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10.1093/nar/gkv361

http://scihub22266oqcxt.onion/10.1093/nar/gkv361
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C4482088!4482088!25897130
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suck abstract from ncbi


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pmid25897130      Nucleic+Acids+Res 2015 ; 43 (9): 4614-26
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  • BLM unfolds G-quadruplexes in different structural environments through different mechanisms #MMPMID25897130
  • Wu WQ; Hou XM; Li M; Dou SX; Xi XG
  • Nucleic Acids Res 2015[May]; 43 (9): 4614-26 PMID25897130show ga
  • Mutations in the RecQ DNA helicase gene BLM give rise to Bloom's syndrome, which is a rare autosomal recessive disorder characterized by genetic instability and cancer predisposition. BLM helicase is highly active in binding and unwinding G-quadruplexes (G4s), which are physiological targets for BLM, as revealed by genome-wide characterizations of gene expression of cells from BS patients. With smFRET assays, we studied the molecular mechanism of BLM-catalyzed G4 unfolding and showed that ATP is required for G4 unfolding. Surprisingly, depending on the molecular environments of G4, BLM unfolds G4 through different mechanisms: unfolding G4 harboring a 3?-ssDNA tail in three discrete steps with unidirectional translocation, and unfolding G4 connected to dsDNA by ssDNA in a repetitive manner in which BLM remains anchored at the ss/dsDNA junction, and G4 was unfolded by reeling in ssDNA. This indicates that one BLM molecule may unfold G4s in different molecular environments through different mechanisms.
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