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Molecular and Cellular Biology, April 2008, p. 2745-2757, Vol. 28, No. 8
0270-7306/08/$08.00+0 doi:10.1128/MCB.01839-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.
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Institut für Molekularbiologie und Tumorforschung, University of Marburg, 35033 Marburg, Germany,1 Nijmegen Centre for Molecular Life Sciences, Molecular Biology Department, Radboud University, Nijmegen, The Netherlands,2 Biochemie III, University of Regensburg, 93053 Regensburg, Germany,3 GSF-Forschungszentrum, Institut für Molekulare Immunologie, 81377 München, Germany4
Received 10 October 2007/ Returned for modification 26 November 2007/ Accepted 28 January 2008
ATP-dependent chromatin remodelers of the CHD family play important roles during differentiation and development. Three CHD proteins, dMi-2, dChd1, and Kismet, have been described for Drosophila melanogaster. Here, we study dCHD3, a novel member of the CHD family. dCHD3 is related in sequence to dMi-2 but lacks several domains implicated in dMi-2 function. We demonstrate that dCHD3 is a nuclear protein and that expression is tightly regulated during fly development. Recombinant dCHD3 remodels mono- and polynucleosomes in an ATP-dependent manner in vitro. Its chromodomains are critical for nucleosome binding and remodeling. Unlike dMi-2, dCHD3 exists as a monomer. Nevertheless, both proteins colocalize with RNA polymerase II to actively transcribed regions on polytene chromosomes, suggesting that both remodelers participate in the process of transcription.
Published ahead of print on 4 February 2008.
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