Home > Publications database > Structural and bioinformatics analyses identify deoxydinucleotide-specific nucleasesand their association with genomic islands in Gram-positive bacteria |
Journal Article | PUBDB-2024-05705 |
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2025
Oxford Univ. Press
Oxford
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Please use a persistent id in citations: doi:10.1093/nar/gkae1235
Abstract: Dinucleases of the DEDD superfamily, such as oligoribonuclease, Rexo2, and nanoRNaseC, catalyze the essential final step of RNA degradation, the conversion of di- tomononucleotides. The active sites of these enzymes are optimized for substrates that are twonucleotides long, and do not discriminate between RNA and DNA. Here, we identified a novelDEDD subfamily, members of which function as dedicated deoxydinucleases (diDNases) thatspecifically hydrolyze single-stranded DNA dinucleotides in a sequence-independent manner.Crystal structures of enzyme-substrate complexes reveal that specificity for DNA stems froma combination of conserved structural elements that exclude diribonucleotides as substrates.Consistently, diDNases fail to complement the loss of enzymes that act on diribonucleotides,indicating that these two groups of enzymes support distinct cellular functions. The genesencoding diDNases are found predominantly in genomic islands of Actinomycetes andClostridia, which, together with their association with phage-defense systems, suggestpotential roles in bacterial immunity.
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