A role for TBP dimerization in preventing unregulated gene expression

Amy J. Jackson-Fisher, Carmelata Chitikila, Madhusmita Mitra, B. Franklin Pugh

Research output: Contribution to journalArticlepeer-review

63 Scopus citations


The recruitment of the TATA box-binding protein (TBP) to promoters in vivo is often rate limiting in gene expression. We present evidence that TBP negatively autoregulates its accessibility to promoter DNA in yeast through dimerization. The crystal structure of TBP dimers was used to design point mutations in the dimer interface. These mutants are impaired for dimerization in vitro, and in vivo they generate large increases in activator-independent gene expression. Overexpression of wild-type TBP suppresses these mutants, possibly by heterodimerizing with them. In addition to loss of autorepression, dimerization-defective TBPs are rapidly degraded in vivo. Direct detection of TBP dimers in vivo was achieved through chemical cross- linking. Taken together, the data suggest that TBP dimerization prevents unregulated gene expression and its own degradation.

Original languageEnglish (US)
Pages (from-to)717-727
Number of pages11
JournalMolecular cell
Issue number6
StatePublished - Jun 1999

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


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