ATP-dependent but proton gradient-independent polyphosphate-synthesizing activity in extraradical hyphae of an arbuscular mycorrhizal fungus.
Identifieur interne : 002851 ( Main/Corpus ); précédent : 002850; suivant : 002852ATP-dependent but proton gradient-independent polyphosphate-synthesizing activity in extraradical hyphae of an arbuscular mycorrhizal fungus.
Auteurs : Chiharu Tani ; Ryo Ohtomo ; Mitsuru Osaki ; Yukari Kuga ; Tatsuhiro EzawaSource :
- Applied and environmental microbiology [ 1098-5336 ] ; 2009.
English descriptors
- KwdEn :
- Acid Anhydride Hydrolases (metabolism), Adenosine Triphosphatases (metabolism), Adenosine Triphosphate (metabolism), Enzyme Activation (drug effects), Enzyme Inhibitors (pharmacology), Glomeromycota (enzymology), Glomeromycota (ultrastructure), Hyphae (enzymology), Hyphae (ultrastructure), Macrolides (pharmacology), Mycorrhizae (enzymology), Mycorrhizae (ultrastructure), Polyphosphates (metabolism), Protons (MeSH), Vanadates (pharmacology).
- MESH :
- chemical , metabolism : Acid Anhydride Hydrolases, Adenosine Triphosphatases, Adenosine Triphosphate, Polyphosphates.
- drug effects : Enzyme Activation.
- enzymology : Glomeromycota, Hyphae, Mycorrhizae.
- chemical , pharmacology : Enzyme Inhibitors, Macrolides, Vanadates.
- ultrastructure : Glomeromycota, Hyphae, Mycorrhizae.
- chemical : Protons.
Abstract
Arbuscular mycorrhizal (AM) fungi benefit their host plants by supplying phosphate obtained from the soil. Polyphosphate is thought to act as the key intermediate in this process, but little is currently understood about how polyphosphate is synthesized or translocated within arbuscular mycorrhizas. Glomus sp. strain HR1 was grown with marigold in a mesh bag compartment system, and extraradical hyphae were harvested and fractionated by density gradient centrifugation. Using this approach, three distinct layers were obtained: layers 1 and 2 were composed of amorphous and membranous materials, together with mitochondria, lipid bodies, and electron-opaque bodies, and layer 3 was composed mainly of partially broken hyphae and fragmented cell walls. The polyphosphate kinase/luciferase system, a highly sensitive polyphosphate detection method, enabled the detection of polyphosphate-synthesizing activity in layer 2 in the presence of ATP. This activity was inhibited by vanadate but not by bafilomycin A(1) or a protonophore, suggesting that ATP may not energize the reaction through H(+)-ATPase but may act as a direct substrate in the reaction. This report represents the first demonstration that AM fungi possess polyphosphate-synthesizing activity that is localized in the organelle fraction and not in the cytosol or at the plasma membrane.
