Biosynthetic pathway of indole-3-acetic acid in ectomycorrhizal fungi collected from northern Thailand.
Identifieur interne : 000210 ( Main/Corpus ); précédent : 000209; suivant : 000211Biosynthetic pathway of indole-3-acetic acid in ectomycorrhizal fungi collected from northern Thailand.
Auteurs : Jaturong Kumla ; Nakarin Suwannarach ; Kenji Matsui ; Saisamorn LumyongSource :
- PloS one [ 1932-6203 ] ; 2020.
English descriptors
- KwdEn :
- Basidiomycota (metabolism), Chromatography, High Pressure Liquid (MeSH), Colorimetry (MeSH), Fungal Proteins (metabolism), Indoleacetic Acids (analysis), Indoleacetic Acids (metabolism), Mycorrhizae (metabolism), Plant Growth Regulators (analysis), Plant Growth Regulators (metabolism), Tryptophan (metabolism), Tryptophan Transaminase (metabolism).
- MESH :
- chemical , analysis : Indoleacetic Acids, Plant Growth Regulators.
- chemical , metabolism : Fungal Proteins, Indoleacetic Acids, Plant Growth Regulators, Tryptophan, Tryptophan Transaminase.
- metabolism : Basidiomycota, Mycorrhizae.
- Chromatography, High Pressure Liquid, Colorimetry.
Abstract
Indole-3-acetic acid (IAA) is an imperative phytohormone for plant growth and development. Ectomycorrhizal fungi (ECM) are able to produce IAA. However, only a few studies on IAA biosynthesis pathways in ECM fungi have been reported. This study aimed to investigate the IAA biosynthesis pathway of six ECM cultures including Astraeus odoratus, Gyrodon suthepensis, Phlebopus portentosus, Pisolithus albus, Pisolithus orientalis and Scleroderma suthepense. The results showed that all ECM fungi produced IAA in liquid medium that had been supplemented with L-tryptophan. Notably, fungal IAA levels vary for different fungal species. The detection of indole-3-lactic acid and indole-3-ethanol in the crude culture extracts of all ECM fungi indicated an enzymatic reduction of indole-3-pyruvic acid and indole-3-acetaldehyde, respectively in the IAA biosynthesis via the indole-3-pyruvic acid pathway. Moreover, the tryptophan aminotransferase activity confirmed that all ECM fungi synthesize IAA through the indole-3-pyruvic acid pathway. Additionally, the elongation of rice and oat coleoptiles was stimulated by crude culture extract. This is the first report of the biosynthesis pathway of IAA in the tested ECM fungi.
DOI: 10.1371/journal.pone.0227478
PubMed: 31899917
PubMed Central: PMC6941825
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pubmed:31899917Le document en format XML
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Excellence in Microbial Diversity and Sustainable Utilization, Chiang Mai University, Chiang Mai Thailand.</nlm:affiliation></affiliation></author><author><name sortKey="Matsui, Kenji" sort="Matsui, Kenji" uniqKey="Matsui K" first="Kenji" last="Matsui">Kenji Matsui</name><affiliation><nlm:affiliation>Graduate School of Sciences and Technology for Innovation, Faculty of Agriculture, Yamaguchi University, Yamaguchi, 7 Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Lumyong, Saisamorn" sort="Lumyong, Saisamorn" uniqKey="Lumyong S" first="Saisamorn" last="Lumyong">Saisamorn Lumyong</name><affiliation><nlm:affiliation>Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center of Excellence in Microbial Diversity and Sustainable Utilization, Chiang Mai University, Chiang Mai Thailand.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Academy of Science, The Royal 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Excellence in Microbial Diversity and Sustainable Utilization, Chiang Mai University, Chiang Mai Thailand.</nlm:affiliation></affiliation></author><author><name sortKey="Suwannarach, Nakarin" sort="Suwannarach, Nakarin" uniqKey="Suwannarach N" first="Nakarin" last="Suwannarach">Nakarin Suwannarach</name><affiliation><nlm:affiliation>Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center of Excellence in Microbial Diversity and Sustainable Utilization, Chiang Mai University, Chiang Mai Thailand.</nlm:affiliation></affiliation></author><author><name sortKey="Matsui, Kenji" sort="Matsui, Kenji" uniqKey="Matsui K" first="Kenji" last="Matsui">Kenji Matsui</name><affiliation><nlm:affiliation>Graduate School of Sciences and Technology for Innovation, Faculty of Agriculture, Yamaguchi University, Yamaguchi, 7 Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Lumyong, Saisamorn" sort="Lumyong, Saisamorn" uniqKey="Lumyong S" first="Saisamorn" last="Lumyong">Saisamorn Lumyong</name><affiliation><nlm:affiliation>Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Center of Excellence in Microbial Diversity and Sustainable Utilization, Chiang Mai University, Chiang Mai Thailand.</nlm:affiliation></affiliation><affiliation><nlm:affiliation>Academy of Science, The Royal Society of Thailand, Bangkok, Thailand.</nlm:affiliation></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (metabolism)</term><term>Chromatography, High Pressure Liquid (MeSH)</term><term>Colorimetry (MeSH)</term><term>Fungal Proteins (metabolism)</term><term>Indoleacetic Acids (analysis)</term><term>Indoleacetic Acids (metabolism)</term><term>Mycorrhizae (metabolism)</term><term>Plant Growth Regulators (analysis)</term><term>Plant Growth Regulators (metabolism)</term><term>Tryptophan (metabolism)</term><term>Tryptophan Transaminase (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Indoleacetic Acids</term><term>Plant Growth Regulators</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fungal Proteins</term><term>Indoleacetic Acids</term><term>Plant Growth Regulators</term><term>Tryptophan</term><term>Tryptophan Transaminase</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Basidiomycota</term><term>Mycorrhizae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Chromatography, High Pressure Liquid</term><term>Colorimetry</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Indole-3-acetic acid (IAA) is an imperative phytohormone for plant growth and development. Ectomycorrhizal fungi (ECM) are able to produce IAA. However, only a few studies on IAA biosynthesis pathways in ECM fungi have been reported. This study aimed to investigate the IAA