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.
CITATION STYLE
Chen, C., & Barbieri, J. T. (2018). Detection of ADP-ribosylating bacterial toxins. In Methods in Molecular Biology (Vol. 1813, pp. 287–295). Humana Press Inc. https://doi.org/10.1007/978-1-4939-8588-3_20
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