Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

BKRF3 - uracil DNA glycosylase

Human herpesvirus 4

Lu, C.C. et al., Géoui, T. et al.

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Disease relevance of BKRF3

However, the expression and enzyme activity of EBV BKRF3 have not yet been characterized [1].
In addition, BKRF3 was able to complement an E. coli ung mutant in rifampin and nalidixic acid resistance mutator assays [1].

High impact information on BKRF3

The efficiency of EBV lytic DNA replication was slightly affected by BKRF3 small interfering RNA (siRNA), whereas cellular UNG2 siRNA or inhibition of cellular and viral UNG activities by expressing Ugi repressed EBV lytic DNA replication [1].
The expression kinetics and subcellular localization of BKRF3 products were detected in EBV-positive lymphoid and epithelial cells by using BKRF3-specific mouse antibodies [1].
Based on its amino acid sequence, the putative UDG of Epstein-Barr virus (EBV), BKRF3, belongs to the UNG family of proteins, and it was demonstrated previously to enhance oriLyt-dependent DNA replication in a cotransfection replication assay [1].
The structure of EBV UNG encoded by the BKRF3 reading frame shows the excellent global structural conservation within the solved examples of family 1 enzymes [2].

Biological context of BKRF3

Characterization of the uracil-DNA glycosylase activity of Epstein-Barr virus BKRF3 and its role in lytic viral DNA replication [1].

References

Characterization of the uracil-DNA glycosylase activity of Epstein-Barr virus BKRF3 and its role in lytic viral DNA replication. Lu, C.C., Huang, H.T., Wang, J.T., Slupphaug, G., Li, T.K., Wu, M.C., Chen, Y.C., Lee, C.P., Chen, M.R. J. Virol. (2007) [Pubmed]
New Insights on the Role of the gamma-Herpesvirus Uracil-DNA Glycosylase Leucine Loop Revealed by the Structure of the Epstein-Barr Virus Enzyme in Complex with an Inhibitor Protein. Géoui, T., Buisson, M., Tarbouriech, N., Burmeister, W.P. J. Mol. Biol. (2007) [Pubmed]

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