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Structure and Activity of a Cytosolic Ribosome-Inactivating Protein from Rice

1
Department of Biotechnology, Faculty of Bioscience Engineering, Ghent University, Coupure links 653, B-9000 Ghent, Belgium
2
Department of Plants and Crops, Faculty of Bioscience Engineering, Ghent University, Coupure links 653, B-9000 Ghent, Belgium
3
UMR 152 PharmaDev, Université Paul Sabatier, Institut de Recherche et Développement, Faculté de Pharmacie, 35 Chemin des Maraîchers, 31062 Toulouse, France
*
Author to whom correspondence should be addressed.
Toxins 2019, 11(6), 325; https://doi.org/10.3390/toxins11060325
Received: 8 May 2019 / Revised: 30 May 2019 / Accepted: 4 June 2019 / Published: 6 June 2019
(This article belongs to the Special Issue Ribosome inactivating proteins (RIPs))
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Abstract

Ribosome-inactivating proteins (RIPs) are cytotoxic enzymes that inhibit protein translation by depurinating ribosomal RNA. Although most plant RIPs are synthesized with leader sequences that sequester them away from the host ribosomes, several RIPs from cereals lack these signal peptides and therefore probably reside in the cytosol near the plant ribosomes. More than 30 RIP genes have been identified in the rice (Oryza sativa spp. japonica) genome, many of them lacking a signal peptide. This paper focuses on a presumed cytosolic type-1 RIP from rice, referred to as OsRIP1. Using 3D modeling it is shown that OsRIP1 structurally resembles other cereal RIPs and has an active site that meets the requirements for activity. Furthermore, localization studies indicate that OsRIP1-eGFP fusion proteins reside in the nucleocytoplasmic space when expressed in epidermal cells of Nicotiana benthamiana or Arabidopsis thaliana suspension cells. Finally, OsRIP1 was recombinantly produced in Escherichia coli and was demonstrated to possess catalytic activity. Interestingly, this recombinant RIP inactivates wheat ribosomes far less efficiently than rabbit ribosomes in an in vitro system. These findings raise some interesting questions concerning the mode of action and physiological role of OsRIP1. This is the first time a RIP from rice is investigated at protein level and is shown to possess biological activity. View Full-Text
Keywords: rice; ribosome-inactivating protein; recombinant protein expression; localization; structure; enzymatic activity rice; ribosome-inactivating protein; recombinant protein expression; localization; structure; enzymatic activity
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De Zaeytijd, J.; Rougé, P.; Smagghe, G.; Van Damme, E.J. Structure and Activity of a Cytosolic Ribosome-Inactivating Protein from Rice. Toxins 2019, 11, 325.

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