Crystal structures of a group II intron maturase reveal a missing link in spliceosome evolution.

Publication Type:

Journal Article


Nat Struct Mol Biol, Volume 23, Issue 6, p.558-65 (2016)


Bacterial Proteins, Clostridiales, Crystallography, X-Ray, Introns, Models, Molecular, Protein Domains, Protein Multimerization, RNA, Bacterial, RNA, Ribosomal, Self-Splicing, RNA-Directed DNA Polymerase, Spliceosomes


<p>Group II introns are self-splicing ribozymes that are essential in many organisms, and they have been hypothesized to share a common evolutionary ancestor with the spliceosome. Although structural similarity of RNA components supports this connection, it is of interest to determine whether associated protein factors also share an evolutionary heritage. Here we present the crystal structures of reverse transcriptase (RT) domains from two group II intron-encoded proteins (maturases) from Roseburia intestinalis and Eubacterium rectale, obtained at 1.2-Å and 2.1-Å resolution, respectively. These domains are more similar in architecture to the spliceosomal Prp8 RT-like domain than to any other RTs, and they share substantial similarity with flaviviral RNA polymerases. The RT domain itself is sufficient for binding intron RNA with high affinity and specificity, and it is contained within an active RT enzyme. These studies provide a foundation for understanding structure-function relationships within group II intron-maturase complexes.</p>

5HHJ (native R.i. RT in space group P21), PDB 5HHK (Se-Met R.i. RT in space group P21), PDB 5IRF (native R.i. RT in space group P1), PDB 5IRG (Se-Met R.i. RT in space group P212121) and PDB 5HHL (native E.r. RT in space group P21)