Concerted Effects of Two Activator Modules on the Group I Ribozyme Reaction

Abstract

Group I intron ribozymes have a modular architecture and structural elements essential for catalysis. The elements are located in the conserved modular domain P3–P7 that is stabilized by another conserved module, P4–P6. It has been reported that artificial modules can complement the function of the native P4–P6. To exploit the modular architecture of group I ribozyme, we have constructed a hybrid ribozyme by attaching an artificial activator module to the wild-type T4 td ribozyme. Kinetic analysis of the hybrid ribozyme revealed that the artificial module and P4–P6 have unusual positive and negative concerted effects in activating the ribozyme.