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Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

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Published on: April 4, 2025

The hTERT core promoter forms three parallel G-quadruplexes.

Robert C Monsen¹, Lynn DeLeeuw², William L Dean²

¹Department of Biochemistry & Molecular Genetics, University of Louisville, Louisville, KY 40202, USA.

Nucleic Acids Research

|February 22, 2020

Summary

This summary is machine-generated.

The human telomerase reverse transcriptase (hTERT) promoter G-quadruplex structure is clarified. Our study confirms it forms a three-parallel G-quadruplex, not a hairpin structure, using integrated biophysical and biochemical methods.

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Area of Science:

Structural biology
Biophysics
Molecular genetics

Background:

The G-quadruplex forming potential within the human telomerase reverse transcriptase (hTERT) promoter is a subject of structural debate.
Two proposed models include a three-parallel G-quadruplex structure or a duplex hairpin adjacent to parallel and antiparallel quadruplexes.

Purpose of the Study:

To definitively distinguish between the proposed structural models for the hTERT promoter G-quadruplex.
To elucidate the precise solution structure of the wild-type hTERT core promoter sequence.

Main Methods:

Integrated structural biology approach utilizing circular dichroism, thermal denaturation, and nuclear magnetic resonance spectroscopy.
Biophysical characterization including analytical ultracentrifugation and small-angle X-ray scattering.
Computational modeling via molecular dynamics simulations and experimental validation with DNase I cleavage assays.

Main Results:

Experimental data, including biophysical and biochemical properties, were inconsistent with a hairpin model for the wild-type hTERT sequence.
The wild-type hTERT core promoter was determined to fold into a compact, stacked, three-parallel G-quadruplex structure.
Molecular dynamics simulations accurately predicted experimental hydrodynamic properties for both proposed structures.

Conclusions:

The wild-type hTERT promoter sequence definitively does not form a hairpin structure in solution.
The predominant conformation adopted by the wild-type hTERT promoter is a stacked three-parallel G-quadruplex structure.