TBP expression and the investigation of on-bead assays for small molecule recognition

Abstract

The TATA binding protein, TBP, plays a central role in transcription by binding to DNA and recruiting other proteins through complementary surface-surface interactions. Understanding the nature of these interactions not only broadens the understanding of the transcription process, but also opens doors for the species-specific interruption of transcription. Such interruptions could ultimately lead to new strategies for combating disease, including malaria. Here, the over expression and isolation of TBP from Arabidopsis thaliana is reported using the Escherichia coli (BL21(DE3)) expression system. The synthesis, isolation, and characterization of peptides corresponding to the C-terminal domain of RNA polymerase II, a protein reported to interact with TBP through this domain, are reported. Initial inquiries into an on-bead colorimetric assay are also described.