Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
BLM, the protein product of the gene mutated in Bloom syndrome, is one of five human RecQ helicases. It functions to separate double Holliday junction DNA without genetic exchange as a component of the "dissolvasome," which also includes topoisomerase IIIalpha and the RMI (RecQ-mediated genome instability) subcomplex (RMI1 and RMI2). We describe the crystal structure of the RMI core complex, comprising RMI2 and the C-terminal OB domain of RMI1. The overall RMI core structure strongly resembles two-thirds of the trimerization core of the eukaryotic single-stranded DNA-binding protein, Replication Protein A. Immunoprecipitation experiments with RMI2 variants confirm key interactions that stabilize the RMI core interface. Disruption of this interface leads to a dramatic increase in cellular sister chromatid exchange events similar to that seen in BLM-deficient cells. The RMI core interface is therefore crucial for BLM dissolvasome assembly and may have additional cellular roles as a docking hub for other proteins.
Structure and cellular roles of the RMI core complex from the bloom syndrome dissolvasome.,Hoadley KA, Xu D, Xue Y, Satyshur KA, Wang W, Keck JL Structure. 2010 Sep 8;18(9):1149-58. PMID:20826341[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hoadley KA, Xu D, Xue Y, Satyshur KA, Wang W, Keck JL. Structure and cellular roles of the RMI core complex from the bloom syndrome dissolvasome. Structure. 2010 Sep 8;18(9):1149-58. PMID:20826341 doi:10.1016/j.str.2010.06.009
