Poly(ADP-Ribosyl) Code Functions

Кошкина, Д. О.; Feofanov, Аlexey V.; Studitsky, Vasily M.; Kirpichnikov, Mikhaǐl P.

doi:10.32607/actanaturae.11089

Cited by 6 publications

(10 citation statements)

References 134 publications

(166 reference statements)

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“…To support spFRET measurements (and, in part, EMSA), the nucleosomes were labeled with a donor-acceptor pair of Cy3 and Cy5 fluorophores (Figure 1a) attached to the neighboring gyres of nucleosomal DNA at the following positions: 13 and 91 bp (N p nucleosomes), 35 and 112 bp (N m nucleosomes) or 57 and 135 bp (N d nucleosomes) from the boundary of the 603 nucleosome positioning DNA sequence (23, 26). The labels placed at these positions allow efficient FRET and probing structural changes near and far from the boundary of the nucleosomal DNA (23, 26, 27). Single nucleosomes or their complexes with PARP2 freely diffusing in a solution were subjected to spFRET measurements and the data were presented as graphs describing the frequency distributions of nucleosomes by proximity ratio E PR (Figure 1b, d).…”

Section: Resultsmentioning

confidence: 99%

Zinc-dependent Nucleosome Reorganization by PARP2

Maluchenko,

Saulina,

Geraskina

et al. 2023

Preprint

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Poly(ADP-ribose)polymerase 2 (PARP2) is a nuclear protein that acts as a DNA damage sensor; it recruits the repair enzymes to a DNA damage site and facilitates formation of the repair complex. Using single particle Forster resonance energy transfer microscopy and electrophoretic mobility shift assay (EMSA) we demonstrated that PARP2 forms complexes with a nucleosome containing different number of PARP2 molecules without altering conformation of nucleosomal DNA both in the presence and in the absence of Mg2+ or Ca2+ ions. In contrast, Zn2+ ions directly interact with PARP2 inducing a local alteration of the secondary structure of the protein and PARP2-mediated, reversible structural reorganization of nucleosomal DNA. AutoPARylation activity of PARP2 is enhanced by Mg2+ ions and modulated by Zn2+ ions: suppressed or enhanced depending on the occupancy of two functionally different Zn2+ binding sites. The data suggest that Zn2+/PARP2-induced nucleosome reorganization and transient changes in the concentration of the cations could modulate PARP2 activity and the DNA damage response.

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Section: Resultsmentioning

confidence: 99%

Zinc-dependent Nucleosome Reorganization by PARP2

Maluchenko,

Saulina,

Geraskina

et al. 2023

Preprint

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“…PAR chains following laser micro-irradiation-induced DNA damage PAR chains show variable length and branching patterns [80], which can influence the number of PAR binding domains that can bind to each PAR chain. Recent findings indicate that linear PAR chains may extend to as much as 200 ADP-ribose units [21].…”

Section: Rnf146(100-182) Overexpression Modulates Par Levels and Par ...mentioning

confidence: 99%

Overexpression of the WWE domain of RNF146 modulates poly-(ADP)-ribose dynamics at sites of DNA damage

Al-Rahahleh,

Saville,

Andrews

et al. 2023

Preprint

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Protein poly-ADP-ribosylation (PARylation) is a post-translational modification formed by transfer of successive units of ADP-ribose to target proteins to form poly-ADP-ribose (PAR) chains. PAR plays a critical role in the DNA damage response (DDR) by acting as a signaling platform to promote the recruitment of DNA repair factors to the sites of DNA damage that bind via their PAR-binding domains (PBDs). Several classes of PBD families have been recognized, which identify distinct parts of the PAR chain. Proteins encoding PBDs play an essential role in conveying the PAR-mediated signal through their interaction with PAR chains, which mediates many cellular functions, including the DDR. The WWE domain identifies the iso-ADP-ribose moiety of the PAR chain. We recently described the WWE domain of RNF146 as a robust genetically encoded probe, when fused to EGFP, for detection of PAR in live cells. Here, we evaluated other PBD candidates as molecular PAR probes in live cells, including several other WWE domains and an engineered macrodomain. In addition, we demonstrate unique PAR dynamics when tracked by different PAR binding domains, a finding that that can be exploited for modulation of the PAR-dependent DNA damage response.

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“…MARylation processes are catalysed by mono(ADP-ribose) transferases (MARTs or PARP “monoenzymes”), whereas PARylation is catalysed by PARP “polyenzymes”, both of which use nicotinamide adenine dinucleotide (NAD+) as a donor of ADP-ribose for PAR (MAR) synthesis. This reaction also leads to the formation of nicotinamide as a collateral product ( Figure 1 ; [ 1 , 3 ]). The resultant ADPRylated proteins, including PARP itself and other protein targets, operate as regulators of various cellular signalling pathways.…”

Section: Introduction To Adp-ribose Metabolismmentioning

confidence: 99%

ADP-Ribosylation and Antiviral Resistance in Plants

Spechenkova

Калинина

Завриев

et al. 2023

Viruses

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ADP-ribosylation (ADPRylation) is a versatile posttranslational modification in eukaryotic cells which is involved in the regulation of a wide range of key biological processes, including DNA repair, cell signalling, programmed cell death, growth and development and responses to biotic and abiotic stresses. Members of the poly(ADP-ribosyl) polymerase (PARP) family play a central role in the process of ADPRylation. Protein targets can be modified by adding either a single ADP-ribose moiety (mono(ADP-ribosyl)ation; MARylation), which is catalysed by mono(ADP-ribosyl) transferases (MARTs or PARP “monoenzymes”), or targets may be decorated with chains of multiple ADP-ribose moieties (PARylation), via the activities of PARP “polyenzymes”. Studies have revealed crosstalk between PARylation (and to a lesser extent, MARylation) processes in plants and plant–virus interactions, suggesting that these tight links may represent a novel factor regulating plant antiviral immunity. From this perspective, we go through the literature linking PARylation-associated processes with other plant regulation pathways controlling virus resistance. Once unraveled, these links may serve as the basis of innovative strategies to improve crop resistance to viruses under challenging environmental conditions which could mitigate yield losses.

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Poly(ADP-Ribosyl) Code Functions

Cited by 6 publications

References 134 publications

Zinc-dependent Nucleosome Reorganization by PARP2

Zinc-dependent Nucleosome Reorganization by PARP2

Overexpression of the WWE domain of RNF146 modulates poly-(ADP)-ribose dynamics at sites of DNA damage

ADP-Ribosylation and Antiviral Resistance in Plants

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