English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/116543
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

Cloning, heterologous expression and biochemical characterization of plastidial sn-glycerol-3-phosphate acyltransferase from Helianthus annuus

AuthorsPayá-Milans, Miriam ; Venegas-Calerón, Mónica ; Salas, Joaquín J. ; Garcés Mancheño, Rafael ; Martínez-Force, Enrique
KeywordsHelianthus annuus
Plastids
Substrate specificity
Glycerol-3-phosphate acyltransferase
Sunflower
Issue Date2015
PublisherElsevier
CitationPhytochemistry 111: 27- 36 (2015)
Abstract© 2015 Elsevier Ltd. All rights reserved. The acyl-[acyl carrier protein]:sn-1-glycerol-3-phosphate acyltransferase (GPAT; E.C. 2.3.1.15) catalyzes the first step of glycerolipid assembly within the stroma of the chloroplast. In the present study, the sunflower (Helianthus annuus, L.) stromal GPAT was cloned, sequenced and characterized. We identified a single ORF of 1344 base pairs that encoded a GPAT sharing strong sequence homology with the plastidial GPAT from Arabidopsis thaliana (ATS1, At1g32200). Gene expression studies showed that the highest transcript levels occurred in green tissues in which chloroplasts are abundant. The corresponding mature protein was heterologously overexpressed in Escherichia coli for purification and biochemical characterization. In vitro assays using radiolabelled acyl-ACPs and glycerol-3-phosphate as substrates revealed a strong preference for oleic versus palmitic acid, and weak activity towards stearic acid. The positional fatty acid composition of relevant chloroplast phospholipids from sunflower leaves did not reflect the in vitro GPAT specificity, suggesting a more complex scenario with mixed substrates at different concentrations, competition with other acyl-ACP consuming enzymatic reactions, etc. In summary, this study has confirmed the affinity of this enzyme which would partly explain the resistance to cold temperatures observed in sunflower plants.
URIhttp://hdl.handle.net/10261/116543
DOI10.1016/j.phytochem.2014.12.028
Identifiersdoi: 10.1016/j.phytochem.2014.12.028
issn: 0031-9422
Appears in Collections:(IG) Artículos
Files in This Item:
File Description SizeFormat 
Postprint_Phytochemistry_2015_V111_P27.pdf4,08 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.