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Title: Crystal structures of RMI1 and RMI2, two OB-fold regulatory subunits of the BLM complex.

Authors: Wang, Feng; Yang, Yuting; Singh, Thiyam Ramsing; Busygina, Valeria; Guo, Rong; Wan, Ke; Wang, Weidong; Sung, Patrick; Meetei, Amom Ruhikanta; Lei, Ming

Published In Structure, (2010 Sep 08)

Abstract: Mutations in BLM, a RecQ-like helicase, are linked to the autosomal recessive cancer-prone disorder Bloom's syndrome. BLM associates with topoisomerase (Topo) IIIα, RMI1, and RMI2 to form the BLM complex that is essential for genome stability. The RMI1-RMI2 heterodimer stimulates the dissolution of double Holliday junction into non-crossover recombinants mediated by BLM-Topo IIIα and is essential for stabilizing the BLM complex. However, the molecular basis of these functions of RMI1 and RMI2 remains unclear. Here we report the crystal structures of multiple domains of RMI1-RMI2, providing direct confirmation of the existence of three oligonucleotide/oligosaccharide binding (OB)-folds in RMI1-RMI2. Our structural and biochemical analyses revealed an unexpected insertion motif in RMI1N-OB, which is important for stimulating the dHJ dissolution. We also revealed the structural basis of the interaction between RMI1C-OB and RMI2-OB and demonstrated the functional importance of the RMI1-RMI2 interaction in genome stability maintenance.

PubMed ID: 20826342 Exiting the NIEHS site

MeSH Terms: Bloom Syndrome/metabolism; Carrier Proteins/chemistry*; Carrier Proteins/metabolism; Crystallography, X-Ray; DNA Topoisomerases, Type I/chemistry; DNA, Cruciform/chemistry; DNA, Cruciform/metabolism; DNA-Binding Proteins/chemistry*; DNA-Binding Proteins/metabolism; Genomic Instability; Humans; Nuclear Proteins/chemistry*; Nuclear Proteins/metabolism; Protein Folding; Protein Subunits

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