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Molecules. 2016 Aug 22;21(8). pii: E1105. doi: 10.3390/molecules21081105.

Ribosome Inactivating Proteins from Rosaceae.

Author information

1
Department of Molecular Biotechnology, Faculty of Bioscience Engineering, Ghent University, 9000 Ghent, Belgium. shangchenjing@scsio.ac.cn.
2
Unité Mixte de Recherche 152 Pharma Développement, Institut de Recherche pour le Développement, Université Paul Sabatier, 31062 Toulouse, France. pierre.rouge@free.fr.
3
Department of Molecular Biotechnology, Faculty of Bioscience Engineering, Ghent University, 9000 Ghent, Belgium. ElsJM.VanDamme@ugent.be.

Abstract

Ribosome-inactivating proteins (RIPs) are widespread among higher plants of different taxonomic orders. In this study, we report on the RIP sequences found in the genome/transcriptome of several important Rosaceae species, including many economically important edible fruits such as apple, pear, peach, apricot, and strawberry. All RIP domains from Rosaceae share high sequence similarity with conserved residues in the catalytic site and the carbohydrate binding sites. The genomes of Malus domestica and Pyrus communis contain both type 1 and type 2 RIP sequences, whereas for Prunus mume, Prunus persica, Pyrus bretschneideri, and Pyrus communis a complex set of type 1 RIP sequences was retrieved. Heterologous expression and purification of the type 1 as well as the type 2 RIP from apple allowed to characterize the biological activity of the proteins. Both RIPs from Malus domestica can inhibit protein synthesis. Furthermore, molecular modelling suggests that RIPs from Rosaceae possess three-dimensional structures that are highly similar to the model proteins and can bind to RIP substrates. Screening of the recombinant type 2 RIP from apple on a glycan array revealed that this type 2 RIP interacts with terminal sialic acid residues. Our data suggest that the RIPs from Rosaceae are biologically active proteins.

KEYWORDS:

carbohydrate binding activity; molecular modeling; protein synthesis inhibition; ribosome-inactivating proteins

PMID:
27556443
DOI:
10.3390/molecules21081105
[Indexed for MEDLINE]
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