Conformational stability and DNA binding specificity of the cardiac T-box transcription factor Tbx20

Ingrid Macindoe, Laura Glockner, Paul Vukasin, Fiona A Stennard, Mauro W Costa, Richard P Harvey, Joel P Mackay, Margaret Sunde
Journal of Molecular Biology 2009 June 12, 389 (3): 606-18
The transcription factor Tbx20 acts within a hierarchy of T-box factors in lineage specification and morphogenesis in the mammalian heart and is mutated in congenital heart disease. T-box family members share a approximately 20-kDa DNA-binding domain termed the T-box. The question of how highly homologous T-box proteins achieve differential transcriptional control in heart development, while apparently binding to the same DNA sequence, remains unresolved. Here we show that the optimal DNA recognition sequence for the T-box of Tbx20 corresponds to a T-half-site. Furthermore, we demonstrate using purified recombinant domains that distinct T-boxes show significant differences in the affinity and kinetics of binding and in conformational stability, with the T-box of Tbx20 displaying molten globule character. Our data highlight unique features of Tbx20 and suggest mechanistic ways in which cardiac T-box factors might interact synergistically and/or competitively within the cardiac regulatory network.

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