Abstract
Many bacterial toxins catalyze the transfer of ADP-ribose from nicotinamide adenine dinucleotide (NAD) to a host protein. Greater than 35 bacterial ADP-ribosyltransferase toxins (bARTTs) have been identified. ADP-ribosylation of host proteins may be specific or promiscuous. Despite this diversity, bARTTs share a common reaction mechanism, three-dimensional active site structure, and a conserved active site glutamic acid. Here, we describe how to measure the ADP-ribosylation of host proteins as purified proteins or within a cell lysate.
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Acknowledgments
JTB laboratory is supported by grants from the NIH: AI-030162 and AI-118389.
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Chen, C., Barbieri, J.T. (2018). Detection of ADP-Ribosylating Bacterial Toxins. In: Chang, P. (eds) ADP-ribosylation and NAD+ Utilizing Enzymes. Methods in Molecular Biology, vol 1813. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-8588-3_20
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DOI: https://doi.org/10.1007/978-1-4939-8588-3_20
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