ArticleNucleic acids research2001
Highly conserved amino acids in Pax and Ets proteins are required for DNA binding and ternary complex assembly.
Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 39 citations in OpenAlex.
- A novel stroma-dependent leukemia cell line from a patient with mixed-phenotype acute leukemia with Ph chromosome and PAX5 mutation.International journal of hematology · 2025Article
- ETS1 Function in Leukemia and Lymphoma.Advances in experimental medicine and biology · 2024Review
- EGL-38/Pax coordinates development in the Caenhorhabditis elegans egg-laying system through EGF pathway dependent and independent functions.Mechanisms of development · 2019Article
- De Novo Mutations in EBF3 Cause a Neurodevelopmental Syndrome.American journal of human genetics · 2017Article
- Understanding the role of ETS-mediated gene regulation in complex biological processes.Advances in cancer research · 2013Review
- Disentangling the many layers of eukaryotic transcriptional regulation.Annual review of genetics · 2012Review
- Histone acetyltransferase p300 acetylates Pax5 and strongly enhances Pax5-mediated transcriptional activity.The Journal of biological chemistry · 2011Article
- Genomic and biochemical insights into the specificity of ETS transcription factors.Annual review of biochemistry · 2011Review
- Thrombocytopenia in mice lacking the carboxy-terminal regulatory domain of the Ets transcription factor Fli1.Molecular and cellular biology · 2010Article
- Genome-wide analysis of ETS-family DNA-binding in vitro and in vivo.The EMBO journal · 2010Article
- Highly cooperative recruitment of Ets-1 and release of autoinhibition by Pax5.Journal of molecular biology · 2009Article
- The 'zinc knuckle' motif of Early B cell Factor is required for transcriptional activation of B cell-specific genes.Molecular immunology · 2008Article
- Distinct promoters mediate the regulation of Ebf1 gene expression by interleukin-7 and Pax5.Molecular and cellular biology · 2007Article
- Requirements for selective recruitment of Ets proteins and activation of mb-1/Ig-alpha gene transcription by Pax-5 (BSAP).Nucleic acids research · 2003Article
- 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
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Combinatorial association of DNA-binding proteins on composite binding sites enhances their nucleotide sequence specificity and functional synergy. As a paradigm for these interactions, Pax-5 (BSAP) assembles ternary complexes with Ets proteins on the B cell-specific mb-1 promoter through interactions between their respective DNA-binding domains. Pax-5 recruits Ets-1 to bind the promoter, but not the closely related Ets protein SAP1a. Here we show that, while several different mutations increase binding of SAP1a to an optimized Ets binding site, only conversion of Val68 to an acidic amino acid facilitates ternary complex assembly with Pax-5 on the mb-1 promoter. This suggests that enhanced DNA binding by SAP1a is not sufficient for recruitment by Pax-5, but instead involves protein-protein interactions mediated by the acidic side chain. Recruitment of Ets proteins by Pax-5 requires Gln22 within the N-terminal beta-hairpin motif of its paired domain. The beta-hairpin also participates in recognition of a subset of Pax-5-binding sites. Thus, Pax-5 incorporates protein-protein interaction and DNA recognition functions in a single motif. The Caenorhabditis elegans Pax protein EGL-38 also binds specifically to the mb-1 promoter and recruits murine Ets-1 or the C.elegans Ets protein T08H4.3, but not the related LIN-1 protein. Together, our results define specific amino acid requirements for Pax-Ets ternary complex assembly and show that the mechanism is conserved between evolutionarily related proteins of diverse animal species. Moreover, the data suggest that interactions between Pax and Ets proteins are an important mechanism that regulates fundamental biological processes in worms and humans.
Indexed as
Identifiers
What OpenQuestion holds
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.