The Lotus japonicus acyl-acyl carrier protein thioesterase FatM is required for mycorrhiza formation and lipid accumulation of Rhizophagus irregularis.
Identifieur interne : 000775 ( Main/Exploration ); précédent : 000774; suivant : 000776The Lotus japonicus acyl-acyl carrier protein thioesterase FatM is required for mycorrhiza formation and lipid accumulation of Rhizophagus irregularis.
Auteurs : Mathias Brands [Allemagne] ; Vera Wewer [Allemagne] ; Andreas Keymer [Allemagne] ; Caroline Gutjahr [Allemagne] ; Peter Dörmann [Allemagne]Source :
- The Plant journal : for cell and molecular biology [ 1365-313X ] ; 2018.
Descripteurs français
- KwdFr :
- Acides gras (métabolisme), Loteae (microbiologie), Loteae (métabolisme), Loteae (physiologie), Mycorhizes (métabolisme), Mycorhizes (physiologie), Métabolisme lipidique (MeSH), Protéines végétales (métabolisme), Protéines végétales (physiologie), Racines de plante (microbiologie), Racines de plante (métabolisme), Symbiose (physiologie), Thiolester hydrolases (métabolisme), Thiolester hydrolases (physiologie).
- MESH :
- microbiologie : Loteae, Racines de plante.
- métabolisme : Acides gras, Loteae, Mycorhizes, Protéines végétales, Racines de plante, Thiolester hydrolases.
- physiologie : Loteae, Mycorhizes, Protéines végétales, Symbiose, Thiolester hydrolases.
- Métabolisme lipidique.
English descriptors
- KwdEn :
- Fatty Acids (metabolism), Lipid Metabolism (MeSH), Lotus (metabolism), Lotus (microbiology), Lotus (physiology), Mycorrhizae (metabolism), Mycorrhizae (physiology), Plant Proteins (metabolism), Plant Proteins (physiology), Plant Roots (metabolism), Plant Roots (microbiology), Symbiosis (physiology), Thiolester Hydrolases (metabolism), Thiolester Hydrolases (physiology).
- MESH :
- chemical , metabolism : Fatty Acids, Plant Proteins, Thiolester Hydrolases.
- metabolism : Lotus, Mycorrhizae, Plant Roots.
- microbiology : Lotus, Plant Roots.
- physiology : Lotus, Mycorrhizae, Plant Proteins, Symbiosis, Thiolester Hydrolases.
- Lipid Metabolism.
Abstract
Arbuscular mycorrhiza (AM) fungi establish symbiotic interactions with plants, providing the host plant with minerals, i.e. phosphate, in exchange for organic carbon. Arbuscular mycorrhiza fungi of the order Glomerales produce vesicles which store lipids as an energy and carbon source. Acyl-acyl carrier protein (ACP) thioesterases (Fat) are essential components of the plant plastid-localized fatty acid synthase and determine the chain length of de novo synthesized fatty acids. In addition to the ubiquitous FatA and FatB thioesterases, AM-competent plants contain an additional, AM-specific, FatM gene. Here, we characterize FatM from Lotus japonicus by phenotypically analyzing fatm mutant lines and by studying the biochemical function of the recombinant FatM protein. Reduced shoot phosphate content in fatm indicates compromised symbiotic phosphate uptake due to reduced arbuscule branching, and the fungus shows reduced lipid accumulation accompanied by the occurrence of smaller and less frequent vesicles. Lipid profiling reveals a decrease in mycorrhiza-specific phospholipid forms, AM fungal signature fatty acids (e.g. 16:1ω5, 18:1ω7 and 20:3) and storage lipids. Recombinant FatM shows preference for palmitoyl (16:0)-ACP, indicating that large amounts of 16:0 fatty acid are exported from the plastids of arbuscule-containing cells. Stable isotope labeling with [13 C2 ]acetate showed reduced incorporation into mycorrhiza-specific fatty acids in the fatm mutant. Therefore, colonized cells reprogram plastidial de novo fatty acid synthesis towards the production of extra amounts of 16:0, which is in agreement with previous results that fatty acid-containing lipids are transported from the plant to the fungus.
