Detection of ADP-Ribosylating Bacterial Toxins. Methods Mol Biol 2018;1813:287-295
Date
08/12/2018Pubmed ID
30097876DOI
10.1007/978-1-4939-8588-3_20Scopus ID
2-s2.0-85051506237 (requires institutional sign-in at Scopus site) 2 CitationsAbstract
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.
Author List
Chen C, Barbieri JTAuthor
Joseph T. Barbieri PhD Professor in the Microbiology and Immunology department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
ADP Ribose TransferasesADP-Ribosylation
Bacterial Toxins
Catalysis
Models, Molecular
Molecular Biology
NAD
