Different nitrogen sources modulate activity but not expression of glutamine synthetase in arbuscular mycorrhizal fungi.
Identifieur interne : 003762 ( Main/Corpus ); précédent : 003761; suivant : 003763Different nitrogen sources modulate activity but not expression of glutamine synthetase in arbuscular mycorrhizal fungi.
Auteurs : Magdalene Breuninger ; Carmen G. Trujillo ; Esther Serrano ; Reinhard Fischer ; Natalia RequenaSource :
- Fungal genetics and biology : FG & B [ 1087-1845 ] ; 2004.
English descriptors
- KwdEn :
- Amino Acid Motifs (MeSH), Amino Acid Sequence (MeSH), Base Sequence (MeSH), DNA, Complementary (chemistry), DNA, Complementary (isolation & purification), DNA, Fungal (chemistry), DNA, Fungal (isolation & purification), Enzyme Activators (metabolism), Fungi (enzymology), Fungi (genetics), Fungi (growth & development), Gene Expression Regulation, Fungal (MeSH), Glutamate-Ammonia Ligase (chemistry), Glutamate-Ammonia Ligase (genetics), Glutamate-Ammonia Ligase (metabolism), Glutamine (metabolism), Molecular Sequence Data (MeSH), Mycelium (enzymology), Mycelium (genetics), Mycelium (growth & development), Mycorrhizae (metabolism), Nitrates (metabolism), Nitrogen (metabolism), Phylogeny (MeSH), Quaternary Ammonium Compounds (metabolism), RNA, Fungal (analysis), RNA, Messenger (analysis), Sequence Alignment (MeSH), Sequence Analysis, DNA (MeSH), Sequence Homology, Amino Acid (MeSH), Spores, Fungal (enzymology), Spores, Fungal (genetics), Spores, Fungal (growth & development).
- MESH :
- chemical , analysis : RNA, Fungal, RNA, Messenger.
- chemical , chemistry : DNA, Complementary, DNA, Fungal, Glutamate-Ammonia Ligase.
- chemical , genetics : Glutamate-Ammonia Ligase.
- chemical , isolation & purification : DNA, Complementary, DNA, Fungal.
- chemical , metabolism : Enzyme Activators, Glutamate-Ammonia Ligase, Glutamine, Nitrates, Nitrogen, Quaternary Ammonium Compounds.
- enzymology : Fungi, Mycelium, Spores, Fungal.
- genetics : Fungi, Mycelium, Spores, Fungal.
- growth & development : Fungi, Mycelium, Spores, Fungal.
- metabolism : Mycorrhizae.
- Amino Acid Motifs, Amino Acid Sequence, Base Sequence, Gene Expression Regulation, Fungal, Molecular Sequence Data, Phylogeny, Sequence Alignment, Sequence Analysis, DNA, Sequence Homology, Amino Acid.
Abstract
Glutamine synthetase (GS) is a central enzyme of nitrogen metabolism that allows assimilation of nitrogen and biosynthesis of glutamine. We isolated the cDNA encoding GS from two arbuscular mycorrhizal fungi, Glomus mosseae (GmGln1) and Glomus intraradices (GiGln1). The deduced protein orthologues have a high degree of similarity (92%) with each other as well as with GSs from other fungi. GmGln1 was constitutively expressed during all stages of the fungal life cycle, i.e., spore germination, intraradical and extraradical mycelium. Feeding experiments with different nitrogen sources did not induce any change in the mRNA level of both genes independent of the symbiotic status of the fungus. However, GS activity of extraradical hypahe in G. intraradices was considerably modulated in response to different nitrogen sources. Thus, in a N re-supplementation time-course experiment, GS activity responded quickly to addition of nitrate, ammonium or glutamine. Re-feeding with ammonium produced a general increase in GS activity when compared with hyphae grown in nitrate as a sole N source.
