A trick of the tail: how electrostatics helps a DNA repair enzyme to localize on nucleosomes
Abstract
Electrostatic interactions are key to the recognition processes of proteins and DNA and have been previously documented for the action of repair enzymes. Uracil-DNA glycosylase (UDG) is the first in a sequence of enzymes that act in the base-excision repair process (BER) and whose task is the extraction of uracil bases from nuclear DNA. The question of how the molecule targets uracil bases in chromatin, in particular in the condensed protein-DNA complexes of nucleosomes, has only recently become a subject of detailed studies. Here we predict that the presence of an arginine anchor motif on the N-terminal tail of UDG can favor its localization on nucleosomes by binding to their acidic patches on their top and bottom surfaces via electrostatic interactions. We argue that this mechanism could play a key role in the detection of uracil defects in nucleosomal DNA.
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BibTeX
@article{ghediri2026trick,
title = {{A trick of the tail: how electrostatics helps a DNA repair enzyme to localize on nucleosomes}},
author = {Safwen Ghediri and Guillaume Brysbaert and Fabrizio Cleri and Ralf Blossey},
journal = {The Journal of Chemical Physics},
year = {2026},
month = oct,
doi = {10.1063/5.0344831},
url = {https://hal.science/hal-05785602v1},
note = {CC BY-NC-ND 4.0},
}
RIS
TY - JOUR
TI - A trick of the tail: how electrostatics helps a DNA repair enzyme to localize on nucleosomes
AU - Safwen Ghediri
AU - Guillaume Brysbaert
AU - Fabrizio Cleri
AU - Ralf Blossey
PY - 2026
DA - 2026/10/05
JO - The Journal of Chemical Physics
DO - 10.1063/5.0344831
UR - https://hal.science/hal-05785602v1
AB - Electrostatic interactions are key to the recognition processes of proteins and DNA and have been previously documented for the action of repair enzymes. Uracil-DNA glycosylase (UDG) is the first in a sequence of enzymes that act in the base-excision repair process (BER) and whose task is the extraction of uracil bases from nuclear DNA. The question of how the molecule targets uracil bases in chromatin, in particular in the condensed protein-DNA complexes of nucleosomes, has only recently become a subject of detailed studies. Here we predict that the presence of an arginine anchor motif on the N-terminal tail of UDG can favor its localization on nucleosomes by binding to their acidic patches on their top and bottom surfaces via electrostatic interactions. We argue that this mechanism could play a key role in the detection of uracil defects in nucleosomal DNA.
SN - 0021-9606
SN - 1089-7690
ER -