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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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) |
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single-molecule manipulations G-quadruplex polymorphism kinetics mechanical stability G4 helicase Microbiology QR1-502 |
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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 |
_version_ |
1718412925862936576 |