A kinetic and thermodynamic framework for the Azoarcus group I ribozyme reaction.

ABSTRACT: Determination of quantitative thermodynamic and kinetic frameworks for ribozymes derived from the Azoarcus group I intron and comparisons to their well-studied analogs from the Tetrahymena group I intron reveal similarities and differences between these RNAs. The guanosine (G) substrate binds to the Azoarcus and Tetrahymena ribozymes with similar equilibrium binding constants and similar very slow association rate constants. These and additional literature observations support a model in which the free ribozyme is not conformationally competent to bind G and in which the probability of assuming the binding-competent state is determined by tertiary interactions of peripheral elements. As proposed previously, the slow binding of guanosine may play a role in the specificity of group I intron

SUBMITTER: Gleitsman KR 

PROVIDER: S-EPMC4201826 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature