Literature DB >> 30097876

Detection of ADP-Ribosylating Bacterial Toxins.

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

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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


  2 in total

1.  Gut microbiome ADP-ribosyltransferases are widespread phage-encoded fitness factors.

Authors:  Eric M Brown; Hugo Arellano-Santoyo; Emily R Temple; Zachary A Costliow; Matthieu Pichaud; A Brantley Hall; Kai Liu; Michael A Durney; Xiebin Gu; Damian R Plichta; Clary A Clish; Jeffrey A Porter; Hera Vlamakis; Ramnik J Xavier
Journal:  Cell Host Microbe       Date:  2021-08-16       Impact factor: 31.316

2.  ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function.

Authors:  Lisa Weixler; Katja Schäringer; Jeffrey Momoh; Bernhard Lüscher; Karla L H Feijs; Roko Žaja
Journal:  Nucleic Acids Res       Date:  2021-04-19       Impact factor: 16.971

  2 in total

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