DOI: 10.1016/j.fgb.2004.01.003
PubMed: 15050543
Links to Exploration step
pubmed:15050543Le document en format XML
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Trujillo</name></author><author><name sortKey="Serrano, Esther" sort="Serrano, Esther" uniqKey="Serrano E" first="Esther" last="Serrano">Esther Serrano</name></author><author><name sortKey="Fischer, Reinhard" sort="Fischer, Reinhard" uniqKey="Fischer R" first="Reinhard" last="Fischer">Reinhard Fischer</name></author><author><name sortKey="Requena, Natalia" sort="Requena, Natalia" uniqKey="Requena N" first="Natalia" last="Requena">Natalia Requena</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:15050543</idno><idno type="pmid">15050543</idno><idno type="doi">10.1016/j.fgb.2004.01.003</idno><idno type="wicri:Area/Main/Corpus">003762</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">003762</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Different nitrogen sources modulate activity but not expression of glutamine synthetase in arbuscular mycorrhizal fungi.</title><author><name sortKey="Breuninger, Magdalene" sort="Breuninger, Magdalene" uniqKey="Breuninger M" first="Magdalene" last="Breuninger">Magdalene Breuninger</name><affiliation><nlm:affiliation>Physiological Ecology of Plants Department, University of Tübingen, Auf der Morgenstelle 1, Tübingen 72076, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Trujillo, Carmen G" sort="Trujillo, Carmen G" uniqKey="Trujillo C" first="Carmen G" last="Trujillo">Carmen G. Trujillo</name></author><author><name sortKey="Serrano, Esther" sort="Serrano, Esther" uniqKey="Serrano E" first="Esther" last="Serrano">Esther Serrano</name></author><author><name sortKey="Fischer, Reinhard" sort="Fischer, Reinhard" uniqKey="Fischer R" first="Reinhard" last="Fischer">Reinhard Fischer</name></author><author><name sortKey="Requena, Natalia" sort="Requena, Natalia" uniqKey="Requena N" first="Natalia" last="Requena">Natalia Requena</name></author></analytic><series><title level="j">Fungal genetics and biology : FG & B</title><idno type="ISSN">1087-1845</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Motifs (MeSH)</term><term>Amino Acid Sequence (MeSH)</term><term>Base Sequence (MeSH)</term><term>DNA, Complementary (chemistry)</term><term>DNA, Complementary (isolation & purification)</term><term>DNA, Fungal (chemistry)</term><term>DNA, Fungal (isolation & purification)</term><term>Enzyme Activators (metabolism)</term><term>Fungi (enzymology)</term><term>Fungi (genetics)</term><term>Fungi (growth & development)</term><term>Gene Expression Regulation, Fungal (MeSH)</term><term>Glutamate-Ammonia Ligase (chemistry)</term><term>Glutamate-Ammonia Ligase (genetics)</term><term>Glutamate-Ammonia Ligase (metabolism)</term><term>Glutamine (metabolism)</term><term>Molecular Sequence Data (MeSH)</term><term>Mycelium (enzymology)</term><term>Mycelium (genetics)</term><term>Mycelium (growth & development)</term><term>Mycorrhizae (metabolism)</term><term>Nitrates (metabolism)</term><term>Nitrogen (metabolism)</term><term>Phylogeny (MeSH)</term><term>Quaternary Ammonium Compounds (metabolism)</term><term>RNA, Fungal (analysis)</term><term>RNA, Messenger (analysis)</term><term>Sequence Alignment (MeSH)</term><term>Sequence Analysis, DNA (MeSH)</term><term>Sequence Homology, Amino Acid (MeSH)</term><term>Spores, Fungal (enzymology)</term><term>Spores, Fungal (genetics)</term><term>Spores, Fungal (growth & development)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>RNA, Fungal</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA, Complementary</term><term>DNA, Fungal</term><term>Glutamate-Ammonia Ligase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutamate-Ammonia Ligase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>DNA, Complementary</term><term>DNA, Fungal</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Enzyme Activators</term><term>Glutamate-Ammonia Ligase</term><term>Glutamine</term><term>Nitrates</term><term>Nitrogen</term><term>Quaternary Ammonium