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Toxins 2018, 10(6), 240;

Functional Assays for Measuring the Catalytic Activity of Ribosome Inactivating Proteins

Department of Plant Biology, School of Environmental and Biological Sciences, Rutgers University, New Brunswick, NJ 08901-8520, USA
Author to whom correspondence should be addressed.
Received: 18 April 2018 / Revised: 1 June 2018 / Accepted: 7 June 2018 / Published: 14 June 2018
(This article belongs to the Special Issue Toxins:10th Anniversary)
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Ribosome-inactivating proteins (RIPs) are potent toxins that inactivate ribosomes by catalytically removing a specific adenine from the α-sarcin/ricin loop (SRL) of the large rRNA. Direct assays for measuring depurination activity and indirect assays for measuring the resulting translation inhibition have been employed to determine the enzyme activity of RIPs. Rapid and sensitive methods to measure the depurination activity of RIPs are critical for assessing their reaction mechanism, enzymatic properties, interaction with ribosomal proteins, ribotoxic stress signaling, in the search for inhibitors and in the detection and diagnosis of enteric infections. Here, we review the major assays developed for measuring the catalytic activity of RIPs, discuss their advantages and disadvantages and explain how they are used in understanding the catalytic mechanism, ribosome specificity, and dynamic enzymatic features of RIPs. View Full-Text
Keywords: ribosome inactivating protein; depurination assays; translation inhibition assays ribosome inactivating protein; depurination assays; translation inhibition assays
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Zhou, Y.; Li, X.-P.; Kahn, J.N.; Tumer, N.E. Functional Assays for Measuring the Catalytic Activity of Ribosome Inactivating Proteins. Toxins 2018, 10, 240.

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