Conformational Stability and DNA Binding Specificity of the Cardiac T-Box Transcription Factor Tbx20. Macindoe, I., Glockner, L., Vukašin, P., Stennard, F., Costa, M., Harvey, R., Mackay, J., & Sunde, M. Journal of Molecular Biology, 389(3):606-618, 2009.
doi  abstract   bibtex   
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 ∼ 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. © 2009 Elsevier Ltd. All rights reserved.
@article{
 title = {Conformational Stability and DNA Binding Specificity of the Cardiac T-Box Transcription Factor Tbx20},
 type = {article},
 year = {2009},
 pages = {606-618},
 volume = {389},
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 abstract = {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 ∼ 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. © 2009 Elsevier Ltd. All rights reserved.},
 bibtype = {article},
 author = {Macindoe, I. and Glockner, L. and Vukašin, P. and Stennard, F.A. and Costa, M.W. and Harvey, R.P. and Mackay, J.P. and Sunde, M.},
 doi = {10.1016/j.jmb.2009.04.056},
 journal = {Journal of Molecular Biology},
 number = {3}
}

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