Compounds</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Fungi</term><term>Mycelium</term><term>Spores, Fungal</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Fungi</term><term>Mycelium</term><term>Spores, Fungal</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Fungi</term><term>Mycelium</term><term>Spores, Fungal</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mycorrhizae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Motifs</term><term>Amino Acid Sequence</term><term>Base Sequence</term><term>Gene Expression Regulation, Fungal</term><term>Molecular Sequence Data</term><term>Phylogeny</term><term>Sequence Alignment</term><term>Sequence Analysis, DNA</term><term>Sequence Homology, Amino Acid</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Glutamine synthetase (GS) is a central enzyme of nitrogen metabolism that allows assimilation of nitrogen and biosynthesis of glutamine. We isolated the cDNA encoding GS from two arbuscular mycorrhizal fungi, Glomus mosseae (GmGln1) and Glomus intraradices (GiGln1). The deduced protein orthologues have a high degree of similarity (92%) with each other as well as with GSs from other fungi. GmGln1 was constitutively expressed during all stages of the fungal life cycle, i.e., spore germination, intraradical and extraradical mycelium. Feeding experiments with different nitrogen sources did not induce any change in the mRNA level of both genes independent of the symbiotic status of the fungus. However, GS activity of extraradical hypahe in G. intraradices was considerably modulated in response to different nitrogen sources. Thus, in a N re-supplementation time-course experiment, GS activity responded quickly to addition of nitrate, ammonium or glutamine. Re-feeding with ammonium produced a general increase in GS activity when compared with hyphae grown in nitrate as a sole N source.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15050543</PMID><DateCompleted><Year>2004</Year><Month>07</Month><Day>16</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1087-1845</ISSN><JournalIssue CitedMedium="Print"><Volume>41</Volume><Issue>5</Issue><PubDate><Year>2004</Year><Month>May</Month></PubDate></JournalIssue><Title>Fungal genetics and biology : FG & B</Title><ISOAbbreviation>Fungal Genet Biol</ISOAbbreviation></Journal><ArticleTitle>Different nitrogen sources modulate activity but not expression of glutamine synthetase in arbuscular mycorrhizal fungi.</ArticleTitle><Pagination><MedlinePgn>542-52</MedlinePgn></Pagination><Abstract><AbstractText>Glutamine synthetase (GS) is a central enzyme of nitrogen metabolism that allows assimilation of nitrogen and biosynthesis of glutamine. We isolated the cDNA encoding GS from two arbuscular mycorrhizal fungi, Glomus mosseae (GmGln1) and Glomus intraradices (GiGln1). The deduced protein orthologues have a high degree of similarity (92%) with each other as well as with GSs from other fungi. GmGln1 was constitutively expressed during all stages of the fungal life cycle, i.e., spore germination, intraradical and extraradical mycelium. Feeding experiments with different nitrogen sources did not induce any change in the mRNA level of both genes independent of the symbiotic status of the fungus. However, GS activity of extraradical hypahe in G. intraradices was considerably modulated in response to different nitrogen sources. Thus, in a N re-supplementation time-course experiment, GS activity responded quickly to addition of nitrate, ammonium or glutamine. Re-feeding with ammonium produced a general increase in GS activity when compared with hyphae grown in nitrate as a sole N source.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Breuninger</LastName><ForeName>Magdalene</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Physiological Ecology of Plants Department, University of Tübingen, Auf der Morgenstelle 1, Tübingen 72076, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Trujillo</LastName><ForeName>Carmen G</ForeName><Initials>CG</Initials></Author><Author ValidYN="Y"><LastName>Serrano</LastName><ForeName>Esther</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Fischer</LastName><ForeName>Reinhard</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Requena</LastName><ForeName>Natalia</ForeName><Initials>N</Initials></Author></AuthorList><Language>eng</Language><DataBankList 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