Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-7670
Nat Struct Biol 2002 Mar 01;93:167-71. doi: 10.1038/nsb762.
Show Gene links Show Anatomy links

The SIN domain of the histone octamer is essential for intramolecular folding of nucleosomal arrays.

Horn PJ, Crowley KA, Carruthers LM, Hansen JC, Peterson CL.


???displayArticle.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.

???displayArticle.pubmedLink??? 11836537
???displayArticle.link??? Nat Struct Biol
???displayArticle.grants??? [+]


References :
Hayes, Changing chromatin from the inside. 2002, Pubmed