% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Mortensen:613926,
      author       = {Mortensen, Sofia and Kuncova, Stanislava and Lormand,
                      Justin David and Myers, Tanner and Kim, Soo-Kyoung and Lee,
                      Vincent and Winkler, Wade and Sondermann, Holger},
      title        = {{S}tructural and bioinformatics analyses identify
                      deoxydinucleotide-specific nucleasesand their association
                      with genomic islands in {G}ram-positive bacteria},
      journal      = {Nucleic acids research},
      volume       = {53},
      number       = {1},
      issn         = {0305-1048},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {PUBDB-2024-05705},
      pages        = {gkae1235},
      year         = {2025},
      note         = {ISSN 1362-4962 not unique: **2 hits**.},
      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.},
      cin          = {CSSB-DESY-HS / FS DOOR-User / CSSB-CF-SPC},
      ddc          = {570},
      cid          = {I:(DE-H253)CSSB-DESY-HS-20210521 /
                      $I:(DE-H253)FS_DOOR-User-20241023$ /
                      I:(DE-H253)CSSB-CF-SPC-20210520},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / 6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-633 / G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P11-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39778863},
      doi          = {10.1093/nar/gkae1235},
      url          = {https://bib-pubdb1.desy.de/record/613926},
}