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Structure-based analysis of the interaction between the simian virus 40 T-antigen origin binding domain and single-stranded DNA.

Meinke G, Phelan PJ, Fradet-Turcotte A, Bohm A, Archambault J, Bullock PA
J Virol 85 818-27 (2011)
Cited: 11 times
EuropePMC logo PMID: 20980496

Abstract

The origin-binding domain (OBD) of simian virus 40 (SV40) large T-antigen (T-Ag) is essential for many of T-Ag's interactions with DNA. Nevertheless, many important issues related to DNA binding, for example, how single-stranded DNA (ssDNA) transits along the T-Ag OBD, have yet to be established. Therefore, X-ray crystallography was used to determine the costructure of the T-Ag OBD bound to DNA substrates such as the single-stranded region of a forked oligonucleotide. A second structure of the T-Ag OBD crystallized in the presence of poly(dT)(12) is also reported. To test the conclusions derived from these structures, residues identified as being involved in binding to ssDNA by crystallography or by an earlier nuclear magnetic resonance study were mutated, and their binding to DNA was characterized via fluorescence anisotropy. In addition, these mutations were introduced into full-length T-Ag, and these mutants were tested for their ability to support replication. When considered in terms of additional homology-based sequence alignments, our studies refine our understanding of how the T-Ag OBDs encoded by the polyomavirus family interact with ssDNA, a critical step during the initiation of DNA replication.

Articles - 5d9i mentioned but not cited (1)

  1. Structural Based Analyses of the JC Virus T-Antigen F258L Mutant Provides Evidence for DNA Dependent Conformational Changes in the C-Termini of Polyomavirus Origin Binding Domains. Meinke G, Phelan PJ, Shin J, Gagnon D, Archambault J, Bohm A, Bullock PA. PLoS Pathog 12 e1005362 (2016)


Reviews citing this publication (2)

  1. Genome analysis of the new human polyomaviruses. Van Ghelue M, Khan MT, Ehlers B, Moens U. Rev Med Virol 22 354-377 (2012)
  2. The large tumor antigen: a "Swiss Army knife" protein possessing the functions required for the polyomavirus life cycle. Topalis D, Andrei G, Snoeck R. Antiviral Res 97 122-136 (2013)

Articles citing this publication (8)

  1. Asymmetric assembly of Merkel cell polyomavirus large T-antigen origin binding domains at the viral origin. Harrison CJ, Meinke G, Kwun HJ, Rogalin H, Phelan PJ, Bullock PA, Chang Y, Moore PS, Bohm A. J Mol Biol 409 529-542 (2011)
  2. Characterization of California sea lion polyomavirus 1: expansion of the known host range of the Polyomaviridae to Carnivora. Wellehan JF, Rivera R, Archer LL, Benham C, Muller JK, Colegrove KM, Gulland FM, St Leger JA, Venn-Watson SK, Nollens HH. Infect Genet Evol 11 987-996 (2011)
  3. The structure of SV40 large T hexameric helicase in complex with AT-rich origin DNA. Gai D, Wang D, Li SX, Chen XS. Elife 5 e18129 (2016)
  4. Insights into the initiation of JC virus DNA replication derived from the crystal structure of the T-antigen origin binding domain. Meinke G, Phelan PJ, Kalekar R, Shin J, Archambault J, Bohm A, Bullock PA. PLoS Pathog 10 e1003966 (2014)
  5. SV40 T antigen interactions with ssDNA and replication protein A: a regulatory role of T antigen monomers in lagging strand DNA replication. Onwubiko NO, Borst A, Diaz SA, Passkowski K, Scheffel F, Tessmer I, Nasheuer HP. Nucleic Acids Res 48 3657-3677 (2020)
  6. Analysis of the costructure of the simian virus 40 T-antigen origin binding domain with site I reveals a correlation between GAGGC spacing and spiral assembly. Meinke G, Phelan PJ, Harrison CJ, Bullock PA. J Virol 87 2923-2934 (2013)
  7. Structure-based design of a disulfide-linked oligomeric form of the simian virus 40 (SV40) large T antigen DNA-binding domain. Meinke G, Phelan P, Fradet-Turcotte A, Archambault J, Bullock PA. Acta Crystallogr D Biol Crystallogr 67 560-567 (2011)
  8. Modeling of the SV40 DNA Replication Machine. Simmons DT. Genes (Basel) 3 742-758 (2012)


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