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Gene Review

BALF5  -  DNA polymerase

Human herpesvirus 4

 
 
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Disease relevance of BALF5

 

High impact information on BALF5

  • In contrast, the BALF5 Pol catalytic protein, the BALF2 single-stranded-DNA binding protein, and the BBLF2/3 protein, a component of the helicase-primase complex, were colocalized as distinct dots distributed within replication compartments, representing viral replication factories [4].
  • Experiments using lysates from insect cells superinfected with combinations of recombinant baculoviruses capable of expressing each of viral replication proteins showed that not the BMRF1 Pol accessory subunit but rather the BALF5 Pol catalytic subunit directly interacts with the BBLF4-BSLF1-BBLF2/3 complex [5].
  • Furthermore, double infection with pairs of recombinant viruses revealed that each component of the BBLF4-BSLF1-BBLF2/3 complex makes contact with the BALF5 Pol catalytic subunit [5].
  • Although the complex was stable in 500 mM NaCl and 1% NP-40, the BALF5 protein became dissociated in the presence of 0.1% sodium dodecyl sulfate [5].
  • In contrast, the hydrolysis of single-stranded DNA by the BALF5 protein was not affected by the addition of the BMRF1 polymerase accessory subunit at all [6].
 

Chemical compound and disease context of BALF5

 

Biological context of BALF5

 

Associations of BALF5 with chemical compounds

 

Physical interactions of BALF5

  • These observations suggest that the BMRF1 polymerase accessory subunit forms a complex with the BALF5 polymerase catalytic subunit to stabilize the interaction of the holoenzyme complex with the 3'-OH end of the primer on the template DNA during exonucleolysis [6].
 

Other interactions of BALF5

  • Optimal stimulation was obtained when the molar ratio of BMRF1 protein to BALF5 protein was 2 and higher, identical to the values required for reconstituting the optimum DNA polymerizing activity (T. Tsurumi, T. Daikoku, R. Kurachi, and Y. Nishiyama, J. Virol. 67:7648-7653, 1993) [6].

References

  1. Multiple Roles of Epstein-Barr Virus SM Protein in Lytic Replication. Han, Z., Marendy, E., Wang, Y.D., Yuan, J., Sample, J.T., Swaminathan, S. J. Virol. (2007) [Pubmed]
  2. Functional expression and characterization of the Epstein-Barr virus DNA polymerase catalytic subunit. Tsurumi, T., Kobayashi, A., Tamai, K., Daikoku, T., Kurachi, R., Nishiyama, Y. J. Virol. (1993) [Pubmed]
  3. Cooperation of EBV DNA polymerase and EA-D(BMRF1) in vitro and colocalization in nuclei of infected cells. Kiehl, A., Dorsky, D.I. Virology (1991) [Pubmed]
  4. Architecture of replication compartments formed during Epstein-Barr virus lytic replication. Daikoku, T., Kudoh, A., Fujita, M., Sugaya, Y., Isomura, H., Shirata, N., Tsurumi, T. J. Virol. (2005) [Pubmed]
  5. The Epstein-Barr virus pol catalytic subunit physically interacts with the BBLF4-BSLF1-BBLF2/3 complex. Fujii, K., Yokoyama, N., Kiyono, T., Kuzushima, K., Homma, M., Nishiyama, Y., Fujita, M., Tsurumi, T. J. Virol. (2000) [Pubmed]
  6. Further characterization of the interaction between the Epstein-Barr virus DNA polymerase catalytic subunit and its accessory subunit with regard to the 3'-to-5' exonucleolytic activity and stability of initiation complex at primer terminus. Tsurumi, T., Daikoku, T., Nishiyama, Y. J. Virol. (1994) [Pubmed]
  7. Bipartite DNA-binding region of the Epstein-Barr virus BMRF1 product essential for DNA polymerase accessory function. Kiehl, A., Dorsky, D.I. J. Virol. (1995) [Pubmed]
  8. Identification and functional characterization of Epstein-Barr virus DNA polymerase by in vitro transcription-translation of a cloned gene. Lin, J.C., Sista, N.D., Besençon, F., Kamine, J., Pagano, J.S. J. Virol. (1991) [Pubmed]
  9. Functional interaction between Epstein-Barr virus DNA polymerase catalytic subunit and its accessory subunit in vitro. Tsurumi, T., Daikoku, T., Kurachi, R., Nishiyama, Y. J. Virol. (1993) [Pubmed]
 
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