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- W3024210813 abstract "Abstract TATA-box binding protein (TBP) is required for every single transcription event in archaea and eukaryotes. It binds DNA and harbors two repeats with an internal structural symmetry that show sequence asymmetry. At various times in evolution, TBP has acquired multiple interaction partners and different organisms have evolved TBP paralogs with additional protein regions. Together, these observations raise questions of what molecular determinants (i.e. key residues) led to the ability of TBP to acquire new interactions, resulting in an increasingly complex transcriptional system in eukaryotes. We present a comprehensive study of the evolutionary history of TBP and its interaction partners across all domains of life, including viruses. Our analysis reveals the molecular determinants and suggests a unified and multi-stage evolutionary model for the functional innovations of TBP. These findings highlight how concerted chemical changes on a conserved structural scaffold allow for the emergence of complexity in a fundamental biological process." @default.
- W3024210813 created "2020-05-21" @default.
- W3024210813 creator A5005879991 @default.
- W3024210813 creator A5011188650 @default.
- W3024210813 creator A5014709451 @default.
- W3024210813 creator A5023375617 @default.
- W3024210813 creator A5067929237 @default.
- W3024210813 creator A5070945766 @default.
- W3024210813 date "2020-05-13" @default.
- W3024210813 modified "2023-10-17" @default.
- W3024210813 title "Molecular determinants underlying functional innovations of TBP and their impact on transcription initiation" @default.
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