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

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Interaction of TIP26 from a hyperthermophilic archaeon with TFB/ TBP/DNA ternary complex.

Interactions of TBP-interacting protein (TIP26), TBP, and TFB from a hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 with TATA-DNA were examined by electrophoretic mobility shift assay. Tk-TFB formed a ternary complex with Tk-TBP and TATA-DNA. Tk-TIP26 did not inhibit the formation of this ternary complex, but interacted with it to form a TIP26/TFB/ TBP/DNA quaternary complex. This interaction is rather weak, and a large excess of Tk-TIP26 over Tk-TBP is required to fully convert the TFB/ TBP/DNA ternary complex to the quaternary complex. However, determination of the concentration of Tk-TIP26 and Tk-TBP in KOD1 cells by Western blotting analysis indicated that the concentration of Tk-TIP26 is approximately ten times that of Tk-TBP, suggesting that the quaternary complex might also form in vivo.[1]

References

  1. Interaction of TIP26 from a hyperthermophilic archaeon with TFB/TBP/DNA ternary complex. Matsuda, T., Fujikawa, M., Haruki, M., Tang, X.F., Ezaki, S., Imanaka, T., Morikawa, M., Kanaya, S. Extremophiles (2001) [Pubmed]
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