Self-association of the Amino-terminal Domain of the Yeast TATA-binding Protein

Claire A. Adams, Sambit R. Kar, James E. Hopper, Michael G. Fried

Research output: Contribution to journalArticlepeer-review

8 Scopus citations


The amino-terminal domain of yeast TATA-binding protein has been proposed to play a crucial role in the self-association mechanism(s) of the full-length protein. Here we tested the ability of this domain to self-associate under a variety of solution conditions. Escherichia coli two-hybrid assays, in vitro pull-down assays, and in vitro cross-linking provided qualitative evidence for a limited and specific self-association. Sedimentation equilibrium analysis using purified protein was consistent with a monomer-dimer equilibrium with an apparent dissociation constant of ∼8.4 μM. Higher stoichiometry associations remain possible but could not be detected by any of these methods. These results demonstrate that the minimal structure necessary for amino-terminal domain self-association must be present even in the absence of carboxyl-terminal domain structures. On the basis of these results we propose that amino-terminal domain structures contribute to the oligomerization interface of the full-length yeast TATA-binding protein.

Original languageEnglish
Pages (from-to)1376-1382
Number of pages7
JournalJournal of Biological Chemistry
Issue number2
StatePublished - Jan 9 2004

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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