Chapter

Endogenous ADP-Ribosylation

Volume 384 of the series Current Topics in Microbiology and Immunology pp 3-32

Date:

The Natural History of ADP-Ribosyltransferases and the ADP-Ribosylation System

  • L. AravindAffiliated withNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health Email author 
  • , Dapeng ZhangAffiliated withNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health
  • , Robson F. de SouzaAffiliated withMicrobiology Department, Biomedical Sciences Institute, University of Sao Paulo
  • , Swadha AnandAffiliated withNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health
  • , Lakshminarayan M. IyerAffiliated withNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health

* Final gross prices may vary according to local VAT.

Get Access

Abstract

Catalysis of NAD+-dependent ADP-ribosylation of proteins, nucleic acids, or small molecules has evolved in at least three structurally unrelated superfamilies of enzymes, namely ADP-ribosyltransferase (ART), the Sirtuins, and probably TM1506. Of these, the ART superfamily is the most diverse in terms of structure, active site residues, and targets that they modify. The primary diversification of the ART superfamily occurred in the context of diverse bacterial conflict systems, wherein ARTs play both offensive and defensive roles. These include toxin–antitoxin systems, virus-host interactions, intraspecific antagonism (polymorphic toxins), symbiont/parasite effectors/toxins, resistance to antibiotics, and repair of RNAs cleaved in conflicts. ARTs evolving in these systems have been repeatedly acquired by lateral transfer throughout eukaryotic evolution, starting from the PARP family, which was acquired prior to the last eukaryotic common ancestor. They were incorporated into eukaryotic regulatory/epigenetic control systems (e.g., PARP family and NEURL4), and also used as defensive (e.g., pierisin and CARP-1 families) or immunity-related proteins (e.g., Gig2-like ARTs). The ADP-ribosylation system also includes other domains, such as the Macro, ADP-ribosyl glycohydrolase, NADAR, and ADP-ribosyl cyclase, which appear to have initially diversified in bacterial conflict-related systems. Unlike ARTs, sirtuins appear to have a much smaller presence in conflict-related systems.