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Both of the TBP lobes (N-terminal and C-terminal lobes) belong to the helix-grip fold and are “joined together” to form a single protein 8– 11 (Fig. TBP is a relatively small protein that is shaped like a saddle and contains two lobes (TBP lobes) that bind to specific DNA sequences in the gene promoter. general transcription factors and RNA polymerase) to assemble the pre-initiation complex (PIC) 1– 7. Transcription initiation in eukaryotes and archaea relies on a central molecule called TATA-box-binding protein (TBP) that recruits additional factors (e.g. ![]() These findings highlight how concerted chemical changes on a conserved structural scaffold allow for the emergence of complexity in a fundamental biological process. Our analysis reveals the molecular determinants and suggests a unified and multi-stage evolutionary model for the functional innovations of TBP. We present a comprehensive study of the evolutionary history of TBP and its interaction partners across all domains of life, including viruses. key residues) led to the ability of TBP to acquire new interactions, resulting in an increasingly complex transcriptional system in eukaryotes. Together, these observations raise questions of what molecular determinants (i.e. At various times in evolution, TBP has acquired multiple interaction partners and different organisms have evolved TBP paralogs with additional protein regions. It binds DNA and harbors two repeats with an internal structural symmetry that show sequence asymmetry. TATA-box binding protein (TBP) is required for every single transcription event in archaea and eukaryotes. ![]() ![]() ![]() ![]() snacks, slippers, books etc., and explains how Beltway makes moves as seamless as possible. 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