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Reverse transcriptases lend a hand in splicing catalysis

Nature Structural & Molecular Biology volume 23, pages 507–509 (2016)Cite this article

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The first high-resolution views of group II intron maturases illuminate the architectural and functional roles of these multidomain proteins in splicing and DNA invasion. The maturases show striking structural and functional homology to a central protein involved in spliceosomal pre–messenger RNA splicing, thus reinforcing the idea that group II introns and the spliceosome descended from a common ancestor.

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Figure 1: Comparison of domain architecture of group II IEPs and Prp8.
Figure 2: Comparison of RT and RT-like domains from R.i., LtrA and Prp8.
Figure 3: Spatial relationship of the thumb domain and RNA active site in the group II intron RNP and spliceosome.

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Authors and Affiliations

  1. Joseph A. Piccirilli is at the Department of Biochemistry and Molecular Biology, and the Department of Chemistry, University of Chicago, Chicago, Illinois, USA.,

    Joseph A Piccirilli

  2. Jonathan P. Staley is at the Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, Illinois, USA.,

    Jonathan P Staley

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  1. Joseph A Piccirilli
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  2. Jonathan P Staley
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Correspondence to Joseph A Piccirilli or Jonathan P Staley.

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Piccirilli, J., Staley, J. Reverse transcriptases lend a hand in splicing catalysis. Nat Struct Mol Biol 23, 507–509 (2016). https://doi.org/10.1038/nsmb.3242

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