The group II intron maturase: a reverse transcriptase and splicing factor go hand in hand.

Publication Type:

Journal Article


Curr Opin Struct Biol, Volume 47, p.30-39 (2017)


Biological Evolution, Introns, Models, Molecular, Nucleic Acid Conformation, Protein Binding, Protein Conformation, Protein Multimerization, RNA Splicing, RNA Splicing Factors, RNA-Directed DNA Polymerase, Structure-Activity Relationship


<p>The splicing of group II introns in vivo requires the assistance of a multifunctional intron encoded protein (IEP, or maturase). Each IEP is also a reverse-transcriptase enzyme that enables group II introns to behave as mobile genetic elements. During splicing or retro-transposition, each group II intron forms a tight, specific complex with its own encoded IEP, resulting in a highly reactive holoenzyme. This review focuses on the structural basis for IEP function, as revealed by recent crystal structures of an IEP reverse transcriptase domain and cryo-EM structures of an IEP-intron complex. These structures explain how the same IEP scaffold is utilized for intron recognition, splicing and reverse transcription, while providing a physical basis for understanding the evolutionary transformation of the IEP into the eukaryotic splicing factor Prp8.</p>