Mechanisms of Nucleosome Reorganization by PARP1

Poly(ADP-ribose) polymerase 1 (PARP1) is an enzyme involved in DNA repair, chromatin organization and transcription. During transcription initiation, PARP1 interacts with gene promoters where it binds to nucleosomes, replaces linker histone H1 and participates in gene regulation. However, the mechan...

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Autores principales:	Natalya V. Maluchenko, Dmitry K. Nilov, Sergey V. Pushkarev, Elena Y. Kotova, Nadezhda S. Gerasimova, Mikhail P. Kirpichnikov, Marie-France Langelier, John M. Pascal, Md. Sohail Akhtar, Alexey V. Feofanov, Vasily M. Studitsky
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	nucleosome poly(ADP-ribose) polymerase 1 spFRET microscopy molecular dynamics Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/0f2f4ab1755440bd8cc0c4ed3e76e9ad
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spelling	oai:doaj.org-article:0f2f4ab1755440bd8cc0c4ed3e76e9ad2021-11-25T17:53:37ZMechanisms of Nucleosome Reorganization by PARP110.3390/ijms2222121271422-00671661-6596https://doaj.org/article/0f2f4ab1755440bd8cc0c4ed3e76e9ad2021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12127https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Poly(ADP-ribose) polymerase 1 (PARP1) is an enzyme involved in DNA repair, chromatin organization and transcription. During transcription initiation, PARP1 interacts with gene promoters where it binds to nucleosomes, replaces linker histone H1 and participates in gene regulation. However, the mechanisms of PARP1-nucleosome interaction remain unknown. Here, using spFRET microscopy, molecular dynamics and biochemical approaches we identified several different PARP1-nucleosome complexes and two types of PARP1 binding to mononucleosomes: at DNA ends and end-independent. Two or three molecules of PARP1 can bind to a nucleosome depending on the presence of linker DNA and can induce reorganization of the entire nucleosome that is independent of catalytic activity of PARP1. Nucleosome reorganization depends upon binding of PARP1 to nucleosomal DNA, likely near the binding site of linker histone H1. The data suggest that PARP1 can induce the formation of an alternative nucleosome state that is likely involved in gene regulation and DNA repair.Natalya V. MaluchenkoDmitry K. NilovSergey V. PushkarevElena Y. KotovaNadezhda S. GerasimovaMikhail P. KirpichnikovMarie-France LangelierJohn M. PascalMd. Sohail AkhtarAlexey V. FeofanovVasily M. StuditskyMDPI AGarticlenucleosomepoly(ADP-ribose) polymerase 1spFRET microscopymolecular dynamicsBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12127, p 12127 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	nucleosome poly(ADP-ribose) polymerase 1 spFRET microscopy molecular dynamics Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	nucleosome poly(ADP-ribose) polymerase 1 spFRET microscopy molecular dynamics Biology (General) QH301-705.5 Chemistry QD1-999 Natalya V. Maluchenko Dmitry K. Nilov Sergey V. Pushkarev Elena Y. Kotova Nadezhda S. Gerasimova Mikhail P. Kirpichnikov Marie-France Langelier John M. Pascal Md. Sohail Akhtar Alexey V. Feofanov Vasily M. Studitsky Mechanisms of Nucleosome Reorganization by PARP1
description	Poly(ADP-ribose) polymerase 1 (PARP1) is an enzyme involved in DNA repair, chromatin organization and transcription. During transcription initiation, PARP1 interacts with gene promoters where it binds to nucleosomes, replaces linker histone H1 and participates in gene regulation. However, the mechanisms of PARP1-nucleosome interaction remain unknown. Here, using spFRET microscopy, molecular dynamics and biochemical approaches we identified several different PARP1-nucleosome complexes and two types of PARP1 binding to mononucleosomes: at DNA ends and end-independent. Two or three molecules of PARP1 can bind to a nucleosome depending on the presence of linker DNA and can induce reorganization of the entire nucleosome that is independent of catalytic activity of PARP1. Nucleosome reorganization depends upon binding of PARP1 to nucleosomal DNA, likely near the binding site of linker histone H1. The data suggest that PARP1 can induce the formation of an alternative nucleosome state that is likely involved in gene regulation and DNA repair.
format	article
author	Natalya V. Maluchenko Dmitry K. Nilov Sergey V. Pushkarev Elena Y. Kotova Nadezhda S. Gerasimova Mikhail P. Kirpichnikov Marie-France Langelier John M. Pascal Md. Sohail Akhtar Alexey V. Feofanov Vasily M. Studitsky
author_facet	Natalya V. Maluchenko Dmitry K. Nilov Sergey V. Pushkarev Elena Y. Kotova Nadezhda S. Gerasimova Mikhail P. Kirpichnikov Marie-France Langelier John M. Pascal Md. Sohail Akhtar Alexey V. Feofanov Vasily M. Studitsky
author_sort	Natalya V. Maluchenko
title	Mechanisms of Nucleosome Reorganization by PARP1
title_short	Mechanisms of Nucleosome Reorganization by PARP1
title_full	Mechanisms of Nucleosome Reorganization by PARP1
title_fullStr	Mechanisms of Nucleosome Reorganization by PARP1
title_full_unstemmed	Mechanisms of Nucleosome Reorganization by PARP1
title_sort	mechanisms of nucleosome reorganization by parp1
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/0f2f4ab1755440bd8cc0c4ed3e76e9ad
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_version_	1718411845317951488

Mechanisms of Nucleosome Reorganization by PARP1

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