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Structure-based Insights into Self-Cleavage by a Four-way Junctional Twister-Sister Ribozyme

  • [设施]:上海设施
  • [期刊/会议名称]:Nature Communication
  • [摘要]:Here we report on the crystal structure and cleavage assays of a four-way junctional twistersister self-cleaving ribozyme. Notably, 11 conserved spatially separated loop nucleotides are brought into close proximity at the ribozyme core through long-range interactions mediated by hydrated Mg2+ cations. The C62–A63 step at the cleavage site adopts a splayed-apart orientation, with flexible C62 directed outwards, whereas A63 is directed inwards and anchored by stacking and hydrogen-bonding interactions. Structure-guided studies of key base, sugar, and phosphate mutations in the twister-sister ribozyme, suggest contributions to the cleavage chemistry from interactions between a guanine at the active site and the nonbridging oxygen of the scissile phosphate, a feature found previously also for the related twister ribozyme. Our four-way junctional pre-catalytic structure differs significantly in the alignment at the cleavage step (splayed-apart vs. base-stacked) and surrounding residues and hydrated Mg2+ ions relative to a reported three-way junctional pre-catalytic structure of the twister-sister ribozyme.
  • [发表日期]:2017
  • [第一作者]:郑路倩
  • [第一作者单位]:浙江大学
  • [通讯作者]:任艾明
  • [通讯作者单位]:浙江大学
  • [论文类型]:0
  • [期刊分类]:SCI1区
  • [学科分类]:生物学_ 生物化学
  • [影响因子]:12.124
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