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Interdependent Interactions between TFIIB, TATA Binding Protein, and DNA

机译：TFIIB，TATA结合蛋白和DNA之间的相互依赖相互作用

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Temperature-sensitive mutants of TFIIB that are defective for essential interactions were isolated. One mutation (G204D) results in disruption of a protein-protein contact between TFIIB and TATA binding protein (TBP), while the other (K272I) disrupts an interaction between TFIIB and DNA. The TBP gene was mutagenized, and alleles that suppress the slow-growth phenotypes of the TFIIB mutants were isolated. TFIIB with the G204D mutation [TFIIB(G204D)] was suppressed by hydrophobic substitutions at lysine 239 of TBP. These changes led to increased affinity between TBP and TFIIB. TFIIB(K272I) was weakly suppressed by TBP mutants in which K239 was changed to hydrophobic residues. However, this mutant TFIIB was strongly suppressed by conservative substitutions in the DNA binding surface of TBP. Biochemical characterization showed that these TBP mutants had increased affinity for a TATA element. The TBPs with increased affinity could not suppress TFIIB(G204D), leading us to propose a two-step model for the interaction between TFIIB and the TBP-DNA complex.
机译：分离出对于必需相互作用有缺陷的TFILB的温度敏感突变体。一个突变（G204D）导致TFIIB和TATA结合蛋白（TBP）之间的蛋白质-蛋白质接触破坏，而另一个（K272I）破坏TFIIB和DNA之间的相互作用。诱变了TBP基因，并分离了抑制TFIIB突变体缓慢生长表型的等位基因。具有T204B突变的TFIIB [TFIIB（G204D）]被TBP赖氨酸239处的疏水取代所抑制。这些变化导致TBP和TFIIB之间的亲和力增加。 TFIIB（K272I）被TBP突变体弱抑制，其中K239变为疏水残基。然而，该突变体TFIIB被TBP的DNA结合表面中的保守取代强烈抑制。生化特征表明，这些TBP突变体对TATA元件的亲和力增加。具有增加的亲和力的TBP不能抑制TFIBB（G204D），从而导致我们提出了TFBIB和TBP-DNA复合物之间相互作用的两步模型。

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