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

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A unique loop in T7 DNA polymerase mediates the binding of helicase-primase, DNA binding protein, and processivity factor.

Bacteriophage T7 DNA polymerase (gene 5 protein, gp5) interacts with its processivity factor, Escherichia coli thioredoxin, via a unique loop at the tip of the thumb subdomain. We find that this thioredoxin- binding domain is also the site of interaction of the phage- encoded helicase/primase (gp4) and ssDNA binding protein (gp2.5). Thioredoxin itself interacts only weakly with gp4 and gp2.5 but drastically enhances their binding to gp5. The acidic C termini of gp4 and gp2.5 are critical for this interaction in the absence of DNA. However, the C-terminal tail of gp4 is not required for binding to gp5 when the latter is bound to a primer/template. We propose that the thioredoxin- binding domain is a molecular switch that regulates the interaction of T7 DNA polymerase with other proteins of the replisome.[1]

References

  1. A unique loop in T7 DNA polymerase mediates the binding of helicase-primase, DNA binding protein, and processivity factor. Hamdan, S.M., Marintcheva, B., Cook, T., Lee, S.J., Tabor, S., Richardson, C.C. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
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