ArticleBiochemistry2007
Biochemical characterization of a SET and transposase fusion protein, Metnase: its DNA binding and DNA cleavage activity.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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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Who cites it
32 citing papers in PubMed, 47 citations in OpenAlex.
- DNA binding and transposition activity of the Sleeping Beauty transposase: role of structural stability of the primary DNA-binding domain.Nucleic acids research · 2025Article
- Structural and genome-wide analyses suggest that transposon-derived protein SETMAR alters transcription and splicing.The Journal of biological chemistry · 2022Article
- SETMAR, a case of primate co-opted genes: towards new perspectives.Mobile DNA · 2022Review
- Metnase and EEPD1: DNA Repair Functions and Potential Targets in Cancer Therapy.Frontiers in oncology · 2022Review
- Role of the DNA Binding Activity of Herpes Simplex Virus 1 VP22 in Evading AIM2-Dependent Inflammasome Activation Induced by the Virus.Journal of virology · 2021Article
- Distinct roles of structure-specific endonucleases EEPD1 and Metnase in replication stress responses.NAR cancer · 2020Article
- The roles of the human SETMAR (Metnase) protein in illegitimate DNA recombination and non-homologous end joining repair.DNA repair · 2019Article
- Transcriptionally promiscuous "blurry" promoters in Tc1/Mobile DNA · 2019Article
- A single active site in the mariner transposase cleaves DNA strands of opposite polarity.Nucleic acids research · 2017Article
- Article
- Metnase Mediates Loading of Exonuclease 1 onto Single Strand Overhang DNA for End Resection at Stalled Replication Forks.The Journal of biological chemistry · 2017Article
- Crystallization of and selenomethionine phasing strategy for a SETMAR-DNA complex.Acta crystallographica. Section F, Structural biology communications · 2016Article
- hPso4/hPrp19: a critical component of DNA repair and DNA damage checkpoint complexes.Oncogene · 2016Review
- EEPD1 Rescues Stressed Replication Forks and Maintains Genome Stability by Promoting End Resection and Homologous Recombination Repair.PLoS genetics · 2015Article
- The SET Domain Is Essential for Metnase Functions in Replication Restart and the 5' End of SS-Overhang Cleavage.PloS one · 2015Article
- The DDN catalytic motif is required for Metnase functions in non-homologous end joining (NHEJ) repair and replication restart.The Journal of biological chemistry · 2014Article
- Article
- Trimming of damaged 3' overhangs of DNA double-strand breaks by the Metnase and Artemis endonucleases.DNA repair · 2013Article
- Targeting the transposase domain of the DNA repair component Metnase to enhance chemotherapy.Cancer research · 2012Article
- Biochemical characterization of metnase's endonuclease activity and its role in NHEJ repair.Biochemistry · 2011Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Metnase (SETMAR) is a SET and transposase fusion protein that promotes in vivo end joining activity and mediates genomic integration of foreign DNA. Recent studies showed that Metnase retained most of the transposase activities, including 5'-terminal inverted repeat (TIR)-specific binding and assembly of a paired end complex, and cleavage of the 5'-end of the TIR element. Here we show that R432 within the helix-turn-helix motif is critical for sequence-specific recognition, as the R432A mutation abolishes its TIR-specific DNA binding activity. Metnase possesses a unique DNA nicking and/or endonuclease activity that mediates cleavage of duplex DNA in the absence of the TIR sequence. While the HTH motif is essential for the Metnase-TIR interaction, it is not required for its DNA cleavage activity. The DDE-like motif is crucial for its DNA cleavage action as a point mutation at this motif (D483A) abolished its DNA cleavage activity. Together, our results suggest that Metnase's DNA cleavage activity, unlike those of other eukaryotic transposases, is not coupled to its sequence-specific DNA binding.
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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.