Efficiency of a Self-aminoacylating Ribozyme: Effect of the Length and Base-composition of Its 3' Extension.
From: Center for Studies in Physics and Biology, The Rockefeller University, New York, NY, 10021, USA. jlehmann@rockefeller.edu
RNA (New York, N.Y.)
- Publish Date: Aug 2007
- ISSN: 1355-8382
- Volume: 13
- Issue: 8
- Pages: 1191-7
- Medium: Print
- Language: English
- Citation (JAMA): Lehmann Jean, Reichel Amy, Buguin Axel, et al. Efficiency of a Self-aminoacylating Ribozyme: Effect of the Length and Base-composition of Its 3' Extension.. RNA Aug 2007;13:1191-7
Abstract
Variants of a previously described small self-aminoacylating ribozyme are tested in order to uncover the potentialities of a 3’ extension responsible for the esterification. The base-composition and the length of this specific part of the ribozyme are investigated. Very short extensions can still reach the active site, reflecting the small persistence length of RNA. The yield of aminoacylation is particularly high for ribozymes with extensions made up of a poly-U, for which a maximum of efficiency is observed for a total length of about 10 nucleotides. A simple model describing the behavior of this region of the ribozyme can account for the data.
Mesh Headings (Keywords): Aminoacylation, Base Composition, Binding Sites, Models, Chemical, Poly U, RNA, Catalytic
Check for Full Text / PubMed Unique Identifier (PMID): 17556712
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