@article{HartlBodemJochheimetal.2011,
  author    = {Hartl, Maximilian J. and Bodem, Jochen and Jochheim, Fabian and Rethwilm, Axel and R{\"o}sch, Paul and W{\"o}hrl, Birgitta M.},
  title     = {Regulation of foamy virus protease activity by viral RNA},
  series = {Retrovirology},
  volume    = {8},
  journal   = {Retrovirology},
  number    = {Suppl. 1},
  doi       = {10.1186/1742-4690-8-S1-A228},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-142248},
  pages     = {A228},
  year      = {2011},
  abstract  = {No abstract available.},
  language  = {en}
}
@article{SpannausHartlWoehrletal.2012,
  author    = {Spannaus, Ralf and Hartl, Maximilian J. and W{\"o}hrl, Birgitta M. and Rethwilm, Axel and Bodem, Jochen},
  title     = {The prototype foamy virus protease is active independently of the integrase domain},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-75370},
  year      = {2012},
  abstract  = {Background: Recently, contradictory results on foamy virus protease activity were published. While our own results indicated that protease activity is regulated by the viral RNA, others suggested that the integrase is involved in the regulation of the protease. Results: To solve this discrepancy we performed additional experiments showing that the protease-reverse transcriptase (PR-RT) exhibits protease activity in vitro and in vivo, which is independent of the integrase domain. In contrast, Pol incorporation, and therefore PR activity in the viral context, is dependent on the integrase domain. To further analyse the regulation of the protease, we incorporated Pol in viruses by expressing a GagPol fusion protein, which supported near wild-type like infectivity. A GagPR-RT fusion, lacking the integrase domain, also resulted in wild-type like Gag processing, indicating that the integrase is dispensable for viral Gag maturation. Furthermore, we demonstrate with a trans-complementation assays that the PR in the context of the PR-RT protein supports in trans both, viral maturation and infectivity. Conclusion: We provide evidence that the FV integrase is required for Pol encapsidation and that the FV PR activity is integrase independent. We show that an active PR can be encapsidated in trans as a GagPR-RT fusion protein.},
  subject      = {Medizin},
  language  = {en}
}
@article{BodemSchromMoschalletal.2013,
  author    = {Bodem, Jochen and Schrom, Eva-Maria and Moschall, Rebecca and Hartl, Maximilian J. and Weitner, Helena and Fecher, David and Langemeier, J{\"o}rg and W{\"o}hrl, Brigitta M.},
  title     = {U1snRNP-mediated suppression of polyadenylation in conjunction with the RNA structure controls poly (A) site selection in foamy viruses},
  series = {Retrovirology},
  journal   = {Retrovirology},
  doi       = {10.1186/1742-4690-10-55},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-96085},
  year      = {2013},
  abstract  = {Background During reverse transcription, retroviruses duplicate the long terminal repeats (LTRs). These identical LTRs carry both promoter regions and functional polyadenylation sites. To express full-length transcripts, retroviruses have to suppress polyadenylation in the 5′LTR and activate polyadenylation in the 3′LTR. Foamy viruses have a unique LTR structure with respect to the location of the major splice donor (MSD), which is located upstream of the polyadenylation signal. Results Here, we describe the mechanisms of foamy viruses regulating polyadenylation. We show that binding of the U1 small nuclear ribonucleoprotein (U1snRNP) to the MSD suppresses polyadenylation at the 5′LTR. In contrast, polyadenylation at the 3′LTR is achieved by adoption of a different RNA structure at the MSD region, which blocks U1snRNP binding and furthers RNA cleavage and subsequent polyadenylation. Conclusion Recently, it was shown that U1snRNP is able to suppress the usage of intronic cryptic polyadenylation sites in the cellular genome. Foamy viruses take advantage of this surveillance mechanism to suppress premature polyadenylation at the 5'end of their RNA. At the 3'end, Foamy viruses use a secondary structure to presumably block access of U1snRNP and thereby activate polyadenylation at the end of the genome. Our data reveal a contribution of U1snRNP to cellular polyadenylation site selection and to the regulation of gene expression.},
  subject      = {Polyadenylierung},
  language  = {en}
}