How Poly-ADP-Ribosylation Affects the ISWI Protein
Author Information
Author(s): Sala Anna, La Rocca Gaspare, Burgio Giosalba, Kotova Elena, Di Gesù Dario, Collesano Marianna, Ingrassia Antonia M. R, Tulin Alexei V, Corona Davide F. V
Primary Institution: Istituto Telethon Dulbecco, Universita' degli Studi di Palermo
Hypothesis
Poly-ADP-ribosylation modulates the function of the nucleosome-remodeling ATPase ISWI.
Conclusion
Poly-ADP-ribosylation inhibits ISWI's ATPase activity and its ability to bind nucleosomes.
Supporting Evidence
- ISWI is a target of poly-ADP-ribosylation.
- Poly-ADP-ribosylation reduces ISWI's affinity for nucleosomes.
- Loss of PARP activity leads to increased ISWI binding to chromatin.
- ISWI misexpression causes over-PARylation of distinct chromatin components.
- PARP and ISWI have nonoverlapping chromatin binding patterns.
Takeaway
This study shows that a protein called ISWI, which helps organize DNA, can be changed by another molecule called poly-ADP-ribose, making it less effective at its job.
Methodology
The study used in vitro and in vivo experiments to analyze the interaction between ISWI and poly-ADP-ribosylation.
Digital Object Identifier (DOI)
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