Deacetylase activity associates with topoisomerase II and is necessary for etoposide-induced apoptosis

Johnson, Colin, Padget, Kay, Austin, Caroline and Turner, Bryan (2001) Deacetylase activity associates with topoisomerase II and is necessary for etoposide-induced apoptosis. The Journal of Biological Chemistry, 276 (7). pp. 4539-42. ISSN 0021-9258

Full text not available from this repository.
Official URL: http://doi.org/10.1074/jbc.C000824200

Abstract

DNA topoisomerase II (topo II) is a ubiquitous nuclear enzyme that is involved in DNA replication, transcription, chromosome segregation, and apoptosis. Here we show by immunoprecipitation, pull down with glutathione S-transferase fusion proteins, and yeast two-hybrid analysis that both topo IIalpha and -beta physically interact with the histone deacetylase HDAC1. The in vitro DNA decatenation activity of recombinant topo IIalpha and -beta is inhibited by association with catalytically inactive, recombinant HDAC1. We provide evidence for the in vivo significance of the topo II-HDAC1 association, showing that inhibition of HDAC activity with trichostatin A suppresses apoptosis induced by the topo II poison etoposide, but not by the topoisomerase I inhibitor camptothecin. We suggest that chromatin remodeling by an HDAC-containing complex facilitates both topo II-catalyzed DNA rearrangement and etoposide-induced DNA damage in vivo.

Item Type: Article
Subjects: C700 Molecular Biology, Biophysics and Biochemistry
Department: Faculties > Health and Life Sciences > Applied Sciences
Depositing User: Kay Padget
Date Deposited: 09 Jul 2018 14:59
Last Modified: 09 Jul 2018 14:59
URI: http://nrl.northumbria.ac.uk/id/eprint/34542

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