A charged and contoured surface on the nucleosome regulates chromatin compaction.
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.
Chodaparambil
Jayanth V
JV
Department of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, Colorado 80523-1870, USA.
Barbera
Andrew J
AJ
Lu
Xu
X
Kaye
Kenneth M
KM
Hansen
Jeffrey C
JC
Luger
Karolin
K
D000956:Antigens, Viral / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002843:Chromatin / Q000737:chemistry / Q000378:metabolism; D042002:Chromatin Assembly and Disassembly; D006657:Histones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D006801:Humans; D046911:Macromolecular Substances / Q000737:chemistry / Q000378:metabolism; D009687:Nuclear Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009690:Nucleic Acid Conformation; D009707:Nucleosomes / Q000737:chemistry* / Q000378:metabolism; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D013499:Surface Properties
D000956:Antigens, Viral; D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances; D009687:Nuclear Proteins; D009707:Nucleosomes; D010455:Peptides; C109540:latency-associated nuclear antigen