Human topoisomerase II-DNA interaction study by using atomic force microscopy.

Détails

ID Serval
serval:BIB_389D85809F23
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Human topoisomerase II-DNA interaction study by using atomic force microscopy.
Périodique
FEBS Letters
Auteur⸱e⸱s
Alonso-Sarduy L., Roduit C., Dietler G., Kasas S.
ISSN
1873-3468 (Electronic)
ISSN-L
0014-5793
Statut éditorial
Publié
Date de publication
2011
Volume
585
Numéro
19
Pages
3139-3145
Langue
anglais
Résumé
Type II topoisomerases (Topo II) are unique enzymes that change the DNA topology by catalyzing the passage of two double-strands across each other by using the energy from ATP hydrolysis. In vitro, human Topo II relaxes positive supercoiled DNA around 10-fold faster than negative supercoiled DNA. By using atomic force microscopy (AFM) we found that human Topo II binds preferentially to DNA cross-overs. Around 50% of the DNA crossings, where Topo II was bound to, presented an angle in the range of 80-90°, suggesting a favored binding geometry in the chiral discrimination by Topo II. Our studies with AFM also helped us visualize the dynamics of the unknotting action of Topo II in knotted molecules.
Mots-clé
DNA/chemistry, DNA/metabolism, DNA Topoisomerases, Type II/chemistry, DNA Topoisomerases, Type II/metabolism, Humans, Microscopy, Atomic Force, Nucleic Acid Conformation, Protein Binding, Protein Conformation
Pubmed
Web of science
Open Access
Oui
Création de la notice
03/11/2011 10:26
Dernière modification de la notice
20/08/2019 14:27
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