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A charged and contoured surface on the nucleosome regulates chromatin compaction.

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.

SUBMITTER: Chodaparambil JV

PROVIDER: S-EPMC2366819 | biostudies-literature | 2007 Nov

REPOSITORIES: biostudies-literature

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A charged and contoured surface on the nucleosome regulates chromatin compaction.

Chodaparambil Jayanth V JV Barbera Andrew J AJ Lu Xu X Kaye Kenneth M KM Hansen Jeffrey C JC Luger Karolin K

Nature structural & molecular biology 20071028 11

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 ...[more]

PMID: 17965723

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