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Inhibition of RNA Helicase Brr2 by the C-Terminal Tail of the Spliceosomal Protein Prp8

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Science  05 Jul 2013:
Vol. 341, Issue 6141, pp. 80-84
DOI: 10.1126/science.1237515

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Spliceosome Helicase

Introns are removed from eukaryotic premessenger RNA by the spliceosome. The spliceosome is assembled and disassembled during the course of each splicing reaction, and the RNA-protein remodeling involved is carried out by RNA helicases, whose activities must be closely regulated. Mozaffari-Jovin et al. (p. 80, published online 23 May) determined the crystal structure of the human Brr helicase in complex with the Jab1 domain of the Prp1 spliceosomal protein. The C-terminal tail of the Prp8 Jab1 domain inserts into the RNA-binding tunnel of Brr2, disrupting interaction of the RNA with the conserved helicase motifs inside tunnel. The temporal regulation of Brr2 RNA-binding and adenosine triphosphatase activity likely avoids premature disassembly of structures required during the splicing reaction.

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