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.
MeSH Terms
Antigens, Viral/chemistry,genetics,metabolism
Chromatin/chemistry,metabolism
Chromatin Assembly and Disassembly
Histones/chemistry,genetics,metabolism
Humans
Macromolecular Substances/chemistry,metabolism
Nuclear Proteins/chemistry,genetics,metabolism
Nucleic Acid Conformation
Nucleosomes/chemistry,metabolism
Peptides/chemistry,genetics,metabolism
Protein Conformation
Protein Folding
Surface Properties
Chemicals
Antigens, Viral
Chromatin
Histones
Macromolecular Substances
Nuclear Proteins
Nucleosomes
Peptides
latency-associated nuclear antigen
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Chodaparambil Jayanth V
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870, USA.
Barbera Andrew J
Lu Xu
Kaye Kenneth M
Hansen Jeffrey C
Luger Karolin
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