A charged and contoured surface on the nucleosome regulates chromatin compaction. Journal Article uri icon

Overview

abstract

  • Local nucleosome-nucleosome interactions in cis drive chromatin folding, whereas interactions in trans lead to fiber-fiber oligomerization. Here we show that peptides derived from the histone H4 tail and Kaposi's sarcoma herpesvirus LANA protein can replace the endogenous H4 tail, resulting in array folding and oligomerization. Neutralization of a LANA binding site on the histone surface enhanced rather than abolished nucleosome-nucleosome interactions. We maintain that the contoured nucleosome surface is centrally involved in regulating chromatin condensation.

publication date

  • November 1, 2007

Full Author List

  • Chodaparambil JV; Barbera AJ; Lu X; Kaye KM; Hansen JC; Luger K

Other Profiles

Additional Document Info

start page

  • 1105

end page

  • 1107

volume

  • 14

issue

  • 11