ArticleArchives of biochemistry and biophysics2010
Regulation of Metnase's TIR binding activity by its binding partner, Pso4.
Article in Archives of biochemistry and biophysics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- SETMAR, a case of primate co-opted genes: towards new perspectives.Mobile DNA · 2022Review
- New Faces of old Friends: Emerging new Roles of RNA-Binding Proteins in the DNA Double-Strand Break Response.Frontiers in molecular biosciences · 2021Review
- The splicing component ISY1 regulates APE1 in base excision repair.DNA repair · 2020Article
- SETMAR isoforms in glioblastoma: A matter of protein stability.Oncotarget · 2017Article
- Ubiquitous overexpression of the DNA repair factorNPJ aging and mechanisms of disease · 2017Article
- hPso4/hPrp19: a critical component of DNA repair and DNA damage checkpoint complexes.Oncogene · 2016Review
- Cross talk of tyrosine kinases with the DNA damage signaling pathways.Nucleic acids research · 2015Review
- The SET Domain Is Essential for Metnase Functions in Replication Restart and the 5' End of SS-Overhang Cleavage.PloS one · 2015Article
- Targeting the transposase domain of the DNA repair component Metnase to enhance chemotherapy.Cancer research · 2012Article
- Tethering of the conserved piggyBac transposase fusion protein CSB-PGBD3 to chromosomal AP-1 proteins regulates expression of nearby genes in humans.PLoS genetics · 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
4 authors at 3 institutions in 1 country.
Funding
Abstract
Metnase (also known as SETMAR) is a SET and transposase fusion protein in humans and plays a positive role in double-strand break (DSB) repair. While the SET domain possesses histone lysine methyltransferase activity, the transposase domain is responsible for 5'-terminal inverted repeat (TIR)-specific binding, DNA looping, and DNA cleavage activities. We recently demonstrated that human homolog of Pso4 (hPso4) is a Metnase binding partner that mediates Metnase binding to non-TIR DNA such as DNA damage sites. Here we show that Metnase functions as a dimer in its TIR binding. While both Metnase and hPso4 can independently interact with TIR DNA, Metnase's DNA binding activity is not required for formation of the Metnase-hPso4-DNA complex. A further stoichiometric analysis indicated that only one protein is involved in interaction with dsDNA when Metnase-hPso4 forms a stable complex. Interaction of the Metnase-hPso4 complex with TIR DNA was competitively inhibited by both TIR and non-TIR DNA, suggesting that hPso4 is solely responsible for binding to DNA in the Metnase-hPso4-DNA complex. Together, our study suggests that hPso4, once it forms a complex with Metnase, negatively regulates Metnase's TIR binding activity, which is perhaps necessary for Metnase localization at non-TIR sites such as DSBs.
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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.