English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/158226
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

Characterization of a small acyl-CoA-binding protein (ACBP) from Helianthus annuus L. and its binding affinities

AuthorsAznar-Moreno, José A. ; Venegas-Calerón, Mónica ; Du, Zhi-Yan; Garcés Mancheño, Rafael ; Tanner, Julian A.; Chye, Mee-Len; Martínez-Force, Enrique ; Salas, Joaquín J.
KeywordsAcyl-CoA
Acyl-CoA binding protein
Phosphatidic acid
Phosphatidylcholine
Phospholipids
Sunflower
Issue DateMay-2016
PublisherElsevier
CitationPlant Physiology and Biochemistry 102: 141-150 (2016)
AbstractAcyl-CoA-binding proteins (ACBPs) bind to acyl-CoA esters and promote their interaction with other proteins, lipids and cell structures. Small class I ACBPs have been identified in different plants, such as Arabidopsis thaliana (AtACBP6), Brassica napus (BnACBP) and Oryza sativa (OsACBP1, OsACBP2, OsACBP3), and they are capable of binding to different acyl-CoA esters and phospholipids. Here we characterize HaACBP6, a class I ACBP expressed in sunflower (Helianthus annuus) tissues, studying the specificity of its corresponding recombinant HaACBP6 protein towards various acyl-CoA esters and phospholipids in vitro, particularly using isothermal titration calorimetry and protein phospholipid binding assays. This protein binds with high affinity to de novo synthetized derivatives palmitoly-CoA, stearoyl-CoA and oleoyl-CoA (Kd 0.29, 0.14 and 0.15 μM respectively). On the contrary, it showed lower affinity towards linoleoyl-CoA (Kd 5.6 μM). Moreover, rHaACBP6 binds to different phosphatidylcholine species (dipalmitoyl-PC, dioleoyl-PC and dilinoleoyl-PC), yet it displays no affinity towards other phospholipids like lyso-PC, phosphatidic acid and lysophosphatidic acid derivatives. In the light of these results, the possible involvement of this protein in sunflower oil synthesis is considered.
Description33 Páginas; 7 Figuras; 2 Tablas
Publisher version (URL)http://dx.doi.org/10.1016/j.plaphy.2016.02.025
URIhttp://hdl.handle.net/10261/158226
DOI10.1016/j.plaphy.2016.02.025
ISSN0981-9428
E-ISSN1873-2690
Appears in Collections:(IG) Artículos
Files in This Item:
File Description SizeFormat 
Postprint_2016_PPB_V102_P141.pdfArtículo principal1,49 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.