Anti-TBP (aa 1-100) Monoclonal Antibody, clone nBcdbn 62952 [HRP]

ab]Abstract A unified model based on published data and authors' experimental results was suggested for describing the extraction of An(VI) (An = U, Np, Pu, Am) from HNO3 solutions into TBP solutions of various concentrations. Parallel occurrence of several extraction reactions and of nonstoichiometric physicochemical interaction of the components is assumed. The calculated parameters of the dependence of the concentration equilibrium constants on the total TBP concentration allowed expansion of the range of extractant concentrations described by the model (from 2.7 to 100%) and reduction of the uncertainty in calculation of the HNO3 and An(VI) distribution ratios. The parameter of apparent hydration of nitrate salt cations in the aqueous phase was used for describing the salting-out effect of these salts.

Transcription factor c-MYC is a potent oncoprotein; however, the mechanism of transcriptional regulation via MYC-protein interactions remains poorly understood. The TATA-binding protein (TBP) is an essential component of the transcription initiation complex TFIID and is required for gene expression. We identify two discrete regions mediating MYC-TBP interactions using structural, biochemical and cellular approaches. A 2.4 -angstrom resolution crystal structure reveals that human MYC amino acids 98-111 interact with TBP in the presence of the amino-terminal domain 1 of TBP-associated factor 1 (TAF1(TAND1)). Using biochemical approaches, we have shown that MYC amino acids 115-124 also interact with TBP independently of TAF1(TAND1). Modeling reveals that this region of MYC resembles a TBP anchor motif found in factors that regulate TBP promoter loading. Site-specific MYC mutants that abrogate MYC-TBP interaction compromise MYC activity. We propose that MYC-TBP interactions propagate transcription by modulating the energetic landscape of transcription initiation complex assembly.