ArticleMolecular and cellular biology1999
The highly conserved beta-hairpin of the paired DNA-binding domain is required for assembly of Pax-Ets ternary complexes.
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 27 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 62 citations in OpenAlex.
- ETS1 Function in Leukemia and Lymphoma.Advances in experimental medicine and biology · 2024Review
- Establishment of the lymphoid ETS-code reveals deregulated ETS genes in Hodgkin lymphoma.PloS one · 2023Article
- Encounters across networks: Windows into principles of genomic regulation.Marine genomics · 2019Article
- Article
- FARE-CAFE: a database of functional and regulatory elements of cancer-associated fusion events.Database : the journal of biological databases and curation · 2015Article
- Molecular cloning and functional characterization of two forms of Pax8 in the rainbow trout, Oncorhynchus mykiss.General and comparative endocrinology · 2014Article
- Article
- PAX5 activates the transcription of the human telomerase reverse transcriptase gene in B cells.The Journal of pathology · 2010Article
- Highly cooperative recruitment of Ets-1 and release of autoinhibition by Pax5.Journal of molecular biology · 2009Article
- Comparative analysis of the mammalian WNT4 promoter.BMC genomics · 2009Article
- Pathogenic mechanisms of tooth agenesis linked to paired domain mutations in human PAX9.Human molecular genetics · 2009Article
- The 'zinc knuckle' motif of Early B cell Factor is required for transcriptional activation of B cell-specific genes.Molecular immunology · 2008Article
- WBP-2, a WW domain binding protein, interacts with the thyroid-specific transcription factor Pax8.The Biochemical journal · 2004Article
- WT1 is a modifier of the Pax2 mutant phenotype: cooperation and interaction between WT1 and Pax2.Oncogene · 2003Article
- The balance between Pax5 and Id2 activities is the key to AID gene expression.The Journal of experimental medicine · 2003Article
- Requirements for selective recruitment of Ets proteins and activation of mb-1/Ig-alpha gene transcription by Pax-5 (BSAP).Nucleic acids research · 2003Article
- The biology of the Ets1 proto-oncogene.Molecular cancer · 2003Review
- Article
- Activation of the early B-cell-specific mb-1 (Ig-alpha) gene by Pax-5 is dependent on an unmethylated Ets binding site.Molecular and cellular biology · 2003Article
- Early B-cell factor, E2A, and Pax-5 cooperate to activate the early B cell-specific mb-1 promoter.Molecular and cellular biology · 2002Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Pax family transcription factors bind DNA through the paired domain. This domain, which is comprised of two helix-turn-helix motifs and a beta-hairpin structure, is a target of mutations in congenital disorders of mice and humans. Previously, we showed that Pax-5 (B-cell-specific activator protein) recruits proteins of the Ets proto-oncogene family to bind a composite DNA site that is essential for efficient transcription of the early-B-cell-specific mb-1 promoter. Here, evidence is provided for specific interactions between Ets-1 and the amino-terminal subdomains of Pax proteins. By tethering deletion fragments of Pax-5 to a heterologous DNA-binding domain, we show that 73 amino acids (amino acids 12 to 84) of its amino-terminal subdomain can recruit the ETS domain of Ets-1 to bind the composite site. Furthermore, an amino acid (Gln22) within the highly conserved beta-hairpin motif of Pax-5 is essential for efficient recruitment of Ets-1. The ability to recruit Ets proteins to bind DNA is a shared property of Pax proteins, as demonstrated by cooperative DNA binding of Ets-1 with sequences derived from the paired domains of Pax-2 and Pax-3. The strict conservation of sequences required for recruitment of Ets proteins suggests that Pax-Ets interactions are important for regulating transcription in diverse tissues during cellular differentiation.
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Registered trials
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.