ArticleNucleic acids research2009
Characterization of RNA aptamers that disrupt the RUNX1-CBFbeta/DNA complex.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- RUNX1 deficiency cooperates with SRSF2 mutation to induce multilineage hematopoietic defects characteristic of MDS.Blood advances · 2022Article
- Review
- Aptamers: Uptake mechanisms and intracellular applications.Advanced drug delivery reviews · 2018Review
- Characterisation of an aptamer against the Runt domain of AML1 (RUNX1) by NMR and mutational analyses.FEBS open bio · 2018Article
- The SMAD3 transcription factor binds complex RNA structures with high affinity.Nucleic acids research · 2017Article
- Anti-Transcription Factor RNA Aptamers as Potential Therapeutics.Nucleic acid therapeutics · 2016Review
- Automated physics-based design of synthetic riboswitches from diverse RNA aptamers.Nucleic acids research · 2016Article
- Instruction of haematopoietic lineage choices, evolution of transcriptional landscapes and cancer stem cell hierarchies derived from an AML1-ETO mouse model.EMBO molecular medicine · 2013Article
- The Runt domain of AML1 (RUNX1) binds a sequence-conserved RNA motif that mimics a DNA element.RNA (New York, N.Y.) · 2013Article
- Article
- Toggled RNA aptamers against aminoglycosides allowing facile detection of antibiotics using gold nanoparticle assays.Analytical chemistry · 2012Article
- Functional binding of hexanucleotides to 3C protease of hepatitis A virus.Nucleic acids research · 2012Article
- A SELEX-screened aptamer of human hepatitis B virus RNA encapsidation signal suppresses viral replication.PloS one · 2011Article
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Authors and funding
7 authors.
Funding
Abstract
The transcription factor RUNX1 (AML1) is an important regulator of haematopoiesis, and an important fusion partner in leukaemic translocations. High-affinity DNA binding by RUNX1 requires the interaction of the RUNX1 Runt-Homology-Domain (RHD) with the core-binding factor beta protein (CBFbeta). To generate novel reagents for in vitro and in vivo studies of RUNX1 function, we have selected high-affinity RNA aptamers against a recombinant RHD-CBFbeta complex. Selection yielded two sequence families, each dominated by a single consensus sequence. Aptamers from each family disrupt DNA binding by the RUNX1 protein in vitro and compete with sequence-specific dsDNA binding. Minimal, high-affinity ( approximately 100-160 nM) active aptamer fragments 28 and 30 nts in length, consisting of simple short stem-loop structures, were then identified. These bind to the RHD subunit and disrupt its interaction with CBFbeta, which is consistent with reduced DNA affinity in the presence of aptamer. These aptamers represent new reagents that target a novel surface on the RHD required to stabilize the recombinant RHD-CBFbeta complex and thus will further aid exploring the functions of this key transcription factor.
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Registered trials
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