ArticleBMC molecular biology2010
The YEATS family member GAS41 interacts with the general transcription factor TFIIF.
Article in BMC molecular biology, 2010. 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, 15 citations in OpenAlex.
- GAS41 modulates ferroptosis by anchoring NRF2 on chromatin.Nature communications · 2024Article
- Histone H3 lysine 27 crotonylation mediates gene transcriptional repression in chromatin.Molecular cell · 2023Article
- Mechanistic insights into genomic structure and functions of a novel oncogene YEATS4.Frontiers in cell and developmental biology · 2023Review
- Multifaceted roles of YEATS domain-containing proteins and novel links to neurological diseases.Cellular and molecular life sciences : CMLS · 2022Review
- The histone variant H2A.Z in gene regulation.Epigenetics & chromatin · 2019Review
- YEATS4 promotes the tumorigenesis of pancreatic cancer by activating beta-catenin/TCF signaling.Oncotarget · 2017Article
- YEATS domain: Linking histone crotonylation to gene regulation.Transcription · 2017Article
- Super elongation complex contains a TFIIF-related subcomplex.Transcription · 2016Article
- Knockdown of YEATS4 inhibits colorectal cancer cell proliferation and induces apoptosis.American journal of translational research · 2015Article
- GAS41 amplification results in overexpression of a new spindle pole protein.Genes, chromosomes & cancer · 2012Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundIn eukaryotes the transcription initiation by RNA polymerase II requires numerous general and regulatory factors including general transcription factors. The general transcription factor TFIIF controls the activity of the RNA polymerase II both at the initiation and elongation stages. The glioma amplified sequence 41 (GAS41) has been associated with TFIIF via its YEATS domain.
resultsUsing GST pull-down assays, we demonstrated that GAS41 binds to both, the small subunit (RAP30) and the large subunit (RAP74) of TFIIF in vitro. The in vivo interaction of GAS41 and endogenous RAP30 and RAP74 was confirmed by co-immunoprecipitation. GAS41 binds to two non-overlapping regions of the C-terminus of RAP30. There is also an ionic component to the binding between GAS41 and RAP30. There was no evidence for a direct interaction between GAS41 and TBP or between GAS41 and RNA polymerase II.
conclusionsOur results demonstrate binding between endogenous GAS41 and the endogenous TFIIF subunits (RAP30 and RAP74). Since we did not find evidence for a binding of GAS41 to TBP or RNA polymerase II, GAS41 seems to preferentially bind to TFIIF. GAS41 that does not contain a DNA-binding domain appears to be a co-factor of TFIIF.
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