% 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{Myers:642942,
      author       = {Myers, Tanner M and Burnim, Andrew A and Jermain, Madison D
                      and Sondermann, Holger and Lee, Vincent T and Jiang,
                      Xiaofang and Winkler, Wade C.},
      title        = {{F}unctional analyses of bacterial {N}ano{RN}ase {B}
                      proteins reveals defining features of this enzyme family},
      journal      = {Nucleic acids symposium series},
      volume       = {53},
      number       = {22},
      issn         = {0305-1048},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {PUBDB-2025-05732},
      pages        = {gkaf1384},
      year         = {2025},
      note         = {ISSN 1362-4962 not unique: **2 hits**.},
      abstract     = {A combination of exoribonucleases and endoribonucleases
                      degrades RNA polymers to recycle nucleoside monophosphates.
                      A byproduct of these reactions is the accumulation of short
                      RNAs, 2–5 nucleotides in length. Characteristic enzymes,
                      generally referred to as nanoRNases, specifically process
                      short RNAs. Genes encoding nanoRNases are essential in some
                      bacteria; therefore, it is assumed that the accumulation of
                      short RNAs is detrimental to cells. However, the substrate
                      preferences and enzymatic mechanisms of the known categories
                      of nanoRNase enzymes have not been equally investigated. The
                      NrnB category of nanoRNases has been particularly
                      understudied. In this study, we identified bacterial NrnB
                      homologs and discovered they can be grouped into three
                      classes of proteins, which can be identified by their
                      characteristic sequence features. Purified representatives
                      of these classes of proteins revealed that they all process
                      RNA substrates from the 3′-terminus. The presence of
                      sequence features at the C-terminus was shown to be
                      diagnostic for general exoribonuclease activity against long
                      RNA substrates, whereas the absence of these C-terminal
                      elements was correlated with proteins that preferentially
                      acted against shorter RNA substrates. Together, these data
                      define members of the overall NrnB family of nanoRNase
                      proteins and identify some of their key features.},
      cin          = {CSSB-DESY-HS},
      ddc          = {540},
      cid          = {I:(DE-H253)CSSB-DESY-HS-20210521},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1093/nar/gkaf1384},
      url          = {https://bib-pubdb1.desy.de/record/642942},
}