The 5'-AG5 CC-3' Fragment from the Human CPEB3 Ribozyme Forms an Ultrastable Parallel RNA G-Quadruplex

Katharina Kulikov; Senada Nozinovic; Stephanie Kath-Schorr

doi:10.1002/cbic.201700028

The 5'-AG₅ CC-3' Fragment from the Human CPEB3 Ribozyme Forms an Ultrastable Parallel RNA G-Quadruplex

Chembiochem. 2017 Jun 1;18(11):969-973. doi: 10.1002/cbic.201700028. Epub 2017 Apr 11.

Authors

Katharina Kulikov¹, Senada Nozinovic², Stephanie Kath-Schorr¹

Affiliations

¹ LIMES Institute, Chemical Biology & Medicinal Chemistry Unit, University of Bonn, Gerhard-Domagk-Strasse 1, 53121, Bonn, Germany.
² Institute for Inorganic Chemistry, University of Bonn, Gerhard-Domagk-Strasse 1, 53121, Bonn, Germany.

PMID: 28296179
DOI: 10.1002/cbic.201700028

Abstract

An unusually thermostable G-quadruplex is formed by a sequence fragment of a naturally occurring ribozyme, the human CPEB3 ribozyme. Strong evidence is provided for the formation of a uniquely stable intermolecular G-quadruplex structure consisting of five tetrad layers, by using CD spectroscopy, UV melting curves, 2D NMR spectroscopy, and gel shift analysis. The cationic porphyrin TMPyP4 destabilizes the complex.

Keywords: CPEB3 ribozyme; G-quadruplexes; RNA; RNA structures; circular dichroism.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Chemistry Techniques, Analytical
G-Quadruplexes*
Humans
Molecular Structure
Porphyrins / pharmacology
RNA / chemistry
RNA Stability / drug effects
RNA, Catalytic / chemistry*
RNA-Binding Proteins / chemistry*

Substances

CPEB3 protein, human
Porphyrins
RNA, Catalytic
RNA-Binding Proteins
tetra(4-N-methylpyridyl)porphine
RNA