@article{RudelPrustySiegletal.2013,
  author    = {Rudel, Thomas and Prusty, Bhupesh K. and Siegl, Christine and Hauck, Petra and Hain, Johannes and Korhonen, Suvi J. and Hiltunen-Back, Eija and Poulakkainen, Mirja},
  title     = {Chlamydia trachomatis Infection Induces Replication of Latent HHV-6},
  series = {PLoS ONE},
  journal   = {PLoS ONE},
  doi       = {10.1371/journal.pone.0061400},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-96731},
  year      = {2013},
  abstract  = {Human herpesvirus-6 (HHV-6) exists in latent form either as a nuclear episome or integrated into human chromosomes in more than 90\% of healthy individuals without causing clinical symptoms. Immunosuppression and stress conditions can reactivate HHV-6 replication, associated with clinical complications and even death. We have previously shown that co-infection of Chlamydia trachomatis and HHV-6 promotes chlamydial persistence and increases viral uptake in an in vitro cell culture model. Here we investigated C. trachomatis-induced HHV-6 activation in cell lines and fresh blood samples from patients having Chromosomally integrated HHV-6 (CiHHV-6). We observed activation of latent HHV-6 DNA replication in CiHHV-6 cell lines and fresh blood cells without formation of viral particles. Interestingly, we detected HHV-6 DNA in blood as well as cervical swabs from C. trachomatis-infected women. Low virus titers correlated with high C. trachomatis load and vice versa, demonstrating a potentially significant interaction of these pathogens in blood cells and in the cervix of infected patients. Our data suggest a thus far underestimated interference of HHV-6 and C. trachomatis with a likely impact on the disease outcome as consequence of co-infection.},
  language  = {en}
}
@article{GassenBrechtefeldSchandryetal.2012,
  author    = {Gassen, Alwine and Brechtefeld, Doris and Schandry, Niklas and Arteaga-Salas, J. Manuel and Israel, Lars and Imhof, Axel and Janzen, Christian J.},
  title     = {DOT1A-dependent H3K76 methylation is required for replication regulation in Trypanosoma brucei},
  series = {Nucleic Acids Research},
  volume    = {40},
  journal   = {Nucleic Acids Research},
  number    = {20},
  doi       = {10.1093/nar/gks801},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-131449},
  pages     = {10302 - 10311},
  year      = {2012},
  abstract  = {Cell-cycle progression requires careful regulation to ensure accurate propagation of genetic material to the daughter cells. Although many cell-cycle regulators are evolutionarily conserved in the protozoan parasite Trypanosoma brucei, novel regulatory mechanisms seem to have evolved. Here, we analyse the function of the histone methyltransferase DOT1A during cell-cycle progression. Over-expression of DOT1A generates a population of cells with aneuploid nuclei as well as enucleated cells. Detailed analysis shows that DOT1A over-expression causes continuous replication of the nuclear DNA. In contrast, depletion of DOT1A by RNAi abolishes replication but does not prevent karyokinesis. As histone H3K76 methylation has never been associated with replication control in eukaryotes before, we have discovered a novel function of DOT1 enzymes, which might not be unique to trypanosomes.},
  language  = {en}
}
@article{HutinLingTarbouriechetal.2022,
  author    = {Hutin, Stephanie and Ling, Wai Li and Tarbouriech, Nicolas and Schoehn, Guy and Grimm, Clemens and Fischer, Utz and Burmeister, Wim P.},
  title     = {The vaccinia virus DNA helicase structure from combined single-particle cryo-electron microscopy and AlphaFold2 prediction},
  series = {Viruses},
  volume    = {14},
  journal   = {Viruses},
  number    = {10},
  issn      = {1999-4915},
  doi       = {10.3390/v14102206},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-290523},
  year      = {2022},
  abstract  = {Poxviruses are large DNA viruses with a linear double-stranded DNA genome circularized at the extremities. The helicase-primase D5, composed of six identical 90 kDa subunits, is required for DNA replication. D5 consists of a primase fragment flexibly attached to the hexameric C-terminal polypeptide (res. 323-785) with confirmed nucleotide hydrolase and DNA-binding activity but an elusive helicase activity. We determined its structure by single-particle cryo-electron microscopy. It displays an AAA+ helicase core flanked by N- and C-terminal domains. Model building was greatly helped by the predicted structure of D5 using AlphaFold2. The 3.9 {\AA} structure of the N-terminal domain forms a well-defined tight ring while the resolution decreases towards the C-terminus, still allowing the fit of the predicted structure. The N-terminal domain is partially present in papillomavirus E1 and polyomavirus LTA helicases, as well as in a bacteriophage NrS-1 helicase domain, which is also closely related to the AAA+ helicase domain of D5. Using the Pfam domain database, a D5_N domain followed by DUF5906 and Pox_D5 domains could be assigned to the cryo-EM structure, providing the first 3D structures for D5_N and Pox_D5 domains. The same domain organization has been identified in a family of putative helicases from large DNA viruses, bacteriophages, and selfish DNA elements.},
  language  = {en}
}