Characterization of G-Quadruplexes Folding/Unfolding Dynamics and Interactions with Proteins from Single-Molecule Force Spectroscopy

G-quadruplexes (G4s) are stable secondary nucleic acid structures that play crucial roles in many fundamental biological processes. The folding/unfolding dynamics of G4 structures are associated with the replication and transcription regulation functions of G4s. However, many DNA G4 sequences can ad...

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Autores principales: Yuanlei Cheng, Yashuo Zhang, Huijuan You
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Lenguaje:EN
Publicado: MDPI AG 2021
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spelling oai:doaj.org-article:d150c29c0ef549d3bfeaee23b081bf462021-11-25T16:52:13ZCharacterization of G-Quadruplexes Folding/Unfolding Dynamics and Interactions with Proteins from Single-Molecule Force Spectroscopy10.3390/biom111115792218-273Xhttps://doaj.org/article/d150c29c0ef549d3bfeaee23b081bf462021-10-01T00:00:00Zhttps://www.mdpi.com/2218-273X/11/11/1579https://doaj.org/toc/2218-273XG-quadruplexes (G4s) are stable secondary nucleic acid structures that play crucial roles in many fundamental biological processes. The folding/unfolding dynamics of G4 structures are associated with the replication and transcription regulation functions of G4s. However, many DNA G4 sequences can adopt a variety of topologies and have complex folding/unfolding dynamics. Determining the dynamics of G4s and their regulation by proteins remains challenging due to the coexistence of multiple structures in a heterogeneous sample. Here, in this mini-review, we introduce the application of single-molecule force-spectroscopy methods, such as magnetic tweezers, optical tweezers, and atomic force microscopy, to characterize the polymorphism and folding/unfolding dynamics of G4s. We also briefly introduce recent studies using single-molecule force spectroscopy to study the molecular mechanisms of G4-interacting proteins.Yuanlei ChengYashuo ZhangHuijuan YouMDPI AGarticlesingle-molecule manipulationsG-quadruplexpolymorphismkineticsmechanical stabilityG4 helicaseMicrobiologyQR1-502ENBiomolecules, Vol 11, Iss 1579, p 1579 (2021)
institution DOAJ
collection DOAJ
language EN
topic single-molecule manipulations
G-quadruplex
polymorphism
kinetics
mechanical stability
G4 helicase
Microbiology
QR1-502
spellingShingle single-molecule manipulations
G-quadruplex
polymorphism
kinetics
mechanical stability
G4 helicase
Microbiology
QR1-502
Yuanlei Cheng
Yashuo Zhang
Huijuan You
Characterization of G-Quadruplexes Folding/Unfolding Dynamics and Interactions with Proteins from Single-Molecule Force Spectroscopy
description G-quadruplexes (G4s) are stable secondary nucleic acid structures that play crucial roles in many fundamental biological processes. The folding/unfolding dynamics of G4 structures are associated with the replication and transcription regulation functions of G4s. However, many DNA G4 sequences can adopt a variety of topologies and have complex folding/unfolding dynamics. Determining the dynamics of G4s and their regulation by proteins remains challenging due to the coexistence of multiple structures in a heterogeneous sample. Here, in this mini-review, we introduce the application of single-molecule force-spectroscopy methods, such as magnetic tweezers, optical tweezers, and atomic force microscopy, to characterize the polymorphism and folding/unfolding dynamics of G4s. We also briefly introduce recent studies using single-molecule force spectroscopy to study the molecular mechanisms of G4-interacting proteins.
format article
author Yuanlei Cheng
Yashuo Zhang
Huijuan You
author_facet Yuanlei Cheng
Yashuo Zhang
Huijuan You
author_sort Yuanlei Cheng
title Characterization of G-Quadruplexes Folding/Unfolding Dynamics and Interactions with Proteins from Single-Molecule Force Spectroscopy
title_short Characterization of G-Quadruplexes Folding/Unfolding Dynamics and Interactions with Proteins from Single-Molecule Force Spectroscopy
title_full Characterization of G-Quadruplexes Folding/Unfolding Dynamics and Interactions with Proteins from Single-Molecule Force Spectroscopy
title_fullStr Characterization of G-Quadruplexes Folding/Unfolding Dynamics and Interactions with Proteins from Single-Molecule Force Spectroscopy
title_full_unstemmed Characterization of G-Quadruplexes Folding/Unfolding Dynamics and Interactions with Proteins from Single-Molecule Force Spectroscopy
title_sort characterization of g-quadruplexes folding/unfolding dynamics and interactions with proteins from single-molecule force spectroscopy
publisher MDPI AG
publishDate 2021
url https://doaj.org/article/d150c29c0ef549d3bfeaee23b081bf46
work_keys_str_mv AT yuanleicheng characterizationofgquadruplexesfoldingunfoldingdynamicsandinteractionswithproteinsfromsinglemoleculeforcespectroscopy
AT yashuozhang characterizationofgquadruplexesfoldingunfoldingdynamicsandinteractionswithproteinsfromsinglemoleculeforcespectroscopy
AT huijuanyou characterizationofgquadruplexesfoldingunfoldingdynamicsandinteractionswithproteinsfromsinglemoleculeforcespectroscopy
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