DOI: 10.1111/tpj.13943
PubMed: 29687516
Affiliations:
- Allemagne
- Bavière, District de Cologne, District de Haute-Bavière, Rhénanie-du-Nord-Westphalie
- Bonn, Cologne, Munich
- Université Louis-et-Maximilien de Munich
Links toward previous steps (curation, corpus...)
Le document en format XML
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thioesterase FatM is required for mycorrhiza formation and lipid accumulation of Rhizophagus irregularis.</title><author><name sortKey="Brands, Mathias" sort="Brands, Mathias" uniqKey="Brands M" first="Mathias" last="Brands">Mathias Brands</name><affiliation wicri:level="3"><nlm:affiliation>Institute for Molecular Biotechnology and Physiology of Plants (IMBIO), University of Bonn, Karlrobert-Kreiten-Straße 13, 53115, Bonn, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Molecular Biotechnology and Physiology of Plants (IMBIO), University of Bonn, Karlrobert-Kreiten-Straße 13, 53115, Bonn</wicri:regionArea><placeName><region type="land" nuts="1">Rhénanie-du-Nord-Westphalie</region><region type="district" nuts="2">District de Cologne</region><settlement type="city">Bonn</settlement></placeName></affiliation></author><author><name sortKey="Wewer, Vera" sort="Wewer, Vera" uniqKey="Wewer V" first="Vera" last="Wewer">Vera Wewer</name><affiliation wicri:level="3"><nlm:affiliation>Institute for Molecular Biotechnology and Physiology of Plants (IMBIO), University of Bonn, Karlrobert-Kreiten-Straße 13, 53115, Bonn, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Molecular Biotechnology and Physiology of Plants (IMBIO), University of Bonn, Karlrobert-Kreiten-Straße 13, 53115, Bonn</wicri:regionArea><placeName><region type="land" nuts="1">Rhénanie-du-Nord-Westphalie</region><region type="district" nuts="2">District de Cologne</region><settlement type="city">Bonn</settlement></placeName></affiliation><affiliation wicri:level="3"><nlm:affiliation>Center of Excellence in Plant Sciences (CEPLAS), Mass Spectrometry Platform, University of Cologne, Zülpicher Straße 47b, 50674, Cologne, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Center of Excellence in Plant Sciences (CEPLAS), Mass Spectrometry Platform, University of 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sort="Gutjahr, Caroline" uniqKey="Gutjahr C" first="Caroline" last="Gutjahr">Caroline Gutjahr</name><affiliation wicri:level="1"><nlm:affiliation>Faculty of Biology, Genetics, Biocenter, Martinsried, LMU Munich, Großhaderner Straße 2-4, 82152, Martinsried, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Faculty of Biology, Genetics, Biocenter, Martinsried, LMU Munich, Großhaderner Straße 2-4, 82152, Martinsried</wicri:regionArea><wicri:noRegion>82152, Martinsried</wicri:noRegion><wicri:noRegion>82152, Martinsried</wicri:noRegion><wicri:noRegion>Martinsried</wicri:noRegion></affiliation><affiliation wicri:level="4"><nlm:affiliation>Plant Genetics, School of Life Sciences Weihenstephan, Technical University of Munich, Emil Ramann Straße 4, 85354, Freising, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Plant Genetics, School of Life Sciences Weihenstephan, Technical University of Munich, Emil Ramann Straße 4, 85354, Freising</wicri:regionArea><wicri:noRegion>85354, Freising</wicri:noRegion><orgName type="university">Université Louis-et-Maximilien de Munich</orgName><placeName><settlement type="city">Munich</settlement><region type="land" nuts="1">Bavière</region><region type="district" nuts="2">District de Haute-Bavière</region></placeName></affiliation></author><author><name sortKey="Dormann, Peter" sort="Dormann, Peter" uniqKey="Dormann P" first="Peter" last="Dörmann">Peter Dörmann</name><affiliation wicri:level="3"><nlm:affiliation>Institute for Molecular Biotechnology and Physiology of Plants (IMBIO), University of Bonn, Karlrobert-Kreiten-Straße 13, 53115, Bonn, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Institute for Molecular Biotechnology and Physiology of Plants (IMBIO), University of Bonn, Karlrobert-Kreiten-Straße 13, 53115, Bonn</wicri:regionArea><placeName><region