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

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Endogenous ADP-Ribosylation

Part of the book series: Current Topics in Microbiology and Immunology ((CT MICROBIOLOGY,volume 384))

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.

Supplementary Material

A list of Genbank identifier and domain architectures of the proteins discussed in this chapter might be found at: ftp://ftp.ncbi.nih.gov/pub/aravind/ADPR/ADPR.html

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Acknowledgments

Work by the authors is supported by the Intramural Research Program of the National Library of Medicine, the National Institutes of Health, USA.

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Authors and Affiliations

  1. National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, 20894, USA

    L. Aravind, Dapeng Zhang, Swadha Anand & Lakshminarayan M. Iyer

  2. Microbiology Department, Biomedical Sciences Institute, University of Sao Paulo, Av. Prof. Lineu Prestes, 1374-Biomédicas II-Sala 250, Cidade Universitária, São Paulo, 05508-900, Brazil

    Robson F. de Souza

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    Friedrich Koch-Nolte

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Aravind, L., Zhang, D., de Souza, R.F., Anand, S., Iyer, L.M. (2014). The Natural History of ADP-Ribosyltransferases and the ADP-Ribosylation System. In: Koch-Nolte, F. (eds) Endogenous ADP-Ribosylation. Current Topics in Microbiology and Immunology, vol 384. Springer, Cham. https://doi.org/10.1007/82_2014_414

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