ArticleMolecular and cellular biology1999
A region within the RAP74 subunit of human transcription factor IIF is critical for initiation but dispensable for complex assembly.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 26 citations in OpenAlex.
- Mechanism of mammalian transcriptional repression by noncoding RNA.Nature structural & molecular biology · 2025Article
- Article
- Review
- Structural basis of transcription initiation by RNA polymerase II.Nature reviews. Molecular cell biology · 2015Review
- Architecture of the RNA polymerase II-TFIIF complex revealed by cross-linking and mass spectrometry.The EMBO journal · 2010Article
- Human RNA polymerase II elongation in slow motion: role of the TFIIF RAP74 alpha1 helix in nucleoside triphosphate-driven translocation.Molecular and cellular biology · 2005Article
- Amino acid substitutions in yeast TFIIF confer upstream shifts in transcription initiation and altered interaction with RNA polymerase II.Molecular and cellular biology · 2004Article
- A nonconserved surface of the TFIIB zinc ribbon domain plays a direct role in RNA polymerase II recruitment.Molecular and cellular biology · 2004Article
- Ctr9, Rtf1, and Leo1 are components of the Paf1/RNA polymerase II complex.Molecular and cellular biology · 2002Article
- The RAP74 subunit of human transcription factor IIF has similar roles in initiation and elongation.Molecular and cellular biology · 1999Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human transcription factor IIF (TFIIF) is an alpha(2)beta(2) heterotetramer of RNA polymerase II-associating 74 (RAP74) and RAP30 subunits. Mutagenic analysis shows that the N-terminal region of RAP74 between L155 (leucine at codon 155) and M177 is important for initiation. Mutants in this region have reduced activity in transcription, but none are inactive. Single amino acid substitutions at hydrophobic residues L155, W164, I176, and M177 have similar activity to RAP74(1-158), from which all but three amino acids of this region are deleted. Residual activity can be explained because each of these mutants forms a complex with RAP30 and recruits RNA polymerase II into the preinitiation complex. Mutants are defective for formation of the first phosphodiester bond from the adenovirus major late promoter but do not appear to have an additional significant defect in promoter escape. Negative DNA supercoiling partially compensates for the defects of TFIIF mutants in initiation, indicating that TFIIF may help to untwist the DNA helix for initiation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.