ArticleMolecular and cellular biology1999
Synergistic transcriptional activation by TATA-binding protein and hTAFII28 requires specific amino acids of the hTAFII28 histone fold.
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 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 22 citations in OpenAlex.
- Article
- Transcription of Nearly All Yeast RNA Polymerase II-Transcribed Genes Is Dependent on Transcription Factor TFIID.Molecular cell · 2017Article
- TFIID TAF6-TAF9 complex formation involves the HEAT repeat-containing C-terminal domain of TAF6 and is modulated by TAF5 protein.The Journal of biological chemistry · 2012Article
- A cytoplasmic negative regulator isoform of ATF7 impairs ATF7 and ATF2 phosphorylation and transcriptional activity.PloS one · 2011Article
- Article
- Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity.Nucleic acids research · 2007Article
- Functional interaction between the homeoprotein CDX1 and the transcriptional machinery containing the TATA-binding protein.Nucleic acids research · 2007Article
- Article
- Mapping and functional characterization of the TAF11 interaction with TFIIA.Molecular and cellular biology · 2005Article
- Systematic analysis of essential yeast TAFs in genome-wide transcription and preinitiation complex assembly.The EMBO journal · 2003Article
- The S. cerevisiae SAGA complex functions in vivo as a coactivator for transcriptional activation by Gal4.Genes & development · 2001Article
- TFIIA interacts with TFIID via association with TATA-binding protein and TAF40.Molecular and cellular biology · 2001Article
- Coordinate regulation of RARgamma2, TBP, and TAFII135 by targeted proteolysis during retinoic acid-induced differentiation of F9 embryonal carcinoma cells.BMC molecular biology · 2001Article
- Cloning and characterization of the histone-fold proteins YBL1 and YCL1.Nucleic acids research · 2000Article
- A single point mutation in TFIIA suppresses NC2 requirement in vivo.The EMBO journal · 2000Article
- The human TFIID components TAF(II)135 and TAF(II)20 and the yeast SAGA components ADA1 and TAF(II)68 heterodimerize to form histone-like pairs.Molecular and cellular biology · 2000Article
- The Spt components of SAGA facilitate TBP binding to a promoter at a post-activator-binding step in vivo.Genes & development · 1999Article
- Synergistic transcriptional activation by TATA-binding protein and hTAFII28 requires specific amino acids of the hTAFII28 histone fold.Molecular and cellular biology · 1999Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coexpression of the human TATA-binding protein (TBP)-associated factor 28 (hTAFII28) with the altered-specificity mutant TBP spm3 synergistically enhances transcriptional activation by the activation function 2 of the nuclear receptors (NRs) for estrogen and vitamin D3 from a reporter plasmid containing a TGTA element in mammalian cells. This synergy is abolished by mutation of specific amino acids in the alpha2-helix of the histone fold in the conserved C-terminal region of hTAFII28. Critical amino acids are found on both the exposed hydrophilic face of this helix and the hydrophobic interface with TAFII18. This alpha-helix of hTAFII28 therefore mediates multiple interactions required for coactivator activity. We further show that mutation of specific residues in the H1' alpha-helix of TBP either reduces or increases interactions with hTAFII28. The mutations which reduce interactions with hTAFII28 do not affect functional synergy, whereas the TBP mutation which increases interaction with hTAFII28 is defective in its ability to synergistically enhance activation by NRs. However, this TBP mutant supports activation by other activators and is thus specifically defective for its ability to synergize with hTAFII28.
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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.