DOI: 10.1128/AEM.01519-09
PubMed: 19767467
PubMed Central: PMC2786526
Links to Exploration step
pubmed:19767467Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">ATP-dependent but proton gradient-independent polyphosphate-synthesizing activity in extraradical hyphae of an arbuscular mycorrhizal fungus.</title><author><name sortKey="Tani, Chiharu" sort="Tani, Chiharu" uniqKey="Tani C" first="Chiharu" last="Tani">Chiharu Tani</name><affiliation><nlm:affiliation>Hokkaido University, Sapporo, Hokkaido 060-8589, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Ohtomo, Ryo" sort="Ohtomo, Ryo" uniqKey="Ohtomo R" first="Ryo" last="Ohtomo">Ryo Ohtomo</name></author><author><name sortKey="Osaki, Mitsuru" sort="Osaki, Mitsuru" uniqKey="Osaki M" first="Mitsuru" last="Osaki">Mitsuru Osaki</name></author><author><name sortKey="Kuga, Yukari" sort="Kuga, Yukari" uniqKey="Kuga Y" first="Yukari" last="Kuga">Yukari Kuga</name></author><author><name sortKey="Ezawa, Tatsuhiro" sort="Ezawa, Tatsuhiro" uniqKey="Ezawa T" first="Tatsuhiro" last="Ezawa">Tatsuhiro Ezawa</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19767467</idno><idno type="pmid">19767467</idno><idno type="doi">10.1128/AEM.01519-09</idno><idno type="pmc">PMC2786526</idno><idno type="wicri:Area/Main/Corpus">002851</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002851</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">ATP-dependent but proton gradient-independent polyphosphate-synthesizing activity in extraradical hyphae of an arbuscular mycorrhizal fungus.</title><author><name sortKey="Tani, Chiharu" sort="Tani, Chiharu" uniqKey="Tani C" first="Chiharu" last="Tani">Chiharu Tani</name><affiliation><nlm:affiliation>Hokkaido University, Sapporo, Hokkaido 060-8589, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Ohtomo, Ryo" sort="Ohtomo, Ryo" uniqKey="Ohtomo R" first="Ryo" last="Ohtomo">Ryo Ohtomo</name></author><author><name sortKey="Osaki, Mitsuru" sort="Osaki, Mitsuru" uniqKey="Osaki M" first="Mitsuru" last="Osaki">Mitsuru Osaki</name></author><author><name sortKey="Kuga, Yukari" sort="Kuga, Yukari" uniqKey="Kuga Y" first="Yukari" last="Kuga">Yukari Kuga</name></author><author><name sortKey="Ezawa, Tatsuhiro" sort="Ezawa, Tatsuhiro" uniqKey="Ezawa T" first="Tatsuhiro" last="Ezawa">Tatsuhiro Ezawa</name></author></analytic><series><title level="j">Applied and environmental microbiology</title><idno type="eISSN">1098-5336</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Acid Anhydride Hydrolases (metabolism)</term><term>Adenosine Triphosphatases (metabolism)</term><term>Adenosine Triphosphate (metabolism)</term><term>Enzyme Activation (drug effects)</term><term>Enzyme Inhibitors (pharmacology)</term><term>Glomeromycota (enzymology)</term><term>Glomeromycota (ultrastructure)</term><term>Hyphae (enzymology)</term><term>Hyphae (ultrastructure)</term><term>Macrolides (pharmacology)</term><term>Mycorrhizae (enzymology)</term><term>Mycorrhizae (ultrastructure)</term><term>Polyphosphates (metabolism)</term><term>Protons (MeSH)</term><term>Vanadates (pharmacology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Acid Anhydride Hydrolases</term><term>Adenosine Triphosphatases</term><term>Adenosine Triphosphate</term><term>Polyphosphates</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Enzyme Activation</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Glomeromycota</term><term>Hyphae</term><term>Mycorrhizae</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Enzyme Inhibitors</term><term>Macrolides</term><term>Vanadates</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Glomeromycota</term><term>Hyphae</term><term>Mycorrhizae</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Protons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Arbuscular mycorrhizal (AM) fungi benefit their host plants by supplying phosphate obtained from the soil. Polyphosphate is thought to act as the key intermediate in this process, but little is currently understood about how polyphosphate is synthesized or translocated within arbuscular mycorrhizas. Glomus sp. strain HR1 was grown with marigold in a mesh bag compartment system, and extraradical hyphae were harvested and fractionated by density gradient centrifugation. Using this approach, three distinct layers were obtained: layers 1 and 2 were composed of amorphous and membranous materials, together with mitochondria, lipid bodies, and electron-opaque bodies, and layer 3 was composed mainly of partially broken hyphae and fragmented cell walls. The polyphosphate kinase/luciferase system, a highly sensitive polyphosphate detection method, enabled the detection of polyphosphate-synthesizing activity in layer 2 in the presence of ATP. This activity was inhibited by vanadate but not by bafilomycin A(1) or a protonophore, suggesting that ATP may not energize the reaction through H(+)-ATPase but may act as a direct substrate in the reaction. This report represents the first demonstration that AM fungi possess polyphosphate-synthesizing activity that is localized in the organelle fraction and not in the cytosol or at the plasma membrane.