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Conflict RNA modification, host-parasite co-evolution, and the origins of DNA and DNA-binding proteins
Stockholm University, Faculty of Science, Department of Molecular Biology and Functional Genomics. University of Edinburgh, UK.
2014 (English)In: Biochemical Society Transactions, ISSN 0300-5127, E-ISSN 1470-8752, Vol. 42, 1159-1167 p.Article in journal (Refereed) Published
Abstract [en]

Nearly 150 different enzymatically modified forms of the four canonical residues in RNA have been identified. For instance, enzymes of the ADAR (adenosine deaminase acting on RNA) family convert adenosine residues into inosine in cellular dsRNAs. Recent findings show that DNA endonuclease V enzymes have undergone an evolutionary transition from cleaving 3' to deoxyinosine in DNA and ssDNA to cleaving 3' to inosine in dsRNA and ssRNA in humans. Recent work on dsRNA-binding domains of ADARs and other proteins also shows that a degree of sequence specificity is achieved by direct readout in the minor groove. However, the level of sequence specificity observed is much less than that of DNA major groove-binding helix-turn-helix proteins. We suggest that the evolution of DNA-binding proteins following the RNA to DNA genome transition represents the major advantage that DNA genomes have over RNA genomes. We propose that a hypothetical RNA modification, a RRAR (ribose reductase acting on genomic dsRNA) produced the first stretches of DNA in RNA genomes. We discuss why this is the most satisfactory explanation for the origin of DNA. The evolution of this RNA modification and later steps to DNA genomes are likely to have been driven by cellular genome co-evolution with viruses and intragenomic parasites. RNA modifications continue to be involved in host-virus conflicts; in vertebrates, edited cellular dsRNAs with inosine-uracil base pairs appear to be recognized as self RNA and to suppress activation of innate immune sensors that detect viral dsRNA.

Place, publisher, year, edition, pages
2014. Vol. 42, 1159-1167 p.
Keyword [en]
DNA-binding protein, Drosophila, evolution of DNA, innate immunity, RNA editing, RNA modification
National Category
Biochemistry and Molecular Biology
URN: urn:nbn:se:su:diva-107429DOI: 10.1042/BST20140147ISI: 000340329200072OAI: diva2:748397

AuthorCount:2;[DUBBELAFFILIERINGEGENKeegan, Liam P.]Stockholm Univ, Dept Mol Biol & Funct Genom, S-10691 Stockholm, Sweden; Keegan, LP (reprint author), Stockholm Univ, Dept Mol Biol & Funct Genom, S-10691 Stockholm, Sweden.

Available from: 2014-09-19 Created: 2014-09-15 Last updated: 2014-09-19Bibliographically approved

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