@article{LealSchwebsBriggsetal.2020,
  author    = {Leal, Andrea Zurita and Schwebs, Marie and Briggs, Emma and Weisert, Nadine and Reis, Helena and Lemgruber, Leondro and Luko, Katarina and Wilkes, Jonathan and Butter, Falk and McCulloch, Richard and Janzen, Christian J.},
  title     = {Genome maintenance functions of a putative Trypanosoma brucei translesion DNA polymerase include telomere association and a role in antigenic variation},
  series = {Nucleic Acids Research},
  volume    = {48},
  journal   = {Nucleic Acids Research},
  number    = {17},
  doi       = {10.1093/nar/gkaa686},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-230579},
  pages     = {9660-9680},
  year      = {2020},
  abstract  = {Maintenance of genome integrity is critical to guarantee transfer of an intact genome from parent to off-spring during cell division. DNA polymerases (Pols) provide roles in both replication of the genome and the repair of a wide range of lesions. Amongst replicative DNA Pols, translesion DNA Pols play a particular role: replication to bypass DNA damage. All cells express a range of translesion Pols, but little work has examined their function in parasites, including whether the enzymes might contribute to host-parasite interactions. Here, we describe a dual function of one putative translesion Pol in African trypanosomes, which we now name TbPolIE. Previously, we demonstrated that TbPolIE is associated with telomeric sequences and here we show that RNAi-mediated depletion of TbPolIE transcripts results in slowed growth, altered DNA content, changes in cell morphology, and increased sensitivity to DNA damaging agents. We also show that TbPolIE displays pronounced localization at the nuclear periphery, and that its depletion leads to chromosome segregation defects and increased levels of endogenous DNA damage. Finally, we demonstrate that TbPolIE depletion leads to deregulation of telomeric variant surface glycoprotein genes, linking the function of this putative translesion DNA polymerase to host immune evasion by antigenic variation.},
  language  = {en}
}
@article{PascoalinoDindarVieiradaRochaetal.2014,
  author    = {Pascoalino, Bruno and Dindar, G{\"u}lcin and Vieira-da-Rocha, Jo{\~a}o P. and Machado, Carlos Renato and Janzen, Christian J. and Schenkman, Sergio},
  title     = {Characterization of two different Asf1 histone chaperones with distinct cellular localizations and functions in Trypanosoma brucei},
  series = {Nucleic Acids Research},
  volume    = {42},
  journal   = {Nucleic Acids Research},
  number    = {5},
  issn      = {1362-4962},
  doi       = {10.1093/nar/gkt1267},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-117220},
  pages     = {2906-2918},
  year      = {2014},
  abstract  = {The anti-silencing function protein 1 (Asf1) is a chaperone that forms a complex with histones H3 and H4 facilitating dimer deposition and removal from chromatin. Most eukaryotes possess two different Asf1 chaperones but their specific functions are still unknown. Trypanosomes, a group of early-diverged eukaryotes, also have two, but more divergent Asf1 paralogs than Asf1 of higher eukaryotes. To unravel possible different functions, we characterized the two Asf1 proteins in Trypanosoma brucei. Asf1A is mainly localized in the cytosol but translocates to the nucleus in S phase. In contrast, Asf1B is predominantly localized in the nucleus, as described for other organisms. Cytosolic Asf1 knockdown results in accumulation of cells in early S phase of the cell cycle, whereas nuclear Asf1 knockdown arrests cells in S/G2 phase. Overexpression of cytosolic Asf1 increases the levels of histone H3 and H4 acetylation. In contrast to cytosolic Asf1, overexpression of nuclear Asf1 causes less pronounced growth defects in parasites exposed to genotoxic agents, prompting a function in chromatin remodeling in response to DNA damage. Only the cytosolic Asf1 interacts with recombinant H3/H4 dimers in vitro. These findings denote the early appearance in evolution of distinguishable functions for the two Asf1 chaperons in trypanosomes.},
  language  = {en}
}