Resveratrol Inhibits Nucleosome Binding and Catalytic Activity of PARP1

The natural polyphenol resveratrol is a biologically active compound that interacts with DNA and affects the activity of some nuclear enzymes. Its effect on the interaction between nucleosomes and poly(ADP-ribose) polymerase-1 (PARP1) and on the catalytic activity of PARP1 was studied using Western...

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Main Authors: Daria O. Koshkina, Natalya V. Maluchenko, Anna N. Korovina, Angelina A. Lobanova, Alexey V. Feofanov, Vasily M. Studitsky
Format: Article
Language:English
Published: MDPI AG 2024-11-01
Series:Biomolecules
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Online Access:https://www.mdpi.com/2218-273X/14/11/1398
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author Daria O. Koshkina
Natalya V. Maluchenko
Anna N. Korovina
Angelina A. Lobanova
Alexey V. Feofanov
Vasily M. Studitsky
author_facet Daria O. Koshkina
Natalya V. Maluchenko
Anna N. Korovina
Angelina A. Lobanova
Alexey V. Feofanov
Vasily M. Studitsky
author_sort Daria O. Koshkina
collection DOAJ
description The natural polyphenol resveratrol is a biologically active compound that interacts with DNA and affects the activity of some nuclear enzymes. Its effect on the interaction between nucleosomes and poly(ADP-ribose) polymerase-1 (PARP1) and on the catalytic activity of PARP1 was studied using Western blotting, spectrophotometry, electrophoretic mobility shift assay, and single particle Förster resonance energy transfer microscopy. Resveratrol inhibited PARP1 activity at micro- and sub-micromolar concentrations, but the inhibitory effect decreased at higher concentrations due to the aggregation of the polyphenol. The inhibition of PARP1 by resveratrol was accompanied by its binding to the enzyme catalytic center and a subsequent decrease in PARP1 affinity to nucleosomal DNA. Concurrent binding of talazoparib to the substrate binding pocket of PARP1, which occurs in the presence of resveratrol, restores the interaction of PARP1 with nucleosomes, suggesting that the binding sites of resveratrol and talazoparib overlap. The data suggest that resveratrol can be classified as a natural inhibitor of PARP1.
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issn 2218-273X
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series Biomolecules
spelling doaj-art-ce06b557d6d24b248cc3d7ae7cb7bb082025-08-20T03:11:10ZengMDPI AGBiomolecules2218-273X2024-11-011411139810.3390/biom14111398Resveratrol Inhibits Nucleosome Binding and Catalytic Activity of PARP1Daria O. Koshkina0Natalya V. Maluchenko1Anna N. Korovina2Angelina A. Lobanova3Alexey V. Feofanov4Vasily M. Studitsky5Department of Bioengineering, Faculty of Biology, Lomonosov Moscow State University, 12, Leninskie Gory, Moscow 119234, RussiaDepartment of Bioengineering, Faculty of Biology, Lomonosov Moscow State University, 12, Leninskie Gory, Moscow 119234, RussiaDepartment of Bioengineering, Faculty of Biology, Lomonosov Moscow State University, 12, Leninskie Gory, Moscow 119234, RussiaDepartment of Bioengineering, Faculty of Biology, Lomonosov Moscow State University, 12, Leninskie Gory, Moscow 119234, RussiaDepartment of Bioengineering, Faculty of Biology, Lomonosov Moscow State University, 12, Leninskie Gory, Moscow 119234, RussiaDepartment of Bioengineering, Faculty of Biology, Lomonosov Moscow State University, 12, Leninskie Gory, Moscow 119234, RussiaThe natural polyphenol resveratrol is a biologically active compound that interacts with DNA and affects the activity of some nuclear enzymes. Its effect on the interaction between nucleosomes and poly(ADP-ribose) polymerase-1 (PARP1) and on the catalytic activity of PARP1 was studied using Western blotting, spectrophotometry, electrophoretic mobility shift assay, and single particle Förster resonance energy transfer microscopy. Resveratrol inhibited PARP1 activity at micro- and sub-micromolar concentrations, but the inhibitory effect decreased at higher concentrations due to the aggregation of the polyphenol. The inhibition of PARP1 by resveratrol was accompanied by its binding to the enzyme catalytic center and a subsequent decrease in PARP1 affinity to nucleosomal DNA. Concurrent binding of talazoparib to the substrate binding pocket of PARP1, which occurs in the presence of resveratrol, restores the interaction of PARP1 with nucleosomes, suggesting that the binding sites of resveratrol and talazoparib overlap. The data suggest that resveratrol can be classified as a natural inhibitor of PARP1.https://www.mdpi.com/2218-273X/14/11/1398poly(ADP-ribose) polymerase-1PARP1nucleosomeresveratrolspFRETWestern blotting
spellingShingle Daria O. Koshkina
Natalya V. Maluchenko
Anna N. Korovina
Angelina A. Lobanova
Alexey V. Feofanov
Vasily M. Studitsky
Resveratrol Inhibits Nucleosome Binding and Catalytic Activity of PARP1
Biomolecules
poly(ADP-ribose) polymerase-1
PARP1
nucleosome
resveratrol
spFRET
Western blotting
title Resveratrol Inhibits Nucleosome Binding and Catalytic Activity of PARP1
title_full Resveratrol Inhibits Nucleosome Binding and Catalytic Activity of PARP1
title_fullStr Resveratrol Inhibits Nucleosome Binding and Catalytic Activity of PARP1
title_full_unstemmed Resveratrol Inhibits Nucleosome Binding and Catalytic Activity of PARP1
title_short Resveratrol Inhibits Nucleosome Binding and Catalytic Activity of PARP1
title_sort resveratrol inhibits nucleosome binding and catalytic activity of parp1
topic poly(ADP-ribose) polymerase-1
PARP1
nucleosome
resveratrol
spFRET
Western blotting
url https://www.mdpi.com/2218-273X/14/11/1398
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