Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/176304
COMPARTIR / EXPORTAR:
logo share SHARE BASE
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE

Invitar a revisión por pares abierta
Título

New Insights Into Sunflower (Helianthus annuus L.) FatA and FatB Thioesterases, Their Regulation, Structure and Distribution

AutorAznar-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 claveSunflower
Helianthus annuus
Acyl-ACP thioesterases
Protein location
FatA
FatB
Fecha de publicación16-oct-2018
EditorFrontiers Media
CitaciónFrontiers in Plant Science 9: 1496 (2018)
ResumenSunflower 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.
Descripción15 Páginas.-- 10 Figuras.-- 1 Tabla
Versión del editorhttp://dx.doi.org/10.3389/fpls.2018.01496
URIhttp://hdl.handle.net/10261/176304
E-ISSN1664-462X
Aparece en las colecciones: (IG) Artículos




Ficheros en este ítem:
Fichero Descripción Tamaño Formato
FrontiersPlanSci_2018_New_Insights.pdfArtículo principal5,86 MBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo

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 Creative Commons