ArticleThe Journal of biological chemistry2009
Minimal promoter systems reveal the importance of conserved residues in the B-finger of human transcription factor IIB.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- TFIIB is only ∼9 Å away from the 5'-end of a trimeric RNA primer in a functional RNA polymerase II preinitiation complex.PloS one · 2015Article
- Transcription initiation factor IIB involves in Schwann cell differentiation after rat sciatic nerve crush.Journal of molecular neuroscience : MN · 2013Article
- Evidence that RNA polymerase II and not TFIIB is responsible for the difference in transcription initiation patterns between Saccharomyces cerevisiae and Schizosaccharomyces pombe.Nucleic acids research · 2012Article
- Architecture of the yeast RNA polymerase II open complex and regulation of activity by TFIIF.Molecular and cellular biology · 2012Article
- Transcription factor TFIIF is not required for initiation by RNA polymerase II, but it is essential to stabilize transcription factor TFIIB in early elongation complexes.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The linker domain of basal transcription factor TFIIB controls distinct recruitment and transcription stimulation functions.Nucleic acids research · 2011Article
- The TFIIB tip domain couples transcription initiation to events involved in RNA processing.The Journal of biological chemistry · 2010Article
- The C53/C37 subcomplex of RNA polymerase III lies near the active site and participates in promoter opening.The Journal of biological chemistry · 2010Article
- Revealing the functions of TFIIB.TranscriptionArticle
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The "B-finger" of transcription factor IIB (TFIIB) is highly conserved and believed to play a role in the initiation process. We performed alanine substitutions across the B-finger of human TFIIB, made change-of-charge mutations in selected residues, and substituted the B-finger sequence from other organisms. Mutant proteins were examined in two minimal promoter systems (containing only RNA polymerase II, TATA-binding protein, and TFIIB) and in a complex system, using TFIIB-immunodepleted HeLa cell nuclear extract (NE). Mutations in conserved residues located on the sides of the B-finger had the greatest effect on activity in both minimal promoter systems, with mutations in residues Glu-51 and Arg-66 eliminating activity. The double change-of-charge mutant (E51R:R66E) did not show activity in either minimal promoter system. Mutations in the nonconserved residues at the tip of the B-finger did not significantly affect activity. However, all of the mutations in the B-finger showed at least 25% activity in the HeLa cell NE. Chimeric proteins, containing B-finger sequences from species with conserved residues on the side of the B-finger, showed wild-type activity in a minimal promoter system and in the HeLa cell NE. However, chimeric proteins whose sequence showed divergence on the sides of the B-finger had reduced activity. Transcription factor IIF (TFIIF) partially restored activity of the inactive mutants in the minimal promoter system, suggesting that TFIIF in HeLa cell NE helps to rescue the inactive mutations by interacting with either the B-finger or another component of the initiation complex that is influenced by the B-finger.
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