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Molecular and Cellular Biology, February 2006, p. 1518-1526, Vol. 26, No. 4
0270-7306/06/$08.00+0 doi:10.1128/MCB.26.4.1518-1526.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Institut Albert Bonniot, INSERM U309, 38706 La Tronche Cedex, France,1 Ecole Normale Supérieure de Lyon, Laboratoire Joliot Curie, 46 Allée d'Italie, 69007 Lyon, France,2 Institut Andre Lwoff, CNRS UPR 9079, 7 rue Guy Moquet, 94800 Villejuif, France,3 Ecole Normale Supérieure de Lyon, LBMC, CNRS-UMR 5161, 46 Allée d'Italie, 69007 Lyon, France4
Received 12 September 2005/ Returned for modification 14 October 2005/ Accepted 21 November 2005
We have studied the functional and structural properties of nucleosomes reconstituted with H2BFWT, a recently identified putative histone variant of the H2B family with totally unknown function. We show that H2BFWT can replace the conventional histone H2B in the nucleosome. The presence of H2BFWT did not affect the overall structure of the nucleosome, and the H2BFWT nucleosomes exhibited the same stability as conventional nucleosomes. SWI/SNF was able to efficiently remodel and mobilize the H2BFWT nucleosomes. Importantly, H2BFWT, in contrast to conventional H2B, was unable to recruit chromosome condensation factors and to participate in the assembly of mitotic chromosomes. This was determined by the highly divergent (compared to conventional H2B) NH2 tail of H2BFWT. These data, in combination with the observations that H2BFWT was found by others in the sperm nuclei and appeared to be associated with the telomeric chromatin, suggest that H2BFWT could act as a specific epigenetic marker.
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