Evolution of the isoprene biosynthetic pathway in kudzu.
Identifieur interne : 004040 ( Main/Exploration ); précédent : 004039; suivant : 004041Evolution of the isoprene biosynthetic pathway in kudzu.
Auteurs : Thomas D. Sharkey [États-Unis] ; Sansun Yeh ; Amy E. Wiberley ; Tanya G. Falbel ; Deming Gong ; Donna E. FernandezSource :
- Plant physiology [ 0032-0889 ] ; 2005.
Descripteurs français
- KwdFr :
- Alkyl et aryl transferases (composition chimique), Alkyl et aryl transferases (génétique), Alkyl et aryl transferases (métabolisme), Arabidopsis (enzymologie), Arabidopsis (génétique), Butadiènes (MeSH), Cartographie chromosomique (MeSH), Données de séquences moléculaires (MeSH), Hémiterpènes (biosynthèse), Oses phosphates (métabolisme), Pentanes (MeSH), Phylogenèse (MeSH), Phénotype (MeSH), Populus (enzymologie), Pueraria (enzymologie), Pueraria (génétique), Similitude de séquences d'acides aminés (MeSH), Sites de fixation (MeSH), Érythritol (analogues et dérivés), Érythritol (métabolisme), Évolution moléculaire (MeSH).
- MESH :
- analogues et dérivés : Érythritol.
- biosynthèse : Hémiterpènes.
- composition chimique : Alkyl et aryl transferases.
- enzymologie : Arabidopsis, Populus, Pueraria.
- génétique : Alkyl et aryl transferases, Arabidopsis, Pueraria.
- métabolisme : Alkyl et aryl transferases, Oses phosphates, Érythritol.
- Butadiènes, Cartographie chromosomique, Données de séquences moléculaires, Pentanes, Phylogenèse, Phénotype, Similitude de séquences d'acides aminés, Sites de fixation, Évolution moléculaire.
English descriptors
- KwdEn :
- Alkyl and Aryl Transferases (chemistry), Alkyl and Aryl Transferases (genetics), Alkyl and Aryl Transferases (metabolism), Arabidopsis (enzymology), Arabidopsis (genetics), Binding Sites (MeSH), Butadienes (MeSH), Chromosome Mapping (MeSH), Erythritol (analogs & derivatives), Erythritol (metabolism), Evolution, Molecular (MeSH), Hemiterpenes (biosynthesis), Molecular Sequence Data (MeSH), Pentanes (MeSH), Phenotype (MeSH), Phylogeny (MeSH), Populus (enzymology), Pueraria (enzymology), Pueraria (genetics), Sequence Homology, Amino Acid (MeSH), Sugar Phosphates (metabolism).
- MESH :
- chemical , analogs & derivatives : Erythritol.
- chemical , biosynthesis : Hemiterpenes.
- chemical , chemistry : Alkyl and Aryl Transferases.
- chemical , genetics : Alkyl and Aryl Transferases.
- chemical , metabolism : Alkyl and Aryl Transferases, Erythritol, Sugar Phosphates.
- enzymology : Arabidopsis, Populus, Pueraria.
- genetics : Arabidopsis, Pueraria.
- Binding Sites, Butadienes, Chromosome Mapping, Evolution, Molecular, Molecular Sequence Data, Pentanes, Phenotype, Phylogeny, Sequence Homology, Amino Acid.
Abstract
Isoprene synthase converts dimethylallyl diphosphate, derived from the methylerythritol 4-phosphate (MEP) pathway, to isoprene. Isoprene is made by some plants in substantial amounts, which affects atmospheric chemistry, while other plants make no isoprene. As part of our long-term study of isoprene synthesis, the genetics of the isoprene biosynthetic pathway of the isoprene emitter, kudzu (Pueraria montana), was compared with similar genes in Arabidopsis (Arabidopsis thaliana), which does not make isoprene. The MEP pathway genes in kudzu were similar to the corresponding Arabidopsis genes. Isoprene synthase genes of kudzu and aspen (Populus tremuloides) were cloned to compare their divergence with the divergence seen in MEP pathway genes. Phylogenetic analysis of the terpene synthase gene family indicated that isoprene synthases are either within the monoterpene synthase clade or sister to it. In Arabidopsis, the gene most similar to isoprene synthase is a myrcene/ocimene (acyclic monoterpenes) synthase. Two phenylalanine residues found exclusively in isoprene synthases make the active site smaller than other terpene synthase enzymes, possibly conferring specificity for the five-carbon substrate rather than precursors of the larger isoprenoids. Expression of the kudzu isoprene synthase gene in Arabidopsis caused Arabidopsis to emit isoprene, indicating that whether or not a plant emits isoprene depends on whether or not it has a terpene synthase capable of using dimethylallyl diphosphate.
