ArticleChromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology2017
The long zinc finger domain of PRDM9 forms a highly stable and long-lived complex with its DNA recognition sequence.
Article in Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology, 2017. 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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13 citing papers in PubMed, 24 citations in OpenAlex.
- Structure and RNA-binding of the helically extended Roquin CCCH-type zinc finger.Nucleic acids research · 2024Article
- Bridging the gap between the evolutionary dynamics and the molecular mechanisms of meiosis: A model based exploration of the PRDM9 intra-genomic Red Queen.PLoS genetics · 2024Article
- Decorating chromatin for enhanced genome editing using CRISPR-Cas9.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Evolution of the recombination regulator PRDM9 in minke whales.BMC genomics · 2022Article
- HELLS and PRDM9 form a pioneer complex to open chromatin at meiotic recombination hot spots.Genes & development · 2020Article
- Identification of a TRBD zinc finger-interacting protein in Giardia duodenalis and its regulation of telomerase.Parasites & vectors · 2019Article
- PRDM9 forms a trimer by interactions within the zinc finger array.Life science alliance · 2019Article
- PRDM9, a driver of the genetic map.PLoS genetics · 2018Review
- The consequences of sequence erosion in the evolution of recombination hotspots.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- The impact of recombination on human mutation load and disease.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Article
- Genomic and chromatin features shaping meiotic double-strand break formation and repair in mice.Cell cycle (Georgetown, Tex.) · 2017Article
- Structural basis of human PR/SET domain 9 (PRDM9) allele C-specific recognition of its cognate DNA sequence.The Journal of biological chemistry · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PR domain containing protein 9 (PRDM9) is a meiosis-specific, multi-domain protein that regulates the location of recombination hotspots by targeting its DNA recognition sequence for double-strand breaks (DSBs). PRDM9 specifically recognizes DNA via its tandem array of zinc fingers (ZnFs), epigenetically marks the local chromatin by its histone methyltransferase activity, and is an important tether that brings the DNA into contact with the recombination initiation machinery. A strong correlation between PRDM9-ZnF variants and specific DNA motifs at recombination hotspots has been reported; however, the binding specificity and kinetics of the ZnF domain are still obscure. Using two in vitro methods, gel mobility shift assays and switchSENSE, a quantitative biophysical approach that measures binding rates in real time, we determined that the PRDM9-ZnF domain forms a highly stable and long-lived complex with its recognition sequence, with a dissociation halftime of many hours. The ZnF domain exhibits an equilibrium dissociation constant (K
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