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Crystal structure of Prp8 reveals active site cavity of the spliceosome

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Nature

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      Abstract

      The active centre of the spliceosome consists of an intricate network formed by U5, U2 and U6 snRNAs, and a pre-mRNA substrate. Prp8, a component of the U5 snRNP, crosslinks extensively with this RNA catalytic core. We present the crystal structure of yeast Prp8 (residues 885-2413) in complex with the U5 snRNP assembly factor Aar2. The structure reveals new tightly associated domains of Prp8 resembling a bacterial group II intron reverse transcriptase and a type II restriction endonuclease. Suppressors of splice site mutations and an intron branchpoint crosslink map to a large cavity formed by the reverse transcriptase thumb, endonuclease-like and the RNaseH-like domains. This cavity is large enough to accommodate the catalytic core of group II intron RNA. The structure provides crucial insights into the architecture of the spliceosome’s active site and reinforces the notion that nuclear pre-mRNA splicing and group II intron splicing have a common origin.

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      Author and article information

      Affiliations
      MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, England
      Author notes
      Correspondence and requests for materials should be addressed to K.N. ( kn@ 123456mrc-lmb.cam.ac.uk ) and A.J.N. ( newman@ 123456mrc-lmb.cam.ac.uk ).
      Journal
      0410462
      6011
      Nature
      Nature
      Nature
      0028-0836
      1476-4687
      19 December 2012
      23 January 2013
      31 January 2013
      31 July 2013
      : 493
      : 7434
      : 638-643
      23354046 3672837 10.1038/nature11843 EMS50962

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      Funding
      Funded by: Medical Research Council :
      Award ID: U.1051.04.016(78933) || MRC_
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