key enzyme in ammonium assimilation and metabolism in higher plants. In poplar, the GS family is organized in 4 groups of duplicated genes, 3 of which code for cytosolic GS isoforms (GS1.1, GS1.2 and GS1.3) and one group that codes for the choroplastic GS isoform (GS2). Our previous work suggested that GS duplicates may have been retained to increase the amount of enzyme in a particular cell type.</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>The current study was conducted to test this hypothesis by developing a more comprehensive understanding of the molecular and biochemical characteristics of the poplar GS isoenzymes and by determinating their kinetic parameters. To obtain further insights into the function of the poplar GS genes, in situ hybridization and laser capture microdissections were conducted in different tissues, and the precise GS gene spatial expression patterns were determined in specific cell/tissue types of the leaves, stems and roots. The molecular and functional analysis of the poplar GS family and the precise localization of the corresponding mRNA in different cell types strongly suggest that the GS isoforms play non-redundant roles in poplar tree biology. Furthermore, our results support the proposal that a function of the duplicated genes in specific cell/tissue types is to increase the abundance of the enzymes.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSION</b></p><p>Taken together, our results reveal that there is no redundancy in the poplar GS family at the whole plant level but it exists in specific cell types where the two duplicated genes are expressed and their gene expression products have similar metabolic roles. Gene redundancy may contribute to the homeostasis of nitrogen metabolism in functions associated with changes in environmental conditions and developmental stages.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25608602</PMID><DateCompleted><Year>2016</Year><Month>03</Month><Day>28</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1471-2229</ISSN><JournalIssue CitedMedium="Internet"><Volume>15</Volume><PubDate><Year>2015</Year><Month>Jan</Month><Day>22</Day></PubDate></JournalIssue><Title>BMC plant biology</Title><ISOAbbreviation>BMC Plant Biol</ISOAbbreviation></Journal><ArticleTitle>Redundancy and metabolic function of the glutamine synthetase gene family in poplar.</ArticleTitle><Pagination><MedlinePgn>20</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1186/s12870-014-0365-5</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Glutamine synthetase (GS; EC: 6.3.1.2, L-glutamate: ammonia ligase ADP-forming) is a key enzyme in ammonium assimilation and metabolism in higher plants. In poplar, the GS family is organized in 4 groups of duplicated genes, 3 of which code for cytosolic GS isoforms (GS1.1, GS1.2 and GS1.3) and one group that codes for the choroplastic GS isoform (GS2). Our previous work suggested that GS duplicates may have been retained to increase the amount of enzyme in a particular cell type.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">The current study was conducted to test this hypothesis by developing a more comprehensive understanding of the molecular and biochemical characteristics of the poplar GS isoenzymes and by determinating their kinetic parameters. To obtain further insights into the function of the poplar GS genes, in situ hybridization and laser capture microdissections were conducted in different tissues, and the precise GS gene spatial expression patterns were determined in specific cell/tissue types of the leaves, stems and roots. The molecular and functional analysis of the poplar GS family and the precise localization of the corresponding mRNA in different cell types strongly suggest that the GS isoforms play non-redundant roles in poplar tree biology. Furthermore, our results support the proposal that a function of the duplicated genes in specific cell/tissue types is to increase the abundance of the enzymes.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">Taken together, our results reveal that there is no redundancy in the poplar GS family at the whole plant level but it exists in specific cell types where the two duplicated genes are expressed and their gene expression products have similar metabolic roles. Gene redundancy may contribute to the homeostasis of nitrogen metabolism in functions associated with changes in environmental conditions and developmental stages.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Castro-Rodríguez</LastName><ForeName>Vanessa</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga, Spain. vavicaro@uma.es.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>García-Gutiérrez</LastName><ForeName>Angel</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga, Spain. aggtez@uma.es.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cañas</LastName><ForeName>Rafael A</ForeName><Initials>RA</Initials><AffiliationInfo><Affiliation>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga, Spain. rcanas@uma.es.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pascual</LastName><ForeName>Ma Belén</ForeName><Initials>MB</Initials><AffiliationInfo><Affiliation>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga, Spain. bpascual@uma.es.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Avila</LastName><ForeName>Concepción</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga, Spain. cavila@uma.es.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cánovas</LastName><ForeName>Francisco M</ForeName><Initials>FM</Initials><AffiliationInfo><Affiliation>Departamento de Biología Molecular y Bioquímica, Facultad de Ciencias, Campus Universitario de Teatinos, Universidad de Málaga, 29071, Málaga, Spain. canovas@uma.es.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>01</Month><Day>22</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>BMC Plant Biol</MedlineTA><NlmUniqueID>100967807</NlmUniqueID><ISSNLinking>1471-2229</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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Ca As</name><name sortKey="Canovas, Francisco M" sort="Canovas, Francisco M" uniqKey="Canovas F" first="Francisco M" last="Cánovas">Francisco M. Cánovas</name><name sortKey="Garcia Gutierrez, Angel" sort="Garcia Gutierrez, Angel" uniqKey="Garcia Gutierrez A" first="Angel" last="García-Gutiérrez">Angel García-Gutiérrez</name><name sortKey="Pascual, Ma Belen" sort="Pascual, Ma Belen" uniqKey="Pascual M" first="Ma Belén" last="Pascual">Ma Belén Pascual</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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