| Literature DB >> 30097876 |
Chen Chen1, Joseph T Barbieri2.
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.Entities:
Keywords: 32P-NAD; ADP-ribosyltransferase; Bacterial toxins; Biotin-NAD; NAD-glycohydrolase; Toxins
Mesh:
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Year: 2018 PMID: 30097876 DOI: 10.1007/978-1-4939-8588-3_20
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745