Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/176304
COMPARTIR / EXPORTAR:
SHARE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | New Insights Into Sunflower (Helianthus annuus L.) FatA and FatB Thioesterases, Their Regulation, Structure and Distribution |
Autor: | Aznar-Moreno, José A. CSIC ORCID ; Sánchez, Rosario CSIC ORCID ; Gidda, Satinder K.; Martínez-Force, Enrique CSIC ORCID ; Moreno-Pérez, Antonio J. CSIC ORCID ; Venegas-Calerón, Mónica CSIC ORCID ; Garcés Mancheño, Rafael CSIC ORCID ; Mullen, Robert T.; Salas, Joaquín J. CSIC ORCID | Palabras clave: | Sunflower Helianthus annuus Acyl-ACP thioesterases Protein location FatA FatB |
Fecha de publicación: | 16-oct-2018 | Editor: | Frontiers Media | Citación: | Frontiers in Plant Science 9: 1496 (2018) | Resumen: | Sunflower seeds (Helianthus annuus L.) accumulate large quantities of triacylglycerols (TAG) between 12 and 28 days after flowering (DAF). This is the period of maximal acyl-acyl carrier protein (acyl-ACP) thioesterase activity in vitro, the enzymes that terminate the process of de novo fatty acid synthesis by catalyzing the hydrolysis of the acyl-ACPs synthesized by fatty acid synthase. Fatty acid thioesterases can be classified into two families with distinct substrate specificities, namely FatA and FatB. Here, some new aspects of these enzymes have been studied, assessing how both enzymes contribute to the acyl composition of sunflower oil, not least through the changes in their expression during the process of seed filling. Moreover, the binding pockets of these enzymes were modeled based on new data from plant thioesterases, revealing important differences in their volume and geometry. Finally, the subcellular location of the two enzymes was evaluated and while both possess an N-terminal plastid transit peptide, only in FatB contains a hydrophobic sequence that could potentially serve as a transmembrane domain. Indeed, using in vivo imaging and organelle fractionation, H. annuus thioesterases, HaFatA and HaFatB, appear to be differentially localized in the plastid stroma and membrane envelope, respectively. The divergent roles fulfilled by HaFatA and HaFatB in oil biosynthesis are discussed in the light of our data. | Descripción: | 15 Páginas.-- 10 Figuras.-- 1 Tabla | Versión del editor: | http://dx.doi.org/10.3389/fpls.2018.01496 | URI: | http://hdl.handle.net/10261/176304 | E-ISSN: | 1664-462X |
Aparece en las colecciones: | (IG) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
FrontiersPlanSci_2018_New_Insights.pdf | Artículo principal | 5,86 MB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
Page view(s)
298
checked on 29-mar-2024
Download(s)
283
checked on 29-mar-2024
Google ScholarTM
Check
Este item está licenciado bajo una Licencia Creative Commons