type="land" nuts="1">Rhénanie-du-Nord-Westphalie</region><region type="district" nuts="2">District de Cologne</region><settlement type="city">Bonn</settlement></placeName></affiliation></author></analytic><series><title level="j">The Plant journal : for cell and molecular biology</title><idno type="eISSN">1365-313X</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Fatty Acids (metabolism)</term><term>Lipid Metabolism (MeSH)</term><term>Lotus (metabolism)</term><term>Lotus (microbiology)</term><term>Lotus (physiology)</term><term>Mycorrhizae (metabolism)</term><term>Mycorrhizae (physiology)</term><term>Plant Proteins (metabolism)</term><term>Plant Proteins (physiology)</term><term>Plant Roots (metabolism)</term><term>Plant Roots (microbiology)</term><term>Symbiosis (physiology)</term><term>Thiolester Hydrolases (metabolism)</term><term>Thiolester Hydrolases (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides gras (métabolisme)</term><term>Loteae (microbiologie)</term><term>Loteae (métabolisme)</term><term>Loteae (physiologie)</term><term>Mycorhizes (métabolisme)</term><term>Mycorhizes (physiologie)</term><term>Métabolisme lipidique (MeSH)</term><term>Protéines végétales (métabolisme)</term><term>Protéines végétales (physiologie)</term><term>Racines de plante (microbiologie)</term><term>Racines de plante (métabolisme)</term><term>Symbiose (physiologie)</term><term>Thiolester hydrolases (métabolisme)</term><term>Thiolester hydrolases (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fatty Acids</term><term>Plant Proteins</term><term>Thiolester Hydrolases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Lotus</term><term>Mycorrhizae</term><term>Plant Roots</term></keywords><keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Loteae</term><term>Racines de plante</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Lotus</term><term>Plant Roots</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Acides gras</term><term>Loteae</term><term>Mycorhizes</term><term>Protéines végétales</term><term>Racines de plante</term><term>Thiolester hydrolases</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Loteae</term><term>Mycorhizes</term><term>Protéines végétales</term><term>Symbiose</term><term>Thiolester hydrolases</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Lotus</term><term>Mycorrhizae</term><term>Plant Proteins</term><term>Symbiosis</term><term>Thiolester Hydrolases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Lipid Metabolism</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Métabolisme lipidique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Arbuscular mycorrhiza (AM) fungi establish symbiotic interactions with plants, providing the host plant with minerals, i.e. phosphate, in exchange for organic carbon. Arbuscular mycorrhiza fungi of the order Glomerales produce vesicles which store lipids as an energy and carbon source. Acyl-acyl carrier protein (ACP) thioesterases (Fat) are essential components of the plant plastid-localized fatty acid synthase and determine the chain length of de novo synthesized fatty acids. In addition to the ubiquitous FatA and FatB thioesterases, AM-competent plants contain an additional, AM-specific, FatM gene. Here, we characterize FatM from Lotus japonicus by phenotypically analyzing fatm mutant lines and by studying the biochemical function of the recombinant FatM protein. Reduced shoot phosphate content in fatm indicates compromised symbiotic phosphate uptake due to reduced arbuscule branching, and the fungus shows reduced lipid accumulation accompanied by the occurrence of smaller and less frequent vesicles. Lipid profiling reveals a decrease in mycorrhiza-specific phospholipid forms, AM fungal signature fatty acids (e.g. 16:1ω5, 18:1ω7 and 20:3) and storage lipids. Recombinant FatM shows preference for palmitoyl (16:0)-ACP, indicating that large amounts of 16:0 fatty acid are exported from the plastids of arbuscule-containing cells. Stable isotope labeling with [<sup>13</sup> C<sub>2</sub> ]acetate showed reduced incorporation into mycorrhiza-specific fatty acids in the fatm mutant. Therefore, colonized cells reprogram plastidial de novo fatty acid synthesis towards the production of extra amounts of 16:0, which is in agreement with previous results that fatty acid-containing lipids are transported from the plant to the fungus.