Abstract
The SIN domain within histones H3 and H4 is defined by a set of single amino acid substitutions that were initially identified as mutations that alleviate the transcriptional defects associated with inactivation of the SWI/SNF chromatin remodeling complex. Here we use recombinant histones to investigate how Sin− versions of H4 alter the structure of nucleosomal arrays. We find that an R45C substitution within the SIN domain of H4 does not disrupt nucleosome positioning nor does this Sin− version alter the accessibility of nucleosomal DNA. In contrast, we find that the R45C substitution eliminates Mg2+-dependent, intramolecular folding of the nucleosomal arrays. Our results suggest that Sin− versions of histones may alleviate the need for SWI/SNF in vivo by disrupting higher-order chromatin folding.
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Acknowledgements
We would like to thank K. Luger for assistance in preparation of recombinant histones and helpful advice throughout the course of these studies, and M. Shogren-Knaak and E. Merithew for help with the preparation of Fig. 4. These studies were supported by grants from the NIH to C.L.P. and J.C.H., and a NIH NRSA to P.J.H.
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Horn, P., Crowley, K., Carruthers, L. et al. The SIN domain of the histone octamer is essential for intramolecular folding of nucleosomal arrays. Nat Struct Mol Biol 9, 167–171 (2002). https://doi.org/10.1038/nsb762
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DOI: https://doi.org/10.1038/nsb762