ArticleScientific reports2013
The proteasome factor Bag101 binds to Rad22 and suppresses homologous recombination.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- PolySUMOylation of PCNA and Rad52 restricts centromeric recombination in fission yeast.Nature communications · 2025Article
- Origin and Evolution of the Human Bcl2-Associated Athanogene-1 (BAG-1).International journal of molecular sciences · 2020Article
- DNA replication machinery prevents Rad52-dependent single-strand annealing that leads to gross chromosomal rearrangements at centromeres.Communications biology · 2020Article
- Rgf1p (Rho1p GEF) is required for double-strand break repair in fission yeast.Nucleic acids research · 2017Article
- UBL/BAG-domain co-chaperones cause cellular stress upon overexpression through constitutive activation of Hsf1.Cell stress & chaperones · 2017Article
- Protein quality control in the nucleus.Biomolecules · 2014Review
- Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although RAD52 plays a critical role in the initiation of homologous recombination (HR) by facilitating the replacement of RPA with RAD51, the mechanism controlling RAD52 remains elusive. Here, we show that Bag101, a factor implicated in proteasome functioning, regulates RAD52 protein levels and subsequent HR. LC-MS/MS analysis identified Bag101 which binds to Rad22, the fission yeast homologue of RAD52. Bag101 reduced HR frequency through its overexpression and conversely, HR frequencies were enhanced when it was deleted. Consistent with this observation, Rad22 protein levels was reduced in cells where bag101 was overexpressed even when Rad22 transcription was up-regulated, suggesting the operation of proteasome-mediated Rad22 degradation. Indeed, Rad22 protein levels were stabilized in proteasome mutants. Rad22 physically interacted with the BAG domain of Bag101, and a lack of this domain enhanced HR frequency. Similarly, radiation exposure triggered the dissociation of these proteins so that Rad22 was stabilized and able to enhance HR.
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