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29687516</PMID><DateCompleted><Year>2019</Year><Month>06</Month><Day>03</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>03</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1365-313X</ISSN><JournalIssue CitedMedium="Internet"><Volume>95</Volume><Issue>2</Issue><PubDate><Year>2018</Year><Month>07</Month></PubDate></JournalIssue><Title>The Plant journal : for cell and molecular biology</Title><ISOAbbreviation>Plant J</ISOAbbreviation></Journal><ArticleTitle>The Lotus japonicus acyl-acyl carrier protein thioesterase FatM is required for mycorrhiza formation and lipid accumulation of Rhizophagus irregularis.</ArticleTitle><Pagination><MedlinePgn>219-232</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/tpj.13943</ELocationID><Abstract><AbstractText>Arbuscular mycorrhiza (AM) fungi establish symbiotic interactions with plants, providing the host plant with minerals, i.e. phosphate, in exchange for organic carbon. Arbuscular mycorrhiza fungi of the order Glomerales produce vesicles which store lipids as an energy and carbon source. Acyl-acyl carrier protein (ACP) thioesterases (Fat) are essential components of the plant plastid-localized fatty acid synthase and determine the chain length of de novo synthesized fatty acids. In addition to the ubiquitous FatA and FatB thioesterases, AM-competent plants contain an additional, AM-specific, FatM gene. Here, we characterize FatM from Lotus japonicus by phenotypically analyzing fatm mutant lines and by studying the biochemical function of the recombinant FatM protein. Reduced shoot phosphate content in fatm indicates compromised symbiotic phosphate uptake due to reduced arbuscule branching, and the fungus shows reduced lipid accumulation accompanied by the occurrence of smaller and less frequent vesicles. Lipid profiling reveals a decrease in mycorrhiza-specific phospholipid forms, AM fungal signature fatty acids (e.g. 16:1ω5, 18:1ω7 and 20:3) and storage lipids. Recombinant FatM shows preference for palmitoyl (16:0)-ACP, indicating that large amounts of 16:0 fatty acid are exported from the plastids of arbuscule-containing cells. Stable isotope labeling with [<sup>13</sup> C<sub>2</sub> ]acetate showed reduced incorporation into mycorrhiza-specific fatty acids in the fatm mutant. Therefore, colonized cells reprogram plastidial de novo fatty acid synthesis towards the production of extra amounts of 16:0, which is in agreement with previous results that fatty acid-containing lipids are transported from the plant to the fungus.</AbstractText><CopyrightInformation>© 2018 The Authors The Plant Journal © 2018 John Wiley & Sons Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Brands</LastName><ForeName>Mathias</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institute for Molecular Biotechnology and Physiology of Plants (IMBIO), University of Bonn, Karlrobert-Kreiten-Straße 13, 53115, Bonn, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wewer</LastName><ForeName>Vera</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Institute for Molecular Biotechnology and Physiology of Plants (IMBIO), University of Bonn, Karlrobert-Kreiten-Straße 13, 53115, Bonn, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center of Excellence in Plant Sciences (CEPLAS), Mass Spectrometry Platform, University of Cologne, Zülpicher Straße 47b, 50674, Cologne, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Keymer</LastName><ForeName>Andreas</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Faculty of Biology, Genetics, Biocenter, Martinsried, LMU Munich, Großhaderner Straße 2-4, 82152, Martinsried, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gutjahr</LastName><ForeName>Caroline</ForeName><Initials>C</Initials><Identifier Source="ORCID">0000-0001-6163-745X</Identifier><AffiliationInfo><Affiliation>Faculty of Biology, Genetics, Biocenter, Martinsried, LMU Munich, Großhaderner Straße 2-4, 82152, Martinsried, Germany.