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19767467</PMID><DateCompleted><Year>2010</Year><Month>03</Month><Day>25</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5336</ISSN><JournalIssue CitedMedium="Internet"><Volume>75</Volume><Issue>22</Issue><PubDate><Year>2009</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Applied and environmental microbiology</Title><ISOAbbreviation>Appl Environ Microbiol</ISOAbbreviation></Journal><ArticleTitle>ATP-dependent but proton gradient-independent polyphosphate-synthesizing activity in extraradical hyphae of an arbuscular mycorrhizal fungus.</ArticleTitle><Pagination><MedlinePgn>7044-50</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/AEM.01519-09</ELocationID><Abstract><AbstractText>Arbuscular mycorrhizal (AM) fungi benefit their host plants by supplying phosphate obtained from the soil. Polyphosphate is thought to act as the key intermediate in this process, but little is currently understood about how polyphosphate is synthesized or translocated within arbuscular mycorrhizas. Glomus sp. strain HR1 was grown with marigold in a mesh bag compartment system, and extraradical hyphae were harvested and fractionated by density gradient centrifugation. Using this approach, three distinct layers were obtained: layers 1 and 2 were composed of amorphous and membranous materials, together with mitochondria, lipid bodies, and electron-opaque bodies, and layer 3 was composed mainly of partially broken hyphae and fragmented cell walls. The polyphosphate kinase/luciferase system, a highly sensitive polyphosphate detection method, enabled the detection of polyphosphate-synthesizing activity in layer 2 in the presence of ATP. This activity was inhibited by vanadate but not by bafilomycin A(1) or a protonophore, suggesting that ATP may not energize the reaction through H(+)-ATPase but may act as a direct substrate in the reaction. This report represents the first demonstration that AM fungi possess polyphosphate-synthesizing activity that is localized in the organelle fraction and not in the cytosol or at the plasma membrane.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tani</LastName><ForeName>Chiharu</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Hokkaido University, Sapporo, Hokkaido 060-8589, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ohtomo</LastName><ForeName>Ryo</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Osaki</LastName><ForeName>Mitsuru</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Kuga</LastName><ForeName>Yukari</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Ezawa</LastName><ForeName>Tatsuhiro</ForeName><Initials>T</Initials></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>2009</Year><Month>09</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Appl Environ Microbiol</MedlineTA><NlmUniqueID>7605801</NlmUniqueID><ISSNLinking>0099-2240</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D018942">Macrolides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011122">Polyphosphates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011522">Protons</NameOfSubstance></Chemical><Chemical><RegistryNumber>3WHH0066W5</RegistryNumber><NameOfSubstance UI="D014638">Vanadates</NameOfSubstance></Chemical><Chemical><RegistryNumber>88899-55-2</RegistryNumber><NameOfSubstance UI="C040929">bafilomycin A1</NameOfSubstance></Chemical><Chemical><RegistryNumber>8L70Q75FXE</RegistryNumber><NameOfSubstance UI="D000255">Adenosine Triphosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.-</RegistryNumber><NameOfSubstance UI="D017766">Acid Anhydride Hydrolases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D000251">Adenosine Triphosphatases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.10</RegistryNumber><NameOfSubstance UI="C022563">endopolyphosphatase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017766" MajorTopicYN="N">Acid Anhydride Hydrolases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000251" MajorTopicYN="N">Adenosine Triphosphatases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000255" MajorTopicYN="N">Adenosine Triphosphate</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055137" MajorTopicYN="N">Glomeromycota</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D025301" 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