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RESEARCH PRODUCT
The nucleosome-remodeling ATPase ISWI is regulated by poly-ADP-ribosylation.
Davide CoronaGiosalba BurgioAnna SalaCollesano MAntonia M. R. IngrassiaDario Di GesùGaspare La RoccaElena KotovaAlexei V. Tulinsubject
Poly Adenosine Diphosphate RiboseImmunoprecipitationQH301-705.5Poly ADP ribose polymeraseATPaseBlotting WesternBiochemistryChromosomesGeneral Biochemistry Genetics and Molecular BiologySettore BIO/10 - BiochimicaAnimalsDrosophila ProteinsImmunoprecipitationNucleosomeBiology (General)Transcription factorIn Situ Hybridization FluorescencePolymeraseAdenosine TriphosphatasesGeneral Immunology and MicrobiologybiologyGeneral NeuroscienceGenetics and GenomicsPARP ISWI Poly(ADP)ribosylation Chromatin remodellingCell BiologyChromatinISWI PARPNucleosomesChromatinSettore BIO/18 - GeneticaDrosophila melanogasterBiochemistrybiology.proteinPoly(ADP-ribose) PolymerasesGeneral Agricultural and Biological SciencesFunction (biology)Transcription FactorsResearch Articledescription
ATP-dependent nucleosome-remodeling enzymes and covalent modifiers of chromatin set the functional state of chromatin. However, how these enzymatic activities are coordinated in the nucleus is largely unknown. We found that the evolutionary conserved nucleosome-remodeling ATPase ISWI and the poly-ADP-ribose polymerase PARP genetically interact. We present evidence showing that ISWI is target of poly-ADP-ribosylation. Poly-ADP-ribosylation counteracts ISWI function in vitro and in vivo. Our work suggests that ISWI is a physiological target of PARP and that poly-ADP-ribosylation can be a new, important post-translational modification regulating the activity of ATP-dependent nucleosome remodelers.
year | journal | country | edition | language |
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2008-10-01 | PLoS Biology |