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Plant Genetics, School of Life Sciences Weihenstephan, Technical University of Munich, Emil Ramann Straße 4, 85354, Freising, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dörmann</LastName><ForeName>Peter</ForeName><Initials>P</Initials><Identifier Source="ORCID">0000-0002-5845-9370</Identifier><AffiliationInfo><Affiliation>Institute for Molecular Biotechnology and Physiology of Plants (IMBIO), University of Bonn, Karlrobert-Kreiten-Straße 13, 53115, Bonn, Germany.</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>2018</Year><Month>05</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Plant J</MedlineTA><NlmUniqueID>9207397</NlmUniqueID><ISSNLinking>0960-7412</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005227">Fatty Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.2.-</RegistryNumber><NameOfSubstance UI="D013869">Thiolester Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.2.14</RegistryNumber><NameOfSubstance UI="C018748">oleoyl-(acyl-carrier-protein) hydrolase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D005227" MajorTopicYN="N">Fatty Acids</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D050356" MajorTopicYN="Y">Lipid Metabolism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000070116" MajorTopicYN="N">Lotus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D038821" MajorTopicYN="N">Mycorrhizae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018517" MajorTopicYN="N">Plant Roots</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013559" MajorTopicYN="N">Symbiosis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013869" MajorTopicYN="N">Thiolester Hydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">acyl-ACP thioesterase</Keyword><Keyword MajorTopicYN="Y">arbuscular mycorrhiza</Keyword><Keyword MajorTopicYN="Y">carbon transfer</Keyword><Keyword MajorTopicYN="Y">fatty acid</Keyword><Keyword MajorTopicYN="Y">lipid</Keyword><Keyword MajorTopicYN="Y">plastid</Keyword><Keyword MajorTopicYN="Y">stable isotope labeling</Keyword><Keyword MajorTopicYN="Y">symbiosis</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>01</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>03</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>04</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>4</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>6</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>4</Month><Day>25</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29687516</ArticleId><ArticleId IdType="doi">10.1111/tpj.13943</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country><region><li>Bavière</li><li>District de Cologne</li><li>District de Haute-Bavière</li><li>Rhénanie-du-Nord-Westphalie</li></region><settlement><li>Bonn</li><li>Cologne</li><li>Munich</li></settlement><orgName><li>Université Louis-et-Maximilien de Munich</li></orgName></list><tree><country name="Allemagne"><region name="Rhénanie-du-Nord-Westphalie"><name sortKey="Brands, Mathias" sort="Brands, Mathias" uniqKey="Brands M" first="Mathias" last="Brands">Mathias Brands</name></region><name sortKey="Dormann, Peter" sort="Dormann, Peter" uniqKey="Dormann P" first="Peter" last="Dörmann">Peter Dörmann</name><name sortKey="Gutjahr, Caroline" sort="Gutjahr, Caroline" uniqKey="Gutjahr C" first="Caroline" last="Gutjahr">Caroline Gutjahr</name><name sortKey="Gutjahr, Caroline" sort="Gutjahr, Caroline" uniqKey="Gutjahr C" first="Caroline" last="Gutjahr">Caroline Gutjahr</name><name sortKey="Keymer, Andreas" sort="Keymer, Andreas" uniqKey="Keymer A" first="Andreas" last="Keymer">Andreas Keymer</name><name sortKey="Wewer, Vera" sort="Wewer, Vera" uniqKey="Wewer V" first="Vera" last="Wewer">Vera Wewer</name><name sortKey="Wewer, Vera" sort="Wewer, Vera" uniqKey="Wewer V" first="Vera" last="Wewer">Vera Wewer</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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