biosynthesis pathway of six ECM cultures including Astraeus odoratus, Gyrodon suthepensis, Phlebopus portentosus, Pisolithus albus, Pisolithus orientalis and Scleroderma suthepense. The results showed that all ECM fungi produced IAA in liquid medium that had been supplemented with L-tryptophan. Notably, fungal IAA levels vary for different fungal species. The detection of indole-3-lactic acid and indole-3-ethanol in the crude culture extracts of all ECM fungi indicated an enzymatic reduction of indole-3-pyruvic acid and indole-3-acetaldehyde, respectively in the IAA biosynthesis via the indole-3-pyruvic acid pathway. Moreover, the tryptophan aminotransferase activity confirmed that all ECM fungi synthesize IAA through the indole-3-pyruvic acid pathway. Additionally, the elongation of rice and oat coleoptiles was stimulated by crude culture extract. This is the first report of the biosynthesis pathway of IAA in the tested ECM fungi.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">31899917</PMID><DateCompleted><Year>2020</Year><Month>04</Month><Day>13</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>13</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>15</Volume><Issue>1</Issue><PubDate><Year>2020</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS One</ISOAbbreviation></Journal><ArticleTitle>Biosynthetic pathway of indole-3-acetic acid in ectomycorrhizal fungi collected from northern Thailand.</ArticleTitle><Pagination><MedlinePgn>e0227478</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0227478</ELocationID><Abstract><AbstractText>Indole-3-acetic acid (IAA) is an imperative phytohormone for plant growth and development. Ectomycorrhizal fungi (ECM) are able to produce IAA. However, only a few studies on IAA biosynthesis pathways in ECM fungi have been reported. This study aimed to investigate the IAA biosynthesis pathway of six ECM cultures including Astraeus odoratus, Gyrodon suthepensis, Phlebopus portentosus, Pisolithus albus, Pisolithus orientalis and Scleroderma suthepense. The results showed that all ECM fungi produced IAA in liquid medium that had been supplemented with L-tryptophan. Notably, fungal IAA levels vary for different fungal species. The detection of indole-3-lactic acid and indole-3-ethanol in the crude culture extracts of all ECM fungi indicated an enzymatic reduction of indole-3-pyruvic acid and indole-3-acetaldehyde, respectively in the IAA biosynthesis via the indole-3-pyruvic acid pathway. Moreover, the tryptophan aminotransferase activity confirmed that all ECM fungi synthesize IAA through the indole-3-pyruvic acid pathway. Additionally, the elongation of rice and oat coleoptiles was stimulated by crude culture extract. This is the first report of the biosynthesis pathway of IAA in the tested ECM fungi.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kumla</LastName><ForeName>Jaturong</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center of Excellence in Microbial Diversity and Sustainable Utilization, Chiang Mai University, Chiang Mai Thailand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Suwannarach</LastName><ForeName>Nakarin</ForeName><Initials>N</Initials><Identifier Source="ORCID">0000-0002-2653-1913</Identifier><AffiliationInfo><Affiliation>Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center of Excellence in Microbial Diversity and Sustainable Utilization, Chiang Mai University, Chiang Mai Thailand.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Matsui</LastName><ForeName>Kenji</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Graduate School of Sciences and Technology for Innovation, Faculty of Agriculture, Yamaguchi University, Yamaguchi, 7 Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lumyong</LastName><ForeName>Saisamorn</ForeName><Initials>S</Initials><Identifier Source="ORCID">0000-0002-6485-414X</Identifier><AffiliationInfo><Affiliation>Department of Biology, Faculty of Science, Chiang Mai University, Chiang Mai, Thailand.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Center of Excellence in Microbial Diversity and Sustainable Utilization, Chiang Mai University, Chiang Mai Thailand.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Academy of Science, The Royal Society of Thailand, Bangkok, Thailand.</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>2020</Year><Month>01</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007210">Indoleacetic Acids</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010937">Plant Growth Regulators</NameOfSubstance></Chemical><Chemical><RegistryNumber>6U1S09C61L</RegistryNumber><NameOfSubstance UI="C030737">indoleacetic acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>8DUH1N11BX</RegistryNumber><NameOfSubstance UI="D014364">Tryptophan</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.6.1.27</RegistryNumber><NameOfSubstance UI="D051279">Tryptophan Transaminase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001487" MajorTopicYN="N">Basidiomycota</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003124" MajorTopicYN="N">Colorimetry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007210" MajorTopicYN="N">Indoleacetic Acids</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D038821" MajorTopicYN="N">Mycorrhizae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010937" MajorTopicYN="N">Plant Growth Regulators</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014364" MajorTopicYN="N">Tryptophan</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051279" MajorTopicYN="N">Tryptophan Transaminase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><CoiStatement>The authors have declared that no competing interests exist.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>05</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2019</Year><Month>12</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>1</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>1</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>4</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">31899917</ArticleId><ArticleId 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