Cloning and biochemical characterization of TAF-172, a human homolog of yeast Mot1

John J. Chicca, David T. Auble, B. Franklin Pugh

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Abstract

The TATA binding protein (TBP) is a central component of the eukaryotic transcriptional machinery and is the target of positive and negative transcriptional regulators. Here we describe the cloning and biochemical characterization of an abundant human TBP-associated factor (TAF-172) which is homologous to the yeast Mot1 protein and a member of the larger Snf2/Swi2 family of DNA-targeted ATPases. Like Mot1, TAF-172 binds to the conserved core of TBP and uses the energy of ATP hydrolysis to dissociate TBP from DNA (ADI activity). Interestingly, ATP also causes TAF-172 to dissociate from TBP, which has not been previously observed with Mot1. Unlike Mot1, TAF-172 requires both TBP and DNA for maximal (~100-fold) ATPase activation. TAF- 172 inhibits TBP-driven RNA polymerase II and in transcription but does not appear to affect transcription driven by TBP-TAF complexes. As it does with Mot1, TFIIA reverses TAF-172-mediated represSion of TBP. Together, these findings suggest that human TAF-172 is the functional homolog of yeast Mot1 and uses the energy of ATP hydrolysis to remove TBP (but apparently not TBP- TAF complexes) from DNA.

Original languageEnglish (US)
Pages (from-to)1701-1710
Number of pages10
JournalMolecular and cellular biology
Volume18
Issue number3
DOIs
Publication statusPublished - Mar 1998

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All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

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