Abstract
Label-free quantitative proteome analysis of extrafloral (EFN) and floral nectar (FN) from castor (Ricinus communis) plants resulted in the identification of 72 and 37 proteins, respectively. Thirty proteins were differentially accumulated between EFN and FN, and 24 of these were more abundant in the EFN. In addition to proteins involved in maintaining the nectar pathogen free such as chitinases and glucan 1,3-beta-glucosidase, both proteomes share an array of peptidases, lipases, carbohydrases, and nucleases. A total of 39 of the identified proteins, comprising different classes of hydrolases, were found to have biochemical matching partners in the exudates of at least five genera of carnivorous plants, indicating the EFN and FN possess a potential to digest biological material from microbial, animal or plant origin equivalent to the exudates of carnivorous plants.
Highlights
Nectar is an energy rich substance secreted by glands situated at the base of flowers or in other parts such as leaves, stems, rachis, etc. (Shah et al, 2016)
Beta-fructofuranosidase (B9R9R9) an enzyme known to balance sucrose levels in the extrafloral nectar of several species is among the proteins unique to the EFN
We present here a direct comparison between the proteomes of EFN and FN from the same species, collected under similar temporal and environmental conditions
Summary
Nectar is an energy rich substance secreted by glands situated at the base of flowers (floral nectar, FN) or in other parts such as leaves, stems, rachis, etc. (extrafloral nectar, EFN) (Shah et al, 2016). While FN attracts pollinating insects, EFN attracts aggressive ants and other mutualists, which in turn provide antiherbivore protection (Marazzi et al, 2013) These functional aspects are widely recognized (Roy et al, 2017), the dynamic of the relation FN/pollinators and EFN/mutualists is poorly known, especially the biochemical properties of the nectar which play a role in the attraction of particular pollinator/mutualists. Only a limited number of studies have presented data on the proteomes of EFN and FN (Orona-Tamayo et al, 2013; Seo et al, 2013; Zhou et al, 2016) These studies demonstrated the worth of establishing the complete proteomes of EFN and FN to acquire a better understanding of the preference of certain mutualists for a particular
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