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Journal of Virology, August 2005, p. 10528-10539, Vol. 79, No. 16
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.16.10528-10539.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Association of Bovine Papillomavirus E2 Protein with Nuclear Structures In Vivo

Reet Kurg,1* Kristiina Sild,2 Aigi Ilves,1 Mari Sepp,2 and Mart Ustav1,2

Institute of Technology,1 Department of Microbiology and Virology, Institute of Molecular and Cell Biology, University of Tartu and Estonian Biocentre, Tartu, Estonia2

Received 11 February 2005/ Accepted 16 May 2005

Papillomaviruses are small DNA viruses which have the capacity to establish a persistent infection in mammalian epithelial cells. The papillomavirus E2 protein is a central coordinator of viral gene expression, genome replication, and maintenance. We have investigated the distribution of bovine papillomavirus E2 protein in nuclei of proliferating cells and found that E2 is associated with cellular chromatin. This distribution does not change during the entire cell cycle. The N-terminal transactivation domain, but not the C-terminal DNA-binding domain, of the E2 protein is responsible for this association. The majority of the full-length E2 protein can only be detected in chromatin-enriched fractions but not as a free protein in the nucleus. Limited micrococcal nuclease digestion revealed that the E2 protein partitioned to different chromatin regions. A fraction of the E2 protein was located at nuclear sites that are resistant against nuclease attack, whereas the remaining E2 resided on compact chromatin accessible to micrococcal nuclease. These data suggest that there are two pools of E2 in the cell nucleus: one that localizes on transcriptionally inactive compact chromatin and the other, which compartmentalizes to transcriptionally active nuclear structures of the cell. Our data also suggest that E2 associates with chromatin through cellular protein(s), which in turn is released from chromatin at 0.4 M salt.

* Corresponding author. Mailing address: Institute of Technology University of Tartu 23 Riia Street, 51010 Tartu, Estonia. Phone: 372-7-375040. Fax: 372-7-420286. E-mail: rkurg{at}ebc.ee.

Journal of Virology, August 2005, p. 10528-10539, Vol. 79, No. 16
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.16.10528-10539.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Jang, M. K., Kwon, D., McBride, A. A. (2009). Papillomavirus E2 Proteins and the Host Brd4 Protein Associate with Transcriptionally Active Cellular Chromatin. J. Virol. 83: 2592-2600 [Abstract] [Full Text]  
  • Donaldson, M. M., Boner, W., Morgan, I. M. (2007). TopBP1 Regulates Human Papillomavirus Type 16 E2 Interaction with Chromatin. J. Virol. 81: 4338-4342 [Abstract] [Full Text]  
  • Kurg, R., Tekkel, H., Abroi, A., Ustav, M. (2006). Characterization of the Functional Activities of the Bovine Papillomavirus Type 1 E2 Protein Single-Chain Heterodimers. J. Virol. 80: 11218-11225 [Abstract] [Full Text]  
  • Ilves, I., Maemets, K., Silla, T., Janikson, K., Ustav, M. (2006). Brd4 is involved in multiple processes of the bovine papillomavirus type 1 life cycle.. J. Virol. 80: 3660-3665 [Abstract] [Full Text]  


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