% 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{Macorano:1014978,
      author       = {Macorano, Luis and Binny, Taniya M. and Spiegl, Tobias and
                      Klimenko, Victoria and Singer, Anna and Oberleitner, Linda
                      and Applegate, Violetta and Seyffert, Sarah and Stefanski,
                      Anja and Gremer, Lothar and Gertzen, Christoph G. W. and
                      Höppner, Astrid and Smits, Sander H. J. and Nowack, Eva C.
                      M.},
      title        = {{DNA}-binding and protein structure of nuclear factors
                      likely acting in genetic information processing in the
                      {P}aulinella chromatophore},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {120},
      number       = {27},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {FZJ-2023-03522},
      pages        = {e2221595120},
      year         = {2023},
      abstract     = {The chromatophores in Paulinella are
                      evolutionary-early-stage photosynthetic organelles.
                      Biological processes in chromatophores depend on a
                      combination of chromatophore and nucleus-encoded proteins.
                      Interestingly, besides proteins carrying
                      chromatophore-targeting signals, a large arsenal of short
                      chromatophore-targeted proteins (sCTPs; <90 amino acids)
                      without recognizable targeting signals were found in
                      chromatophores. This situation resembles endosymbionts in
                      plants and insects that are manipulated by host-derived
                      antimicrobial peptides. Previously, we identified an
                      expanded family of sCTPs of unknown function, named here
                      "DNA-binding (DB)-sCTPs". DB-sCTPs contain a ~45 amino acid
                      motif that is conserved in some bacterial proteins with
                      predicted functions in DNA processing. Here, we explored
                      antimicrobial activity, DNA-binding capacity, and structures
                      of three purified recombinant DB-sCTPs. All three proteins
                      exhibited antimicrobial activity against bacteria involving
                      membrane permeabilization, and bound to bacterial lipids in
                      vitro. A combination of in vitro assays demonstrated binding
                      of recombinant DB-sCTPs to chromatophore-derived genomic DNA
                      sequences with an affinity in the low nM range.
                      Additionally, we report the 1.2 Å crystal structure of one
                      DB-sCTP. In silico docking studies suggest that helix α2
                      inserts into the DNA major grove and the exposed residues,
                      that are highly variable between different DB-sCTPs, confer
                      interaction with the DNA bases. Identification of
                      photosystem II subunit CP43 as a potential interaction
                      partner of one DB-sCTP, suggests DB-sCTPs to be involved in
                      more complex regulatory mechanisms. We hypothesize that
                      membrane binding of DB-sCTPs is related to their import into
                      chromatophores. Once inside, they interact with the
                      chromatophore genome potentially providing nuclear control
                      over genetic information processing.},
      cin          = {IBI-7},
      ddc          = {500},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524) / SFB 1208 B09 - Erforschung der Kontaktzone
                      zwischen Wirtszelle und ihren neu erworbenen
                      photosynthetischen Organellen in der Amöbe Paulinella
                      chromatophora (Rhizaria, Cercozoa) (B09) (289580405)},
      pid          = {G:(DE-HGF)POF4-5241 / G:(GEPRIS)289580405},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {37364116},
      UT           = {WOS:001041172600005},
      doi          = {10.1073/pnas.2221595120},
      url          = {https://juser.fz-juelich.de/record/1014978},
}