Biochemical and Structural Studies of the Enzymes Involved in RNA Cleavage and Modification
type: CreativeWork
description: Part IV: Cleavage of 16S rRNA. Colicin E3 is a highly specific endonuclease that cleaves a single bond in 16S rRNA between A1493 and G1494. This cleavage results in termination of protein synthesis in the cell. In order to determine whether the nucleotide sequence of the target site accounts for colicin E3's specificity, we tested the activity of colicin E3 on short, synthetic double-stranded RNAs that have both identical and modified sequences of the target section of the rRNA. In addition, we tested the activity of the nuclease domain of colicin E3 on ribosomes. The results indicate that the nuclease domain of colicin E3 alone cleaves the short double stranded RNAs non-specifically, while it does not cleave the A1493-G1494 bond in rRNA of purified ribosomes.
abstract: Part IV: Cleavage of 16S rRNA. Colicin E3 is a highly specific endonuclease that cleaves a single bond in 16S rRNA between A1493 and G1494. This cleavage results in termination of protein synthesis in the cell. In order to determine whether the nucleotide sequence of the target site accounts for colicin E3's specificity, we tested the activity of colicin E3 on short, synthetic double-stranded RNAs that have both identical and modified sequences of the target section of the rRNA. In addition, we tested the activity of the nuclease domain of colicin E3 on ribosomes. The results indicate that the nuclease domain of colicin E3 alone cleaves the short double stranded RNAs non-specifically, while it does not cleave the A1493-G1494 bond in rRNA of purified ribosomes.
author: Cicmil, Nenad
language: eng
keywords: Chemistry, Biochemistry
date published: 2015-09-25T22:28:11Z
date modified: 2026-07-22T22:26:24Z
provider: University of Illinois - Urbana-Champaign
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Illinois at Urbana-Champaign

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2142/84850