Structure analysis of free and bound states of an RNA aptamer against ribosomal protein S8 from Bacillus anthracis.

ABSTRACT: Several protein-targeted RNA aptamers have been identified for a variety of applications and although the affinities of numerous protein-aptamer complexes have been determined, the structural details of these complexes have not been widely explored. We examined the structural accommodation of an RNA aptamer that binds bacterial r-protein S8. The core of the primary binding site for S8 on helix 21 of 16S rRNA contains a pair of conserved base triples that mold the sugar-phosphate backbone to S8. The aptamer, which does not contain the conserved sequence motif, is specific for the rRNA binding site of S8. The protein-free RNA aptamer adopts a helical structure with multiple non-canonical base pairs. Surprisingly, binding of S8 leads to a dramatic change in the RNA conformation that restores

SUBMITTER: Davlieva M 

PROVIDER: S-EPMC4176348 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature