Mol._Cell._Biol.-2002-Buratowski-8735-43.pdf (427.89 kB)
Interdependent interactions between TFIIB, TATA binding protein, and DNA.
journal contribution
posted on 2023-06-07, 19:23 authored by Robin M Buratowski, Jessica Downs, Stephen BuratowskiTemperature-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.
History
Publication status
- Published
File Version
- Published version
Journal
Molecular and Cellular BiologyISSN
0270-7306External DOI
Issue
24Volume
22Page range
8735-8743Pages
9.0Department affiliated with
- Sussex Centre for Genome Damage Stability Publications
Notes
More than half of the figures were generated by me, and I had a great deal of input into both the dirrection and the interpretation of the project.Full text available
- Yes
Peer reviewed?
- Yes
Legacy Posted Date
2012-02-06First Open Access (FOA) Date
2016-03-22First Compliant Deposit (FCD) Date
2016-11-03Usage metrics
Categories
No categories selectedKeywords
Licence
Exports
RefWorks
BibTeX
Ref. manager
Endnote
DataCite
NLM
DC