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  Functional characterization and in silico modelling of MdPSY2 variants and MdPSY5 phytoene synthases from Malus domestica

Cerda, A., Moreno, J., Acosta, D., Godoy, F., Cáceres, J. C., Cabrera, R., et al. (2020). Functional characterization and in silico modelling of MdPSY2 variants and MdPSY5 phytoene synthases from Malus domestica. Journal of Plant Physiology, 249: 153166. doi:10.1016/j.jplph.2020.153166.

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Cerda, Ariel1, Autor
Moreno, J.C.2, Autor           
Acosta, Daniel1, Autor
Godoy, Francisca1, Autor
Cáceres, Juan Carlos1, Autor
Cabrera, Ricardo1, Autor
Stange, Claudia1, Autor
Affiliations:
1external, ou_persistent22              
2Small Molecules, Department Willmitzer, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753340              

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Schlagwörter: carotenoids, cv. ‘Fuji’, phytoene synthase, heterologous complementation, modelling
 Zusammenfassung: Carotenoids are plastid isoprenoid pigments that play critical roles in light harvesting, photoprotection, and phytohormone biosynthesis. They are also vitamin-A precursors and antioxidant molecules important for human nutrition. Apples (e.g. Malus x domestica Borkh), one of the most widely consumed fruits with high nutrient levels, have a very low carotenoid concentration in flesh, compared with other fruits and vegetables. This could be explained by a deficiency in carotenoid synthesis/accumulation and/or accelerated degradation. We analyzed the contribution of M. domestica cv. ‘Fuji’ phytoene synthase (PSY) in the biosynthesis of carotenoids and determined that among four MdPSY genes present in the organism, MdPSY2 and MdPSY5 are highly expressed in leaves and during fruit ripening in line with an increment in carotenoid content in fruits. Furthermore, two representative polymorphic MdPSY2 variants were found, one with a Tyr358Phe substitution (MdPSY2_F) and the other that additionally has a six-amino-acid deletion in the signal peptide (MdPSY2_CG). MdPSY2, MdPSY5, MdPSY2_F and MdPSY2_CG are all localized in plastids. Interestingly, the polymorphic MdPSY2_F and MdPSY2_CG variants show lower enzymatic activity than the wild-type form in a heterologous complementation assay, which could be attributed to the Tyr358Phe substitution close to the active-site pocket, as was suggested by 3-D modeling analysis. The presence of polymorphic MdPSY2 variants with lower enzymatic activity could be partially responsible for the low carotenoid content in Fuji apple fruits.

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Sprache(n): eng - English
 Datum: 2020
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: -
 Art des Abschluß: -

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Titel: Journal of Plant Physiology
  Andere : J. Plant Physiol.
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Stuttgart : Urban & Fischer
Seiten: 153166 Band / Heft: 249 Artikelnummer: 153166 Start- / Endseite: - Identifikator: ISSN: 0176-1617
CoNE: https://pure.mpg.de/cone/journals/resource/954928517792