DOI: 10.1104/pp.104.054445
PubMed: 15653811
PubMed Central: PMC1065370
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Isoprene is made by some plants in substantial amounts, which affects atmospheric chemistry, while other plants make no isoprene. As part of our long-term study of isoprene synthesis, the genetics of the isoprene biosynthetic pathway of the isoprene emitter, kudzu (Pueraria montana), was compared with similar genes in Arabidopsis (Arabidopsis thaliana), which does not make isoprene. The MEP pathway genes in kudzu were similar to the corresponding Arabidopsis genes. Isoprene synthase genes of kudzu and aspen (Populus tremuloides) were cloned to compare their divergence with the divergence seen in MEP pathway genes. Phylogenetic analysis of the terpene synthase gene family indicated that isoprene synthases are either within the monoterpene synthase clade or sister to it. In Arabidopsis, the gene most similar to isoprene synthase is a myrcene/ocimene (acyclic monoterpenes) synthase. Two phenylalanine residues found exclusively in isoprene synthases make the active site smaller than other terpene synthase enzymes, possibly conferring specificity for the five-carbon substrate rather than precursors of the larger isoprenoids. Expression of the kudzu isoprene synthase gene in Arabidopsis caused Arabidopsis to emit isoprene, indicating that whether or not a plant emits isoprene depends on whether or not it has a terpene synthase capable of using dimethylallyl diphosphate.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15653811</PMID><DateCompleted><Year>2005</Year><Month>05</Month><Day>31</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0032-0889</ISSN><JournalIssue CitedMedium="Print"><Volume>137</Volume><Issue>2</Issue><PubDate><Year>2005</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Evolution of the isoprene biosynthetic pathway in kudzu.</ArticleTitle><Pagination><MedlinePgn>700-12</MedlinePgn></Pagination><Abstract><AbstractText>Isoprene synthase converts dimethylallyl diphosphate, derived from the methylerythritol 4-phosphate (MEP) pathway, to isoprene. Isoprene is made by some plants in substantial amounts, which affects atmospheric chemistry, while other plants make no isoprene. As part of our long-term study of isoprene synthesis, the genetics of the isoprene biosynthetic pathway of the isoprene emitter, kudzu (Pueraria montana), was compared with similar genes in Arabidopsis (Arabidopsis thaliana), which does not make isoprene. The MEP pathway genes in kudzu were similar to the corresponding Arabidopsis genes. Isoprene synthase genes of kudzu and aspen (Populus tremuloides) were cloned to compare their divergence with the divergence seen in MEP pathway genes. Phylogenetic analysis of the terpene synthase gene family indicated that isoprene synthases are either within the monoterpene synthase clade or sister to it. In Arabidopsis, the gene most similar to isoprene synthase is a myrcene/ocimene (acyclic monoterpenes) synthase. Two phenylalanine residues found exclusively in isoprene synthases make the active site smaller than other terpene synthase enzymes, possibly conferring specificity for the five-carbon substrate rather than precursors of the larger isoprenoids. Expression of the kudzu isoprene synthase gene in Arabidopsis caused Arabidopsis to emit isoprene, indicating that whether or not a plant emits isoprene depends on whether or not it has a terpene synthase capable of using dimethylallyl diphosphate.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sharkey</LastName><ForeName>Thomas D</ForeName><Initials>TD</Initials><AffiliationInfo><Affiliation>Department of Botany, University of Wisconsin, Madison, Wisconsin 53706, USA. tsharkey@wisc.edu</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yeh</LastName><ForeName>Sansun</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Wiberley</LastName><ForeName>Amy E</ForeName><Initials>AE</Initials></Author><Author ValidYN="Y"><LastName>Falbel</LastName><ForeName>Tanya G</ForeName><Initials>TG</Initials></Author><Author ValidYN="Y"><LastName>Gong</LastName><ForeName>Deming</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Fernandez</LastName><ForeName>Donna E</ForeName><Initials>DE</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>GENBANK</DataBankName><AccessionNumberList><AccessionNumber>AY315650</AccessionNumber><AccessionNumber>AY315651</AccessionNumber><AccessionNumber>AY315652</AccessionNumber><AccessionNumber>AY316691</AccessionNumber><AccessionNumber>AY341431</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2005</Year><Month>01</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Physiol</MedlineTA><NlmUniqueID>0401224</NlmUniqueID><ISSNLinking>0032-0889</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C114232">2-C-methylerythritol 4-phosphate</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D002070">Butadienes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D045782">Hemiterpenes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010420">Pentanes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013403">Sugar Phosphates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0A62964IBU</RegistryNumber><NameOfSubstance UI="C005059">isoprene</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.-</RegistryNumber><NameOfSubstance UI="D019883">Alkyl and Aryl Transferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.-</RegistryNumber><NameOfSubstance UI="C093854">isoprene synthase</NameOfSubstance></Chemical><Chemical><RegistryNumber>RA96B954X6</RegistryNumber><NameOfSubstance UI="D004896">Erythritol</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019883" MajorTopicYN="N">Alkyl and Aryl Transferases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002070" MajorTopicYN="N">Butadienes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002874" MajorTopicYN="N">Chromosome Mapping</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004896" MajorTopicYN="N">Erythritol</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="Y">analogs & derivatives</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019143" MajorTopicYN="N">Evolution, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045782" MajorTopicYN="N">Hemiterpenes</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010420" MajorTopicYN="N">Pentanes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010641" MajorTopicYN="N">Phenotype</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D032107" MajorTopicYN="N">Populus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029908" MajorTopicYN="N">Pueraria</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017386" MajorTopicYN="N">Sequence Homology, Amino Acid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013403" MajorTopicYN="N">Sugar Phosphates</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>1</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>6</Month><Day>1</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>1</Month><Day>18</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15653811</ArticleId><ArticleId IdType="pii">pp.104.054445</ArticleId><ArticleId IdType="doi">10.1104/pp.104.054445</ArticleId><ArticleId IdType="pmc">PMC1065370</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Mol Biol Evol. 1999 Feb;16(2):266-74</Citation><ArticleIdList><ArticleId IdType="pubmed">10028292</ArticleId></ArticleIdList></Reference><Reference><Citation>Plant J. 1998 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sortKey="Falbel, Tanya G" sort="Falbel, Tanya G" uniqKey="Falbel T" first="Tanya G" last="Falbel">Tanya G. 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