Article
The exocyclic amine at the RNase P cleavage site contributes to substrate binding and catalysis.
Journal of molecular biology - 9 Jun 2006
Kikovska Ema, Brännvall Mathias, Kirsebom Leif A
Abstract excerpt
Most tRNAs carry a G at their 5' termini, i.e. at position +1. This position corresponds to the position immediately downstream of the site of cleavage in tRNA precursors. Here we studied RNase P RNA-mediated cleavage of substrates carrying substitutions/modifications at position +1 in the absence of the RNase P protein, C5, to investigate the role of G at the RNase P cleavage site. We present data suggesting...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.