Unfolding of core nucleosomes by PARP-1 revealed by spFRET microscopy.

Autor: Sultanov DC; Biology Faculty, Lomonosov Moscow State University, Moscow, 119992, Russia.; Fox Chase Cancer Center, Philadelphia, PA, 19111-2497, USA., Gerasimova NS; Biology Faculty, Lomonosov Moscow State University, Moscow, 119992, Russia., Kudryashova KS; Biology Faculty, Lomonosov Moscow State University, Moscow, 119992, Russia.; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia., Maluchenko NV; Biology Faculty, Lomonosov Moscow State University, Moscow, 119992, Russia., Kotova EY; Fox Chase Cancer Center, Philadelphia, PA, 19111-2497, USA., Langelier MF; Department of Biochemistry and Molecular Medicine, Université de Montréal, 2900 Boulevard Edouard-Montpetit, Montréal, QC H3T 1J4, Canada., Pascal JM; Department of Biochemistry and Molecular Medicine, Université de Montréal, 2900 Boulevard Edouard-Montpetit, Montréal, QC H3T 1J4, Canada., Kirpichnikov MP; Fox Chase Cancer Center, Philadelphia, PA, 19111-2497, USA., Feofanov AV; Biology Faculty, Lomonosov Moscow State University, Moscow, 119992, Russia.; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry of Russian Academy of Sciences, 117997 Moscow, Russia., Studitsky VM; Biology Faculty, Lomonosov Moscow State University, Moscow, 119992, Russia.; Fox Chase Cancer Center, Philadelphia, PA, 19111-2497, USA.
Jazyk: angličtina
Zdroj: AIMS genetics [AIMS Genet] 2017; Vol. 4 (1), pp. 21-31. Date of Electronic Publication: 2017 Jan 05.
DOI: 10.3934/genet.2017.1.21
Abstrakt: DNA accessibility to various protein complexes is essential for various processes in the cell and is affected by nucleosome structure and dynamics. Protein factor PARP-1 (poly(ADP-ribose)polymerase 1) increases the accessibility of DNA in chromatin to repair proteins and transcriptional machinery, but the mechanism and extent of this chromatin reorganization are unknown. Here we report on the effects of PARP-1 on single nucleosomes revealed by spFRET (single-particle Förster Resonance Energy Transfer) microscopy. PARP-1 binding to a double-strand break in the vicinity of a nucleosome results in a significant increase of the distance between the adjacent gyres of nucleosomal DNA. This partial uncoiling of the entire nucleosomal DNA occurs without apparent loss of histones and is reversed after poly(ADP)-ribosylation of PARP-1. Thus PARP-1-nucleosome interactions result in reversible, partial uncoiling of the entire nucleosomal DNA.
Competing Interests: Conflict of interest The authors declare no competing financial interests.
Databáze: MEDLINE
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