Mechanisms of nucleosome reorganization by PARP1

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

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

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.

Original languageEnglish
Article number12127
JournalInternational Journal of Molecular Sciences
Volume22
Issue number22
DOIs
StatePublished - Nov 1 2021

Keywords

  • Molecular dynamics
  • Nucleosome
  • Poly(ADP‐ribose) polymerase 1
  • SpFRET microscopy

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