PARP3 Affects Nucleosome Compaction Regulation

Genome compaction is one of the important subject areas for understanding the mechanisms regulating genes’ expression and DNA replication and repair. The basic unit of DNA compaction in the eukaryotic cell is the nucleosome. The main chromatin proteins responsible for DNA compaction have already bee...

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Main Authors: Alexander Ukraintsev, Mikhail Kutuzov, Ekaterina Belousova, Marie Joyeau, Victor Golyshev, Alexander Lomzov, Olga Lavrik
Format: Article
Language:English
Published: MDPI AG 2023-05-01
Series:International Journal of Molecular Sciences
Subjects:
Online Access:https://www.mdpi.com/1422-0067/24/10/9042
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author Alexander Ukraintsev
Mikhail Kutuzov
Ekaterina Belousova
Marie Joyeau
Victor Golyshev
Alexander Lomzov
Olga Lavrik
author_facet Alexander Ukraintsev
Mikhail Kutuzov
Ekaterina Belousova
Marie Joyeau
Victor Golyshev
Alexander Lomzov
Olga Lavrik
author_sort Alexander Ukraintsev
collection DOAJ
description Genome compaction is one of the important subject areas for understanding the mechanisms regulating genes’ expression and DNA replication and repair. The basic unit of DNA compaction in the eukaryotic cell is the nucleosome. The main chromatin proteins responsible for DNA compaction have already been identified, but the regulation of chromatin architecture is still extensively studied. Several authors have shown an interaction of ARTD proteins with nucleosomes and proposed that there are changes in the nucleosomes’ structure as a result. In the ARTD family, only PARP1, PARP2, and PARP3 participate in the DNA damage response. Damaged DNA stimulates activation of these PARPs, which use NAD<sup>+</sup> as a substrate. DNA repair and chromatin compaction need precise regulation with close coordination between them. In this work, we studied the interactions of these three PARPs with nucleosomes by atomic force microscopy, which is a powerful method allowing for direct measurements of geometric characteristics of single molecules. Using this method, we evaluated perturbations in the structure of single nucleosomes after the binding of a PARP. We demonstrated here that PARP3 significantly alters the geometry of nucleosomes, possibly indicating a new function of PARP3 in chromatin compaction regulation.
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spelling doaj.art-102a02fae91a4878af76e1bb600fb6df2023-11-18T01:46:23ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-05-012410904210.3390/ijms24109042PARP3 Affects Nucleosome Compaction RegulationAlexander Ukraintsev0Mikhail Kutuzov1Ekaterina Belousova2Marie Joyeau3Victor Golyshev4Alexander Lomzov5Olga Lavrik6Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, 630090 Novosibirsk, RussiaInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, 630090 Novosibirsk, RussiaInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, 630090 Novosibirsk, RussiaInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, 630090 Novosibirsk, RussiaInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, 630090 Novosibirsk, RussiaInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, 630090 Novosibirsk, RussiaInstitute of Chemical Biology and Fundamental Medicine, Siberian Branch of Russian Academy of Sciences, 630090 Novosibirsk, RussiaGenome compaction is one of the important subject areas for understanding the mechanisms regulating genes’ expression and DNA replication and repair. The basic unit of DNA compaction in the eukaryotic cell is the nucleosome. The main chromatin proteins responsible for DNA compaction have already been identified, but the regulation of chromatin architecture is still extensively studied. Several authors have shown an interaction of ARTD proteins with nucleosomes and proposed that there are changes in the nucleosomes’ structure as a result. In the ARTD family, only PARP1, PARP2, and PARP3 participate in the DNA damage response. Damaged DNA stimulates activation of these PARPs, which use NAD<sup>+</sup> as a substrate. DNA repair and chromatin compaction need precise regulation with close coordination between them. In this work, we studied the interactions of these three PARPs with nucleosomes by atomic force microscopy, which is a powerful method allowing for direct measurements of geometric characteristics of single molecules. Using this method, we evaluated perturbations in the structure of single nucleosomes after the binding of a PARP. We demonstrated here that PARP3 significantly alters the geometry of nucleosomes, possibly indicating a new function of PARP3 in chromatin compaction regulation.https://www.mdpi.com/1422-0067/24/10/9042nucleosomeatomic force microscopypoly(ADP-ribose)polymerasechromatin structureDNA compaction
spellingShingle Alexander Ukraintsev
Mikhail Kutuzov
Ekaterina Belousova
Marie Joyeau
Victor Golyshev
Alexander Lomzov
Olga Lavrik
PARP3 Affects Nucleosome Compaction Regulation
International Journal of Molecular Sciences
nucleosome
atomic force microscopy
poly(ADP-ribose)polymerase
chromatin structure
DNA compaction
title PARP3 Affects Nucleosome Compaction Regulation
title_full PARP3 Affects Nucleosome Compaction Regulation
title_fullStr PARP3 Affects Nucleosome Compaction Regulation
title_full_unstemmed PARP3 Affects Nucleosome Compaction Regulation
title_short PARP3 Affects Nucleosome Compaction Regulation
title_sort parp3 affects nucleosome compaction regulation
topic nucleosome
atomic force microscopy
poly(ADP-ribose)polymerase
chromatin structure
DNA compaction
url https://www.mdpi.com/1422-0067/24/10/9042
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