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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MDPI AG
2023-05-01
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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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issn | 1661-6596 1422-0067 |
language | English |
last_indexed | 2024-03-11T03:38:10Z |
publishDate | 2023-05-01 |
publisher | MDPI AG |
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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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