Poster abstracts
Poster number 58 submitted by Megan Van Horn
Inhibition of lariat debranching enzyme with click-branched RNA: effects of the 2'-branch and the branch-point residue
Megan Van Horn (Chemistry, Carnegie Mellon University ), Timothy Chad Ratterman (Chemistry, Carnegie Mellon University ), Stephanie Mack (Chemistry, Carnegie Mellon University ), Subha Das (Chemistry, Carnegie Mellon University )
Abstract:
During RNA splicing, lariat introns are formed via a 2’,5-phosphodiester bond, with an adenosine branch-point residue. Lariat debranching enzyme (Dbr1p) specifically cleaves the 2’,5’-phosphodiester bond in the branch-point of the lariat intron.
Previous studies in our lab have shown that Dbr1p can bind, but not cleave, branched RNAs containing an unnatural 2ʹ,5ʹ-triazole linkage at the branch-point residue generated through ‘click’ chemistry. These click-branched RNAs are competitive inhibitors of the Dbr1p cleavage reaction. Recently our lab has shown that Dbr1p can cleave backbone-branched RNAs with branch-point residues other than adenosine. Here we describe the use of click-branched RNAs with altered 2'-branch sequences and non-canonical branch-point residues to study the effects of the 2'-branch and the branch-point residue identity on the Dbr1p cleavage reaction.
Keywords: Dbr1p, E histolytica, Inhibitor