Lipases and the biosynthesis of free oxylipins in plants.
Identifieur interne : 001060 ( Main/Exploration ); précédent : 001059; suivant : 001061Lipases and the biosynthesis of free oxylipins in plants.
Auteurs : Gustavo Bonaventure [Belgique]Source :
- Plant signaling & behavior [ 1559-2324 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Chloroplastes, Lipoxygénases, Oxylipines, Plantes, Triacylglycerol lipase.
- Modèles biologiques, Métabolisme lipidique.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Lipase, Lipoxygenases, Oxylipins.
- metabolism : Chloroplasts, Plants.
- Lipid Metabolism, Models, Biological.
Abstract
The production of free oxylipins in plants is exquisitely controlled by cellular mechanisms that respond to environmental factors such as mechanical damage, insect herbivory and pathogen infection. One of the main targets of these cellular mechanisms are glycerolipases class A (GLA); acyl-hydrolyzing enzymes that upon their biochemical activation release unsaturated fatty acids or acylated oxylipins from glycerolipids. Recent studies performed in the wild tobacco species Nicotiana attenuata have started to reveal the complexity and specificity of GLA-regulated free oxylipin production. I present a model in which individual GLA lipases associate with individual lipoxygenases (LOX) in chloroplast membranes and envelope to define the initial committed steps of distinct oxylipin biosynthesis pathways. The unravelling of the mechanisms that activate GLAs and LOXs at the biochemical level and that control the interaction between these enzymes and their association with membranes will prove to be fundamental to understand how plants control free oxylipin biogenesis.
DOI: 10.4161/psb.28429
PubMed: 24603593
PubMed Central: PMC4091546
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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One of the main targets of these cellular mechanisms are glycerolipases class A (GLA); acyl-hydrolyzing enzymes that upon their biochemical activation release unsaturated fatty acids or acylated oxylipins from glycerolipids. Recent studies performed in the wild tobacco species Nicotiana attenuata have started to reveal the complexity and specificity of GLA-regulated free oxylipin production. I present a model in which individual GLA lipases associate with individual lipoxygenases (LOX) in chloroplast membranes and envelope to define the initial committed steps of distinct oxylipin biosynthesis pathways. The unravelling of the mechanisms that activate GLAs and LOXs at the biochemical level and that control the interaction between these enzymes and their association with membranes will prove to be fundamental to understand how plants control free oxylipin biogenesis. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24603593</PMID><DateCompleted><Year>2015</Year><Month>04</Month><Day>21</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1559-2324</ISSN><JournalIssue CitedMedium="Internet"><Volume>9</Volume><Issue>3</Issue><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>Plant signaling & behavior</Title><ISOAbbreviation>Plant Signal Behav</ISOAbbreviation></Journal><ArticleTitle>Lipases and the biosynthesis of free oxylipins in plants.</ArticleTitle><Pagination><MedlinePgn>e28429</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">28429</ELocationID><Abstract><AbstractText>The production of free oxylipins in plants is exquisitely controlled by cellular mechanisms that respond to environmental factors such as mechanical damage, insect herbivory and pathogen infection. One of the main targets of these cellular mechanisms are glycerolipases class A (GLA); acyl-hydrolyzing enzymes that upon their biochemical activation release unsaturated fatty acids or acylated oxylipins from glycerolipids. Recent studies performed in the wild tobacco species Nicotiana attenuata have started to reveal the complexity and specificity of GLA-regulated free oxylipin production. I present a model in which individual GLA lipases associate with individual lipoxygenases (LOX) in chloroplast membranes and envelope to define the initial committed steps of distinct oxylipin biosynthesis pathways. The unravelling of the mechanisms that activate GLAs and LOXs at the biochemical level and that control the interaction between these enzymes and their association with membranes will prove to be fundamental to understand how plants control free oxylipin biogenesis. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Bonaventure</LastName><ForeName>Gustavo</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>BASF Plant Sciences; Ghent, Belgium.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>01</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant Signal 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MajorTopicYN="N">lipoxygenase</Keyword><Keyword MajorTopicYN="N">oxylipin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>3</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>3</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>4</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24603593</ArticleId><ArticleId IdType="pii">28429</ArticleId><ArticleId IdType="pmc">PMC4091546</ArticleId><ArticleId IdType="doi">10.4161/psb.28429</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Dev Cell. 2008 Feb;14(2):183-92</Citation><ArticleIdList><ArticleId IdType="pubmed">18267087</ArticleId></ArticleIdList></Reference><Reference><Citation>Planta. 2007 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