Structural highlights
FunctionPublication Abstract from PubMedConformational rearrangements are critical to regulating the assembly and activity of the spliceosome. The spliceosomal protein Prp8 undergoes multiple conformational changes during the course of spliceosome assembly, activation, and catalytic activity. Most of these rearrangements of Prp8 involve the disposition of the C-terminal Jab-MPN and RH domains with respect to the core of Prp8. Here we use X-ray structural analysis to show that a previously characterized and highly conserved beta-hairpin structure in the RH domain, that acts as a toggle in the spliceosome, is absent in Prp8 from the reduced spliceosome of the red alga C. merolae. Using comparative sequence analysis, we show that the presence or absence of this hairpin corresponds to the presence or absence of protein partners that interact with this hairpin as observed by X-ray and cryo-EM studies. The presence of the toggle correlates with increasing intron number suggesting a role in the regulation of splicing. Prp8 in a Reduced Spliceosome Lacks a Conserved Toggle that Correlates with Splicing Complexity across Diverse Taxa.,Garside EL, Whelan TA, Stark MR, Rader SD, Fast NM, MacMillan AM J Mol Biol. 2019 May 9. pii: S0022-2836(19)30257-8. doi:, 10.1016/j.jmb.2019.04.047. PMID:31078556[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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