Linking the branchpoint helix to a newly found receptor allows lariat formation by a group II intron.

ABSTRACT: Like spliceosomal introns, the ribozyme-containing group II introns are excised as branched, lariat structures: a 2'-5' bond is created between the first nucleotide of the intron and an adenosine in domain VI, a component which is missing from available crystal structures of the ribozyme. Comparative sequence analysis, modelling and nucleotide substitutions point to the existence, and probable location, of a specific RNA receptor for the section of domain VI that lies just distal to the branchpoint adenosine. By designing oligonucleotides that tether domain VI to this novel binding site, we have been able to specifically activate lariat formation in an engineered, defective group II ribozyme. The location of the newly identified receptor implies that prior to exon ligation, the distal part

SUBMITTER: Li CF 

PROVIDER: S-EPMC3160188 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature