Vanathi, Perumal ; Mishra, Anurag Kumar ; Bhargava, Purnima (2003) Regulation of activity of the yeast TATA-binding protein through intra-molecular interactions Journal of Biosciences, 28 (4). pp. 413-421. ISSN 0250-5991
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Official URL: http://www.ias.ac.in/jbiosci/jun2003/413.pdf
Related URL: http://dx.doi.org/10.1007/BF02705116
Abstract
Dimerization is proposed to be a regulatory mechanism for TATA-binding protein (TBP) activity bothin vitro andin vivo. The reversible dimer-monomer transition of TBP is influenced by the buffer conditionsin vitro. Usingin vitro chemical cross-linking, we found yeast TBP (yTBP) to be largely monomeric in the presence of the divalent cation Mg2+, even at high salt concentrations. Apparent molecular mass of yTBP at high salt with Mg2+, run through a gel filtration column, was close to that of monomeric yTBP. Lowering the monovalent ionic concentration in the absence of Mg2+, resulted in dimerization of TBP. Effect of Mg2+ was seen at two different levels: at higher TBP concentrations, it suppressed the TBP dimerization and at lower TBP levels, it helped keep TBP monomers in active conformation (competent for binding TATA box), resulting in enhanced TBP-TATA complex formation in the presence of increasing Mg2+. At both the levels, activity of the full-length TBP in the presence of Mg2+ was like that reported for the truncated C-terminal domain of TBP from which the N-terminus is removed. Therefore for full-length TBP, intra-molecular interactions can regulate its activity via a similar mechanism.
Item Type: | Article |
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Source: | Copyright of this article belongs to Indian Academy of Sciences. |
Keywords: | Chemical Cross-linking; Dimerization; Gene Regulation; TBP; Transcription; Yeast |
ID Code: | 60011 |
Deposited On: | 08 Sep 2011 10:12 |
Last Modified: | 18 May 2016 10:21 |
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