ArticleNucleic acids research1997
The ETS family member ERM contains an alpha-helical acidic activation domain that contacts TAFII60.
Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 39 citations in OpenAlex.
- Multivalent and Bidirectional Binding of Transcriptional Transactivation Domains to the MED25 Coactivator.Biomolecules · 2020Article
- Complementary Activity of ETV5, RBPJ, and TCF3 Drives Formative Transition from Naive Pluripotency.Cell stem cell · 2019Article
- Characterization of ERM transactivation domain binding to the ACID/PTOV domain of the Mediator subunit MED25.Nucleic acids research · 2015Article
- The Mediator complex subunit MED25 is targeted by the N-terminal transactivation domain of the PEA3 group members.Nucleic acids research · 2013Article
- The possible functions of duplicated ets (GGAA) motifs located near transcription start sites of various human genes.Cellular and molecular life sciences : CMLS · 2011Article
- A small ubiquitin-related modifier-interacting motif functions as the transcriptional activation domain of Krüppel-like factor 4.The Journal of biological chemistry · 2010Article
- The E3 ubiquitin ligase complex component COP1 regulates PEA3 group member stability and transcriptional activity.Oncogene · 2010Article
- Transactivation, dimerization, and DNA-binding activity of white spot syndrome virus immediate-early protein IE1.Journal of virology · 2008Article
- The 26S proteasome system degrades the ERM transcription factor and regulates its transcription-enhancing activity.Oncogene · 2007Article
- Analysis of transcriptional modulation of the presenilin 1 gene promoter by ZNF237, a candidate binding partner of the Ets transcription factor ERM.Brain research · 2007Article
- FEV acts as a transcriptional repressor through its DNA-binding ETS domain and alanine-rich domain.Oncogene · 2003Article
- Hepatocyte growth factor/scatter factor activates the ETS1 transcription factor by a RAS-RAF-MEK-ERK signaling pathway.Oncogene · 2002Article
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- The activity of the activation function 2 of the human hepatocyte nuclear factor 4 (HNF-4alpha) is differently modulated by F domains from various origins.The Biochemical journal · 1999Article
- Conservation and divergence of NF-Y transcriptional activation function.Nucleic acids research · 1998Article
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Authors and funding
4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Transcription factors are modular entities built up of discrete domains, some devoted to DNA binding and others permitting transcriptional modulation. The structure of DNA binding domains has been thoroughly investigated and structural classes clearly defined. In sharp contrast, the structural constraints put on transactivating regions, if any, are mostly unknown. Our investigations focus on ERM, a eukaryotic transcription factor of the ETS family. We have previously shown that ERM harbours two transactivating domains (TADs) with distinct functional features: AD1 lies in the first 72 amino acids of ERM, while AD2 sits in the last 62. Here we show that AD1 is a bona fide acidic TAD, for it activated transcription in yeast cells, while AD2 did not. AD1 contains a 20 amino acid stretch predicted to form an alpha-helix that is found unchanged in the related PEA3 and ER81 transcription factors. Circular dichroism analysis revealed that a 32 amino acid peptide encompassing this region is unstructured in water but folds into a helix when the hydrophobic solvent trifluoroethanol is added. The isolated helix was sufficient to activate transcription and mutations predicted to disrupt it dramatically affected AD1-driven transactivation, whereas mutations decreasing its acidity had more gentle effects. A phenylalanine residue within the helix was particularly sensitive to mutations. Finally, we observed that ERM bound TAFII60 via AD1 and bound TBP and TAFII40, presumably via other activation domains.
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