Unknown

Dataset Information

0

The poly(ADP-ribose)-dependent chromatin remodeler Alc1 induces local chromatin relaxation upon DNA damage.


ABSTRACT: Chromatin relaxation is one of the earliest cellular responses to DNA damage. However, what determines these structural changes, including their ATP requirement, is not well understood. Using live-cell imaging and laser microirradiation to induce DNA lesions, we show that the local chromatin relaxation at DNA damage sites is regulated by PARP1 enzymatic activity. We also report that H1 is mobilized at DNA damage sites, but, since this mobilization is largely independent of poly(ADP-ribosyl)ation, it cannot solely explain the chromatin relaxation. Finally, we demonstrate the involvement of Alc1, a poly(ADP-ribose)- and ATP-dependent remodeler, in the chromatin-relaxation process. Deletion of Alc1 impairs chromatin relaxation after DNA damage, while its overexpression strongly enhances relaxation. Altogether our results identify Alc1 as an important player in the fast kinetics of the NAD+- and ATP-dependent chromatin relaxation upon DNA damage in vivo.

SUBMITTER: Sellou H 

PROVIDER: S-EPMC5170603 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

The poly(ADP-ribose)-dependent chromatin remodeler Alc1 induces local chromatin relaxation upon DNA damage.

Sellou Hafida H   Lebeaupin Théo T   Chapuis Catherine C   Smith Rebecca R   Hegele Anna A   Singh Hari R HR   Kozlowski Marek M   Bultmann Sebastian S   Ladurner Andreas G AG   Timinszky Gyula G   Huet Sébastien S  

Molecular biology of the cell 20161012 24


Chromatin relaxation is one of the earliest cellular responses to DNA damage. However, what determines these structural changes, including their ATP requirement, is not well understood. Using live-cell imaging and laser microirradiation to induce DNA lesions, we show that the local chromatin relaxation at DNA damage sites is regulated by PARP1 enzymatic activity. We also report that H1 is mobilized at DNA damage sites, but, since this mobilization is largely independent of poly(ADP-ribosyl)ation  ...[more]

Similar Datasets

| S-EPMC3443743 | biostudies-literature
| S-EPMC3527939 | biostudies-literature
| S-EPMC9376112 | biostudies-literature
| S-EPMC10175808 | biostudies-literature
| S-EPMC5745148 | biostudies-literature
| S-EPMC6581741 | biostudies-literature
| S-EPMC4794993 | biostudies-literature
| S-EPMC2912421 | biostudies-literature
| S-EPMC9319841 | biostudies-literature
| S-EPMC2722505 | biostudies-literature