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• W2123267727 abstract "The transcription factor p73 triggers developmental pathways and overlaps stress-induced p53 transcriptional pathways. How p53-family response elements determine and regulate transcriptional specificity remains an unsolved problem. In this work, we have determined the first crystal structures of p73 DNA-binding domain tetramer bound to response elements with spacers of different length. The structure and function of the adaptable tetramer are determined by the distance between two half-sites. The structures with zero and one base-pair spacers show compact p73 DNA-binding domain tetramers with large tetramerization interfaces; a two base-pair spacer results in DNA unwinding and a smaller tetramerization interface, whereas a four base-pair spacer hinders tetramerization. Functionally, p73 is more sensitive to spacer length than p53, with one base-pair spacer reducing 90% of transactivation activity and longer spacers reducing transactivation to basal levels. Our results establish the quaternary structure of the p73 DNA-binding domain required as a scaffold to promote transactivation." @default.
• W2123267727 created "2016-06-24" @default.
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• W2123267727 date "2012-04-02" @default.
• W2123267727 modified "2023-10-12" @default.
• W2123267727 title "Structure of p73 DNA-binding domain tetramer modulates p73 transactivation" @default.
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• W2123267727 doi "https://doi.org/10.1073/pnas.1115463109" @default.
• W2123267727 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3341074" @default.
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