Oleosin di-or tri-meric fusions with GFP undergo correct targeting and provide advantages for recombinant protein production

dc.contributor.author	Μπανίλας, Γεώργιος Π.	el
dc.contributor.author	Δάρας, Γεράσιμος	el
dc.contributor.author	Ρήγας, Σταμάτης	el
dc.contributor.author	Moloney, Maurice M.	en
dc.contributor.author	Χατζόπουλος, Πολυδεύκης	el
dc.date.accessioned	2015-05-24T07:00:08Z
dc.date.available	2015-05-24T07:00:08Z
dc.date.issued	2015-05-24
dc.identifier.uri	http://hdl.handle.net/11400/11022
dc.rights	Αναφορά Δημιουργού-Μη Εμπορική Χρήση-Όχι Παράγωγα Έργα 3.0 Ηνωμένες Πολιτείες	*
dc.rights.uri	http://creativecommons.org/licenses/by-nc-nd/3.0/us/	*
dc.source	http://www.sciencedirect.com/science/article/pii/S0981942810002512#	el
dc.subject	Recombinant proteins
dc.subject	Fusion expression
dc.subject	Έκφραση Fusion
dc.subject	Homo-oligomers
dc.subject	Ομο-ολιγομερή
dc.subject	Oilbody stability
dc.subject	Oilbody targeting
dc.subject	Oleosins
dc.subject	Ολεοσίνες
dc.subject	Ανασυνδυασμένες πρωτεΐνες
dc.title	Oleosin di-or tri-meric fusions with GFP undergo correct targeting and provide advantages for recombinant protein production	en
heal.type	journalArticle
heal.classification	Agriculture
heal.classification	Biology
heal.classification	Γεωργία
heal.classification	Βιολογία
heal.classificationURI	http://skos.um.es/unescothes/C00112
heal.classificationURI	http://skos.um.es/unescothes/C00399
heal.classificationURI	N/A-Γεωργία
heal.classificationURI	N/A-Βιολογία
heal.keywordURI	http://id.loc.gov/authorities/subjects/sh90005744
heal.identifier.secondary	doi:10.1016/j.plaphy.2010.12.002
heal.language	en
heal.access	campus
heal.recordProvider	Τεχνολογικό Εκπαιδευτικό Ίδρυμα Αθήνας. Σχολή Τεχνολογίας Τροφίμων και Διατροφής. Τμήμα Οινολογίας και Τεχνολογίας Ποτών	el
heal.publicationDate	2011-02
heal.bibliographicCitation	Banilas, G. Daras, G.., Rigas, S., Moloney, M. M. and Hatzopoulos, P. (2011). Oleosin di-or tri-meric fusions with GFP undergo correct targeting and provide advantages for recombinant protein production. "Plant Physiology and Biochemistry", 46(2), February 2011. pp 216-222. Available from: http://www.sciencedirect.com/science/article/pii/S0981942810002512#. [Accessed 10/12/2010]	en
heal.abstract	Plant oleosins are small proteins embedded within the phospholipid monolayer separating the triacylglycerol storage site of embryo-located oilbodies from the cytoplasm of oilseed cells. The potential of oleosins to act as carriers for recombinant proteins foreign to plant cells has been well established. Using this approach, the recombinant polypeptide is accumulated in oilbodies as a fusion with oleosin. DNA constructs having tandemly arranged oleosins followed by GFP or flanked by oleosins were used to transform Arabidopsis plants. In all cases the green fluorescence revealed that the fusion polypeptide had a native conformation and the recombinant proteins were correctly targeted to seed oilbodies. Mobilization of lipids was not retarded when using homo-dimer or -trimer oleosin fusions, since seed production, germination rates and seedling establishment were similar among all constructs, and comparable to wild-type Arabidopsis plants. Plant physiology and growth of recombinant lines were similar to wild-type plants. The construct specifying two oleosins flanking the GFP polypeptide revealed interesting properties regarding both the accumulation and the relative stability of the oilbody protein assembly. Although expression levels varied among transgenic lines, those transgenes accumulated significantly higher levels of fusion proteins as compared to previously reported values obtained by a single-oleosin configuration, reaching up to 2.3% of the total embryo proteins. These results shows that the expression cassettes comprising three oleosin molecules in frame to the GFP molecule or two oleosins flanking the GFP could be advantageous over the single-oleosin configuration for higher production and better commercialization of this plant biotechnological platform without jeopardizing plant vigour and physiology or oilbody stability.	en
heal.publisher	Elsevier Masson SAS	en
heal.journalName	Plant Physiology and Biochemistry	en
heal.journalType	peer-reviewed
heal.fullTextAvailability	true