Single molecule technique unveils the role of electrostatic interactions in ssDNA–gp32 molecular complex stability-Reference-Cited by-同舟云学术

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Single molecule technique unveils the role of electrostatic interactions in ssDNA–gp32 molecular complex stability

Published:2024 Issue:8 Volume:14 Page:5449-5460
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Schiopu Irina¹,Dragomir Isabela¹,Asandei Alina¹^ORCID

Affiliation:

1. The Institute of Interdisciplinary Research, Department of Exact Sciences and Natural Sciences, “Alexandru Ioan Cuza” University of Iaşi, 700506 Iasi, Romania

Abstract

A single-molecule electrophysiology assay was employed using an α-HL nanopore to test the stability of ssDNA and gp32 SSB–protein, in different salt conditions. Low salt and the presence of Zn2+ increases ssDNA–gp32 complex stability.

Funder

Unitatea Executiva pentru Finantarea Invatamantului Superior, a Cercetarii, Dezvoltarii si Inovarii

Publisher

Royal Society of Chemistry (RSC)

Link

http://pubs.rsc.org/en/content/articlepdf/2024/RA/D3RA07746B

Reference75 articles.

1. Small-molecule tools for dissecting the roles of SSB/protein interactions in genome maintenance

2. Molecular mechanism of DNA association with single-stranded DNA binding protein

3. Single-molecule FRET studies of the cooperative and non-cooperative binding kinetics of the bacteriophage T4 single-stranded DNA binding protein (gp32) to ssDNA lattices at replication fork junctions

4. Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level

5. DNA–protein π-interactions in nature: abundance, structure, composition and strength of contacts between aromatic amino acids and DNA nucleobases or deoxyribose sugar

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